ID ABCA4_HUMAN Reviewed; 2273 AA. AC P78363; O15112; O60438; O60915; Q0QD48; Q4LE31; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 3. DT 27-MAR-2024, entry version 219. DE RecName: Full=Retinal-specific phospholipid-transporting ATPase ABCA4 {ECO:0000305}; DE EC=7.6.2.1 {ECO:0000269|PubMed:24097981}; DE AltName: Full=ATP-binding cassette sub-family A member 4; DE AltName: Full=RIM ABC transporter; DE Short=RIM proteinv; DE Short=RmP; DE AltName: Full=Retinal-specific ATP-binding cassette transporter; DE AltName: Full=Stargardt disease protein; GN Name=ABCA4 {ECO:0000312|HGNC:HGNC:34}; GN Synonyms=ABCR {ECO:0000303|PubMed:9054934}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], VARIANTS STGD1, AND VARIANTS HIS-846; GLN-943 RP AND ASP-1817. RX PubMed=9054934; DOI=10.1038/ng0397-236; RA Allikmets R., Singh N., Sun H., Shroyer N.F., Hutchinson A., RA Chidambaram A., Gerrard B., Baird L., Stauffer D., Peiffer A., Rattner A., RA Smallwood P.M., Li Y., Anderson K.L., Lewis R.A., Nathans J., Leppert M., RA Dean M., Lupski J.R.; RT "A photoreceptor cell-specific ATP-binding transporter gene (ABCR) is RT mutated in recessive Stargardt macular dystrophy."; RL Nat. Genet. 15:236-246(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=9202155; DOI=10.1016/s0014-5793(97)00517-6; RA Azarian S.M., Travis G.H.; RT "The photoreceptor rim protein is an ABC transporter encoded by the gene RT for recessive Stargardt's disease (ABCR)."; RL FEBS Lett. 409:247-252(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS STGD1 TRP-18 AND CYS-212, AND RP VARIANT ASP-1817. RX PubMed=9503029; DOI=10.1006/geno.1997.5164; RA Gerber S., Rozet J.-M., van de Pol T.J.R., Hoyng C.B., Munnich A., RA Blankenagel A., Kaplan J., Cremers F.P.M.; RT "Complete exon-intron structure of the retina-specific ATP binding RT transporter gene (ABCR) allows the identification of novel mutations RT underlying Stargardt disease."; RL Genomics 48:139-142(1998). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS STGD1. RX PubMed=9490294; DOI=10.1007/s004390050649; RA Nasonkin I., Illing M., Koehler M.R., Schmid M., Molday R.S., Weber B.H.F.; RT "Mapping of the rod photoreceptor ABC transporter (ABCR) to 1p21-p22.1 and RT identification of novel mutations in Stargardt's disease."; RL Hum. Genet. 102:21-26(1998). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-943. RC TISSUE=Brain; RA Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., RA Okazaki N., Koga H., Nagase T., Ohara O.; RT "Preparation of a set of expression-ready clones of mammalian long cDNAs RT encoding large proteins by the ORF trap cloning method."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-29. RC TISSUE=Retina; RX PubMed=17286855; DOI=10.1186/1471-2164-8-42; RA Roni V., Carpio R., Wissinger B.; RT "Mapping of transcription start sites of human retina expressed genes."; RL BMC Genomics 8:42-42(2007). RN [8] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=10075733; DOI=10.1074/jbc.274.12.8269; RA Sun H., Molday R.S., Nathans J.; RT "Retinal stimulates ATP hydrolysis by purified and reconstituted ABCR, the RT photoreceptor-specific ATP-binding cassette transporter responsible for RT Stargardt disease."; RL J. Biol. Chem. 274:8269-8281(1999). RN [9] RP INVOLVEMENT IN RP19. RX PubMed=9466990; DOI=10.1093/hmg/7.3.355; RA Cremers F.P.M., van de Pol D.J.R., van Driel M.A., den Hollander A.I., RA van Haren F.J.J., Knoers N.V.A.M., Tijmes N., Bergen A.A.B., RA Rohrschneider K., Blankenagel A., Pinckers A.J.L.G., Deutman A.F., RA Hoyng C.B.; RT "Autosomal recessive retinitis pigmentosa and cone-rod dystrophy caused by RT splice site mutations in the Stargardt's disease gene ABCR."; RL Hum. Mol. Genet. 7:355-362(1998). RN [10] RP MEMBRANE TOPOLOGY, AND GLYCOSYLATION AT ASN-98; ASN-415; ASN-444; ASN-504; RP ASN-1469; ASN-1529; ASN-1588 AND ASN-1662. RX PubMed=11320094; DOI=10.1074/jbc.m101902200; RA Bungert S., Molday L.L., Molday R.S.; RT "Membrane topology of the ATP binding cassette transporter ABCR and its RT relationship to ABC1 and related ABCA transporters: identification of N- RT linked glycosylation sites."; RL J. Biol. Chem. 276:23539-23546(2001). RN [11] RP DOMAIN, FUNCTION, VARIANTS STGD1 LEU-1408; HIS-1443 AND ARG-1488, AND RP CHARACTERIZATION OF VARIANTS STGD1 LEU-1408; HIS-1443 AND ARG-1488. RX PubMed=20404325; DOI=10.1074/jbc.m110.112896; RA Biswas-Fiss E.E., Kurpad D.S., Joshi K., Biswas S.B.; RT "Interaction of extracellular domain 2 of the human retina-specific ATP- RT binding cassette transporter (ABCA4) with all-trans-retinal."; RL J. Biol. Chem. 285:19372-19383(2010). RN [12] RP DOMAIN, FUNCTION, VARIANT STGD1 ALA-863, CHARACTERIZATION OF VARIANT STGD1 RP ALA-863, MUTAGENESIS OF PRO-940, AND VARIANT GLN-943. RX PubMed=23144455; DOI=10.1074/jbc.m112.409623; RA Biswas-Fiss E.E., Affet S., Ha M., Biswas S.B.; RT "Retinoid binding properties of nucleotide binding domain 1 of the RT Stargardt disease-associated ATP binding cassette (ABC) transporter, RT ABCA4."; RL J. Biol. Chem. 287:44097-44107(2012). RN [13] RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-969 AND LYS-1978, VARIANTS RP STGD1 ALA-863 AND SER-965, AND CHARACTERIZATION OF VARIANTS STGD1 ALA-863 RP AND SER-965. RX PubMed=22735453; DOI=10.1038/ncomms1927; RA Quazi F., Lenevich S., Molday R.S.; RT "ABCA4 is an N-retinylidene-phosphatidylethanolamine and RT phosphatidylethanolamine importer."; RL Nat. Commun. 3:925-925(2012). RN [14] RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, FUNCTION, SUBCELLULAR LOCATION, RP VARIANTS STGD1 PRO-100; ILE-608; ILE-959; SER-965 AND MET-1537, RP CHARACTERIZATION OF VARIANTS STGD1 PRO-100; ILE-608; ILE-959; SER-965 AND RP MET-1537, AND MUTAGENESIS OF CYS-1502; ARG-2107 AND PRO-2180. RX PubMed=24097981; DOI=10.1074/jbc.m113.508812; RA Quazi F., Molday R.S.; RT "Differential phospholipid substrates and directional transport by ATP- RT binding cassette proteins ABCA1, ABCA7, and ABCA4 and disease-causing RT mutants."; RL J. Biol. Chem. 288:34414-34426(2013). RN [15] RP REGION. RX PubMed=31481235; DOI=10.1016/j.bbrc.2019.08.121; RA Patel M.J., Biswas S.B., Biswas-Fiss E.E.; RT "Functional significance of the conserved C-Terminal VFVNFA motif in the RT retina-specific ABC transporter, ABCA4, and its role in inherited visual RT disease."; RL Biochem. Biophys. Res. Commun. 519:46-52(2019). RN [16] RP STRUCTURE BY ELECTRON MICROSCOPY (3.27 ANGSTROMS) IN COMPLEX WITH ATP, RP MUTAGENESIS OF GLU-1087 AND GLU-2096, BIOPHYSICOCHEMICAL PROPERTIES, RP DISULFIDE BOND, GLYCOSYLATION AT ASN-98; ASN-415; ASN-444; ASN-504; RP ASN-1469; ASN-1529; ASN-1588 AND ASN-1662, AND ATP BINDING SITE. RX PubMed=33605212; DOI=10.7554/elife.63524; RA Liu F., Lee J., Chen J.; RT "Molecular structures of the eukaryotic retinal importer ABCA4."; RL Elife 10:0-0(2021). RN [17] RP REVIEW, VARIANTS ARMD2 LYS-471; LEU-1129; SER-1517; THR-1562; ARG-1578; RP HIS-1898; PHE-1970 AND ASN-2177, AND VARIANTS GLY-643; HIS-846; ALA-863; RP GLN-943; MET-1428; GLU-1961 AND ILE-2255. RX PubMed=9295268; DOI=10.1126/science.277.5333.1805; RA Allikmets R., Shroyer N.F., Singh N., Seddon J.M., Lewis R.A., RA Bernstein P.S., Peiffer A., Zabriskie N.A., Li Y., Hutchinson A., Dean M., RA Lupski J.R., Leppert M.; RT "Mutation of the Stargardt disease gene (ABCR) in age-related macular RT degeneration."; RL Science 277:1805-1807(1997). RN [18] RP VARIANTS STGD1 TRP-18; CYS-212; HIS-636; MET-1019; VAL-1038; CYS-1108; RP TRP-1640; SER-1977 AND HIS-2107, AND VARIANTS FFM PRO-11; PRO-541; RP VAL-1038; GLU-1091; CYS-1508; PHE-1970 AND ARG-1971. RX PubMed=9781034; DOI=10.1038/sj.ejhg.5200221; RA Rozet J.-M., Gerber S., Souied E., Perrault I., Chatelin S., Ghazi I., RA Leowski C., Dufier J.-L., Munnich A., Kaplan J.; RT "Spectrum of ABCR gene mutations in autosomal recessive macular RT dystrophies."; RL Eur. J. Hum. Genet. 6:291-295(1998). RN [19] RP REVIEW, AND VARIANTS STGD1 ARG-68; GLY-75; GLY-249; CYS-336; GLU-523; RP LEU-1071; ALA-1072; TYR-1406; ASP-1439; SER-1440; 1761-PRO--LEU-1763 DEL; RP PRO-1820 AND GLU-1886. RX PubMed=9973280; DOI=10.1086/302251; RA Lewis R.A., Shroyer N.F., Singh N., Allikmets R., Hutchinson A., Li Y., RA Lupski J.R., Leppert M., Dean M.; RT "Genotype/phenotype analysis of a photoreceptor-specific ATP-binding RT cassette transporter gene, ABCR, in Stargardt disease."; RL Am. J. Hum. Genet. 64:422-434(1999). RN [20] RP REVIEW, AND VARIANTS STGD1 ARG-957; ASN-1112 AND PRO-1631. RX PubMed=10090887; DOI=10.1086/302323; RA Maugeri A., van Driel M.A., van de Pol D.J.R., Klevering B.J., RA van Haren F.J.J., Tijmes N., Bergen A.A.B., Rohrschneider K., RA Blankenagel A., Pinckers A.J.L.G., Dahl N., Brunner H.G., Deutman A.F., RA Hoyng C.B., Cremers F.P.M.; RT "The 2588G-->C mutation in the ABCR gene is a mild frequent founder RT mutation in the western European population and allows the classification RT of ABCR Mutations in patients with Stargardt disease."; RL Am. J. Hum. Genet. 64:1024-1035(1999). RN [21] RP VARIANT STGD1 TYR-54, AND VARIANT ALA-863. RX PubMed=10612508; DOI=10.1016/s0002-9394(99)00236-6; RA Zhang K., Garibaldi D.C., Kniazeva M., Albini T., Chiang M.F., Kerrigan M., RA Sunness J.S., Han M., Allikmets R.; RT "A novel mutation in the ABCR gene in four patients with autosomal RT recessive Stargardt disease."; RL Am. J. Ophthalmol. 128:720-724(1999). RN [22] RP VARIANTS STGD1 VAL-60; ARG-206; ASN-300; PRO-541; ALA-849; PRO-974; RP VAL-1038; CYS-1108; LEU-1408; ARG-1488; ASP-1652; PRO-1729; GLU-1961; RP TRP-2038; TRP-2077; HIS-2107; ARG-2128 AND TYR-2150. RX PubMed=10206579; DOI=10.1001/archopht.117.4.504; RA Fishman G.A., Stone E.M., Grover S., Derlacki D.J., Haines H.L., RA Hockey R.R.; RT "Variation of clinical expression in patients with Stargardt dystrophy and RT sequence variations in the ABCR gene."; RL Arch. Ophthalmol. 117:504-510(1999). RN [23] RP VARIANTS GLU-1961 AND ASN-2177. RX PubMed=10880298; DOI=10.1086/303018; RA Allikmets R., Tammur J., Hutchinson A., Lewis R.A., Shroyer N.F., RA Dalakishvili K., Lupski J.R., Steiner K., Pauleikhoff D., Holz F.G., RA Weber B.H.F., Dean M., Atkinson A., Gail M.H., Bernstein P.S., Singh N., RA Peiffer A., Zabriskie N.A., Leppert M., Seddon J.M., Zhang K., RA Sunness J.S., Udar N.S., Yelchits S., Silva-Garcia R., Small K.W., RA Simonelli F., Testa F., D'Urso M., Brancato R., Rinaldi E., Ingvast S., RA Taube A., Wadelius C., Souied E., Ducroq D., Kaplan J., Assink J.J.M., RA ten Brink J.B., de Jong P.T.V.M., Bergen A.A.B., Maugeri A., RA van Driel M.A., Hoyng C.B., Cremers F.P.M., Paloma E., Coco R., RA Balcells S., Gonzalez-Duarte R., Kermani S., Stanga P., Bhattacharya S.S., RA Bird A.C.; RT "Further evidence for an association of ABCR alleles with age-related RT macular degeneration."; RL Am. J. Hum. Genet. 67:487-491(2000). RN [24] RP VARIANTS STGD1 GLU-60; THR-60; GLU-65; LEU-68; ARG-72; CYS-212; SER-230; RP SER-247; VAL-328; LYS-471; PRO-541; GLN-572; ARG-607; LYS-635; CYS-653; RP TYR-764; ARG-765; ALA-901; ILE-959; LYS-1036; VAL-1038; PRO-1063; ASP-1087; RP CYS-1097; CYS-1108; LEU-1380; LYS-1399; PRO-1430; VAL-1440; HIS-1443; RP LEU-1486; TYR-1488; MET-1537; PRO-1689; LEU-1705; THR-1733; ARG-1748; RP PRO-1763; LYS-1885; HIS-1898; GLU-1961; ARG-1975; SER-1977; GLY-2077; RP TRP-2077 AND VAL-2241, AND VARIANTS GLN-152; HIS-212; ARG-423; ILE-552; RP ARG-914; GLN-943; THR-1562; ILE-1868; MET-1921; LEU-1948; PHE-1970; RP ALA-2059; ASN-2177 AND VAL-2216. RX PubMed=10958763; DOI=10.1086/303090; RA Rivera A., White K., Stoehr H., Steiner K., Hemmrich N., Grimm T., RA Jurklies B., Lorenz B., Scholl H.P.N., Apfelstedt-Sylla E., Weber B.H.F.; RT "A comprehensive survey of sequence variation in the ABCA4 (ABCR) gene in RT Stargardt disease and age-related macular degeneration."; RL Am. J. Hum. Genet. 67:800-813(2000). RN [25] RP VARIANTS CORD3 GLU-65; CYS-212; PRO-541; ALA-863; GLY-863 DEL; VAL-1038; RP LYS-1122; TYR-1490 AND ASP-1598. RX PubMed=10958761; DOI=10.1086/303079; RA Maugeri A., Klevering B.J., Rohrschneider K., Blankenagel A., Brunner H.G., RA Deutman A.F., Hoyng C.B., Cremers F.P.M.; RT "Mutations in the ABCA4 (ABCR) gene are the major cause of autosomal RT recessive cone-rod dystrophy."; RL Am. J. Hum. Genet. 67:960-966(2000). RN [26] RP VARIANTS STGD1 ASP-340; GLN-572; ALA-863; SER-965; VAL-1038; ALA-1780 AND RP HIS-1898, AND VARIANT GLN-943. RX PubMed=10746567; DOI=10.1007/s004390051034; RA Shroyer N.F., Lewis R.A., Lupski J.R.; RT "Complex inheritance of ABCR mutations in Stargardt disease: linkage RT disequilibrium, complex alleles, and pseudodominance."; RL Hum. Genet. 106:244-248(2000). RN [27] RP VARIANTS GLN-943 AND SER-1948, VARIANTS STGD1 TYR-54; ASP-96; HIS-96; RP VAL-156; VAL-407; ALA-424; ARG-445; TRP-602; 779-CYS--ASP-2273 DEL; RP ALA-863; ALA-1429; TRP-1640; GLU-1703; 1779-TYR--ASP-2273 DEL AND ARG-2160, RP VARIANTS CORD3 VAL-407; 2030-ARG--ASP-2273 DEL AND TYR-2150, AND VARIANT RP RP19 ALA-424. RX PubMed=10634594; RA Papaioannou M., Ocaka L., Bessant D., Lois N., Bird A.C., Payne A., RA Bhattacharya S.S.; RT "An analysis of ABCR mutations in British patients with recessive retinal RT dystrophies."; RL Invest. Ophthalmol. Vis. Sci. 41:16-19(2000). RN [28] RP VARIANTS STGD1 CYS-212; ASP-767; ILE-897; VAL-1038; LYS-1087; LYS-1399; RP GLN-1640 AND GLU-1961, AND VARIANT HIS-212. RX PubMed=10711710; RA Simonelli F., Testa F., de Crecchio G., Rinaldi E., Hutchinson A., RA Atkinson A., Dean M., D'Urso M., Allikmets R.; RT "New ABCR mutations and clinical phenotype in Italian patients with RT Stargardt disease."; RL Invest. Ophthalmol. Vis. Sci. 41:892-897(2000). RN [29] RP CHARACTERIZATION OF VARIANTS, AND MUTAGENESIS OF GLY-966; LYS-969; GLY-1975 RP AND LYS-1978. RX PubMed=11017087; DOI=10.1038/79994; RA Sun H., Smallwood P.M., Nathans J.; RT "Biochemical defects in ABCR protein variants associated with human RT retinopathies."; RL Nat. Genet. 26:242-246(2000). RN [30] RP VARIANT STGD1 ASN-972, AND VARIANTS GLN-943; ILE-1868 AND LEU-1948. RX PubMed=11594993; DOI=10.1034/j.1600-0420.2001.790520.x; RA Eksandh L., Ekstroem U., Abrahamson M., Bauer B., Andreasson S.; RT "Different clinical expressions in two families with Stargardt's macular RT dystrophy (STGD1)."; RL Acta Ophthalmol. Scand. 79:524-530(2001). RN [31] RP VARIANTS RETINAL TOXICITY CYS-1129; ARG-1201 AND HIS-2107, AND VARIANTS RP HIS-212; ARG-423; ILE-1868 AND ILE-2255. RX PubMed=11384574; DOI=10.1016/s0002-9394(01)00838-8; RA Shroyer N.F., Lewis R.A., Lupski J.R.; RT "Analysis of the ABCR (ABCA4) gene in 4-aminoquinoline retinopathy: is RT retinal toxicity by chloroquine and hydroxychloroquine related to Stargardt RT disease?"; RL Am. J. Ophthalmol. 131:761-766(2001). RN [32] RP VARIANTS GLU-1961 AND ASN-2177. RX PubMed=11346402; DOI=10.1001/archopht.119.5.745; RA Guymer R.H., Heon E., Lotery A.J., Munier F.L., Schorderet D.F., RA Baird P.N., McNeil R.J., Haines H.L., Sheffield V.C., Stone E.M.; RT "Variation of codons 1961 and 2177 of the Stargardt disease gene is not RT associated with age-related macular degeneration."; RL Arch. Ophthalmol. 119:745-751(2001). RN [33] RP VARIANTS FFM GLY-339; ALA-863; TRP-943; ARG-991; VAL-1038; CYS-1108; RP ARG-1488; THR-1562; GLN-1640; PHE-2027; GLN-2030 AND CYS-2106, AND VARIANTS RP HIS-212; ARG-423; GLN-943; THR-1148; ILE-1868 AND ILE-2255. RX PubMed=11379881; DOI=10.1007/s004390100493; RA Yatsenko A.N., Shroyer N.F., Lewis R.A., Lupski J.R.; RT "Late-onset Stargardt disease is associated with missense mutations that RT map outside known functional regions of ABCR (ABCA4)."; RL Hum. Genet. 108:346-355(2001). RN [34] RP VARIANTS STGD1 SER-686; TRP-1055; ASP-1799; ASP-1805; PRO-1940 AND RP HIS-2107, VARIANTS FFM MET-1253 AND PRO-1940, VARIANTS CORD3 CYS-212 AND RP ARG-2060, AND VARIANTS GLN-943; LEU-1948 AND ILE-2255. RX PubMed=11385708; DOI=10.1002/humu.1133; RA Paloma E., Martinez-Mir A., Vilageliu L., Gonzalez-Duarte R., Balcells S.; RT "Spectrum of ABCA4 (ABCR) gene mutations in Spanish patients with autosomal RT recessive macular dystrophies."; RL Hum. Mutat. 17:504-510(2001). RN [35] RP REVIEW, VARIANTS STGD1 THR-192; CYS-220; TRP-333; TRP-607; LEU-873; RP ASN-971; ALA-1019; GLU-1031; PRO-1250; PHE-1488; ARG-1513; PRO-1525; RP ILE-1693; PRO-1736; GLU-1884; ASP-1896; PHE-2071; PRO-2229 AND LEU-2263, RP AND VARIANT THR-1314. RX PubMed=11328725; RA Webster A.R., Heon E., Lotery A.J., Vandenburgh K., Casavant T.L., Oh K.T., RA Beck G., Fishman G.A., Lam B.L., Levin A., Heckenlively J.R., RA Jacobson S.G., Weleber R.G., Sheffield V.C., Stone E.M.; RT "An analysis of allelic variation in the ABCA4 gene."; RL Invest. Ophthalmol. Vis. Sci. 42:1179-1189(2001). RN [36] RP VARIANTS STGD1 13-LYS--TRP-15 DEL; TYR-54; LYS-58; VAL-60; GLU-65; GLU-77; RP HIS-190; PRO-244; ARG-309; CYS-525; CYS-537; PRO-541; PRO-549; ARG-550; RP GLN-602; ARG-607; MET-643; ASP-767; PRO-797; ARG-821; THR-824; ALA-863; RP ALA-935; TRP-943; ALA-989; VAL-1038; CYS-1108; LEU-1108; LYS-1122; RP ARG-1201; GLN-1300; LEU-1380; PRO-1388; ARG-1408; LEU-1486; ARG-1488; RP TYR-1490; MET-1526; ASN-1532; THR-1562; TRP-1640; LEU-1776; THR-1846; RP GLU-1961; SER-1977; PHE-2027; GLN-2030; PRO-2035; LEU-2050; CYS-2107; RP HIS-2107; TRP-2139; ARG-2150 AND TYR-2150, VARIANTS CORD3 GLN-1640 AND RP ASP-2146, AND VARIANTS HIS-212; ARG-423; GLN-943; THR-1637; ILE-1868 AND RP LEU-1948. RX PubMed=11527935; RA Briggs C.E., Rucinski D., Rosenfeld P.J., Hirose T., Berson E.L., RA Dryja T.P.; RT "Mutations in ABCR (ABCA4) in patients with Stargardt macular degeneration RT or cone-rod degeneration."; RL Invest. Ophthalmol. Vis. Sci. 42:2229-2236(2001). RN [37] RP VARIANT ARG-423. RX PubMed=12111378; DOI=10.1007/s100380200041; RA Iida A., Saito S., Sekine A., Mishima C., Kitamura Y., Kondo K., RA Harigae S., Osawa S., Nakamura Y.; RT "Catalog of 605 single-nucleotide polymorphisms (SNPs) among 13 genes RT encoding human ATP-binding cassette transporters: ABCA4, ABCA7, ABCA8, RT ABCD1, ABCD3, ABCD4, ABCE1, ABCF1, ABCG1, ABCG2, ABCG4, ABCG5, and ABCG8."; RL J. Hum. Genet. 47:285-310(2002). RN [38] RP VARIANTS STGD1 TRP-18; LYS-96; VAL-108; LEU-143; GLN-152; GLN-223; SER-230; RP 245-TYR--ASP-2273 DEL; THR-246; GLU-498; PRO-541; ARG-550; GLN-572; RP 639-TYR--ASP-2273 DEL; SER-641; CYS-653; VAL-690; 700-TRP--ASP-2273 DEL; RP ASP-767; ARG-821; ALA-863; 876-GLN--ASP-2273 DEL; ILE-897; ASP-954; RP SER-965; ASP-978; LYS-1022; VAL-1038; ASP-1050; LYS-1087; CYS-1098; RP PRO-1099; CYS-1108; HIS-1108; LEU-1129; ARG-1203; ASP-1203; ASN-1204; RP 1300-ARG--ASP-2273 DEL; GLN-1300; TYR-1490; ARG-1512; MET-1526; ASP-1598; RP 1652-TYR--ASP-2273 DEL; ASP-1762; ASN-1838; TYR-1838; GLU-1961; PHE-1970; RP PHE-2027; GLN-2030; LEU-2050; HIS-2107; TRP-2139; LEU-2149; TYR-2150; RP ASN-2177 AND VAL-2241, AND VARIANTS HIS-212; ARG-423; GLN-943; LEU-1380; RP ILE-1868 AND LEU-1948. RX PubMed=15192030; DOI=10.1373/clinchem.2004.033241; RA Stenirri S., Fermo I., Battistella S., Galbiati S., Soriani N., Paroni R., RA Manitto M.P., Martina E., Brancato R., Allikmets R., Ferrari M., RA Cremonesi L.; RT "Denaturing HPLC profiling of the ABCA4 gene for reliable detection of RT allelic variations."; RL Clin. Chem. 50:1336-1343(2004). RN [39] RP VARIANT [LARGE SCALE ANALYSIS] MET-224. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [40] RP VARIANTS ARMD2 GLU-762; LEU-1129; CYS-1724; SER-1977; ASN-2047 AND RP TYR-2137, AND VARIANT ILE-552. RX PubMed=19028736; DOI=10.1136/bjo.2008.145193; RA Aguirre-Lamban J., Riveiro-Alvarez R., Maia-Lopes S., Cantalapiedra D., RA Vallespin E., Avila-Fernandez A., Villaverde-Montero C., RA Trujillo-Tiebas M.J., Ramos C., Ayuso C.; RT "Molecular analysis of the ABCA4 gene for reliable detection of allelic RT variations in Spanish patients: identification of 21 novel variants."; RL Br. J. Ophthalmol. 93:614-621(2009). RN [41] RP VARIANTS STGD1 VAL-156; CYS-212; LYS-380; ARG-550; PRO-572; TRP-602; RP ARG-607; CYS-653; ASP-767; ILE-897; ALA-901; MET-931; SER-965; MET-1019; RP HIS-1108; LEU-1129; LEU-1380; ILE-1433; LEU-1486; TYR-1490; GLN-1640; RP TRP-1640; ARG-1748; ASP-1799; PRO-1940; GLU-1961; SER-1977; PHE-2027; RP ARG-2060; HIS-2107; TYR-2150 AND VAL-2241. RX PubMed=18977788; DOI=10.1136/bjo.2008.148155; RA Riveiro-Alvarez R., Aguirre-Lamban J., Lopez-Martinez M.A., RA Trujillo-Tiebas M.J., Cantalapiedra D., Vallespin E., Avila-Fernandez A., RA Ramos C., Ayuso C.; RT "Frequency of ABCA4 mutations in 278 Spanish controls: an insight into the RT prevalence of autosomal recessive Stargardt disease."; RL Br. J. Ophthalmol. 93:1359-1364(2009). RN [42] RP VARIANTS STGD1 21-GLN--ASP-2273 DEL; LEU-68; HIS-96; LYS-96; SER-172; RP CYS-212; LYS-415; PRO-541; 572-ARG--ASP-2273 DEL; LYS-616; CYS-653; RP VAL-690; 700-TRP--ASP-2273 DEL; ASP-767; ARG-821; ARG-840; MET-931; RP SER-965; PRO-970; PRO-977; ASP-978; MET-1019; VAL-1038; TRP-1055; GLU-1078; RP LYS-1087; CYS-1098; 1099-SER--ASP-2273 DEL; CYS-1108; 1177-CYS--ASP-2273 RP DEL; 1332-GLN--ASP-2273 DEL; LEU-1380; 1408-TRP--ASP-2273 DEL; ILE-1433; RP 1461-TRP--ASP-2273 DEL; 1479-TRP--ASP-2273 DEL; SER-1484; MET-1526; RP ASP-1598; ASN-1696; GLU-1961; PHE-1970; SER-1977; 2030-ARG--ASP-2273 DEL; RP LYS-2096; GLN-2140 AND PRO-2221. RX PubMed=19265867; DOI=10.1038/eye.2009.35; RA Passerini I., Sodi A., Giambene B., Mariottini A., Menchini U., RA Torricelli F.; RT "Novel mutations in of the ABCR gene in Italian patients with Stargardt RT disease."; RL Eye 24:158-164(2010). RN [43] RP VARIANT LEU-2050. RX PubMed=20335603; DOI=10.1167/iovs.09-4655; RA Poloschek C.M., Bach M., Lagreze W.A., Glaus E., Lemke J.R., Berger W., RA Neidhardt J.; RT "ABCA4 and ROM1: implications for modification of the PRPH2-associated RT macular dystrophy phenotype."; RL Invest. Ophthalmol. Vis. Sci. 51:4253-4265(2010). RN [44] RP VARIANTS 219-ARG--ASP-2273 DEL; HIS-576; GLN-943; ARG-1488; MET-1526; RP CYS-1557; THR-1562; GLU-1773; ASP-1794; 2040-ARG--ASP-2273 DEL AND RP CYS-2107, AND VARIANTS STGD1 TYR-54; GLN-152; ARG-184; PHE-184; CYS-212; RP SER-418; LYS-471; MET-643; CYS-653; 782-TRP--ASP-2273 DEL; ALA-863; RP ALA-989; ARG-991; MET-1019; LYS-1022; SER-1097; CYS-1108; LYS-1122; RP LEU-1129; ARG-1201; LEU-1380; LYS-1442; LEU-1486; TYR-1490; ASP-1598; RP ASP-1754; THR-1846; GLU-1961; PHE-2027; GLN-2030; CYS-2106; LYS-2131; RP TYR-2150 AND PRO-2237. RX PubMed=23143460; DOI=10.1001/archophthalmol.2012.1697; RA Downes S.M., Packham E., Cranston T., Clouston P., Seller A., Nemeth A.H.; RT "Detection rate of pathogenic mutations in ABCA4 using direct sequencing: RT clinical and research implications."; RL Arch. Ophthalmol. 130:1486-1490(2012). RN [45] RP VARIANTS STGD1 TRP-18; HIS-24; 89-GLU--ASP-2273 DEL; CYS-212; ASP-241; RP TRP-290; TRP-602; GLU-818; SER-965; ARG-1014; LEU-1129; LEU-1380; PHE-1416 RP DEL; HIS-1443; TRP-1551 DEL; THR-1556; 1681-VAL--VAL-1685 DEL; GLN-1705; RP VAL-1773; ASN-1775; HIS-1779; GLN-1942; VAL-2074 AND ARG-2128, AND VARIANTS RP GLN-943; ILE-1868 AND ILE-2255. RX PubMed=23419329; DOI=10.1016/j.exer.2013.02.006; RA Chacon-Camacho O.F., Granillo-Alvarez M., Ayala-Ramirez R., Zenteno J.C.; RT "ABCA4 mutational spectrum in Mexican patients with Stargardt disease: RT Identification of 12 novel mutations and evidence of a founder effect for RT the common p.A1773V mutation."; RL Exp. Eye Res. 109:77-82(2013). RN [46] RP VARIANT STGD1 TRP-602. RX PubMed=24444108; DOI=10.1186/1471-2350-15-11; RA Ortube M.C., Strom S.P., Nelson S.F., Nusinowitz S., Martinez A., RA Gorin M.B.; RT "Whole exome sequencing detects homozygosity for ABCA4 p.Arg602Trp missense RT mutation in a pediatric patient with rapidly progressive retinal RT dystrophy."; RL BMC Med. Genet. 15:11-11(2014). RN [47] RP VARIANTS STGD1 CYS-212; PRO-541; LEU-640; ASP-767; VAL-1038; CYS-1108; RP ARG-1408; GLN-1640; TRP-1640; ASP-1838; GLU-1961 AND HIS-2107. RX PubMed=24457364; DOI=10.1136/bjophthalmol-2013-304270; RA Miraldi Utz V., Coussa R.G., Marino M.J., Chappelow A.V., Pauer G.J., RA Hagstrom S.A., Traboulsi E.I.; RT "Predictors of visual acuity and genotype-phenotype correlates in a cohort RT of patients with Stargardt disease."; RL Br. J. Ophthalmol. 98:513-518(2014). RN [48] RP VARIANTS CORD3 CYS-440; GLY-643; HIS-1145; GLU-1203; LEU-2050 AND ASN-2177, RP VARIANTS STGD1 HIS-24; GLU-65; SER-247; 431-TRP--ASP-2273 DEL; PRO-541; RP ARG-607; HIS-653; ALA-863; 1029-GLN--ASP-2273 DEL; VAL-1038; GLN-1300; RP MET-1537; TRP-1640; PRO-1763; HIS-1898; GLU-1961; PHE-1970; PHE-2027; RP GLN-2030 AND ARG-2033, VARIANTS RP19 MET-455 AND ILE-552, VARIANTS RP 681-ARG--ASP-2273 DEL; ASP-767 AND ARG-1591, AND VARIANT CORD3 GLU-1961. RX PubMed=25346251; DOI=10.1002/humu.22716; RA Bauwens M., De Zaeytijd J., Weisschuh N., Kohl S., Meire F., Dahan K., RA Depasse F., De Jaegere S., De Ravel T., De Rademaeker M., Loeys B., RA Coppieters F., Leroy B.P., De Baere E.; RT "An augmented ABCA4 screen targeting noncoding regions reveals a deep RT intronic founder variant in Belgian Stargardt patients."; RL Hum. Mutat. 36:39-42(2015). RN [49] RP VARIANTS STGD1 LYS-14; PRO-18; HIS-24; VAL-72; CYS-97; 185-GLN--ASP-2273 RP DEL; ARG-240; LEU-291; 326-TYR--ASP-2273 DEL; VAL-328; SER-345; THR-410; RP CYS-508; CYS-511; ARG-519; 533-GLN--ASP-2273 DEL; CYS-537; ARG-548; RP ARG-550; LEU-593; TRP-602; CYS-603; ARG-607; ASN-645; HIS-653; SER-754; RP 808-TYR--ASP-2273 DEL; VAL-816; SER-965; TYR-965; SER-973; MET-1019; RP GLY-1022; LYS-1036; LEU-1074; THR-1094; HIS-1108; LYS-1122; THR-1130; RP TRP-1140; SER-1159; HIS-1161; 1300-ARG--ASP-2273 DEL; ASN-1371; RP 1453-TYR--ASP-2273 DEL; LEU-1503; HIS-1511; MET-1526; ARG-1591; RP 1724-TRP--ASP-2273 DEL; VAL-1773; LEU-1776; TRP-1843; LYS-1885; GLY-1921; RP MET-1921; ARG-1961; SER-1977; TYR-2017; THR-2023; 2030-ARG--ASP-2273 DEL; RP ARG-2032; TRP-2038; 2040-ARG--ASP-2273 DEL; GLN-2040; GLY-2042; THR-2064; RP GLU-2078; SER-2097; ARG-2150 AND SER-2188, VARIANTS ARG-423; TYR-1102; RP THR-1209; MET-1428; MET-1572; 1618-TRP--ASP-2273 DEL; VAL-1623; GLN-1640; RP 1652-TYR--ASP-2273 DEL; ILE-1868 AND ILE-2255, AND VARIANTS CORD3 RP 53-GLU--ASP-2273 DEL; ARG-55; PRO-63; 107-ARG--ASP-2273 DEL; RP 218-GLN--ASP-2273 DEL; CYS-320; 339-TRP--ASP-2273 DEL; 605-TRP--ASP-2273 RP DEL; LYS-636; ARG-661; CYS-1183; CYS-1368; 1479-TRP--ASP-2273 DEL; RP 1650-GLU--ASP-2273 DEL; ILE-1882; SER-2043; HIS-2107 AND ASP-2146. RX PubMed=26780318; DOI=10.1167/iovs.15-18190; RA Jiang F., Pan Z., Xu K., Tian L., Xie Y., Zhang X., Chen J., Dong B., RA Li Y.; RT "Screening of ABCA4 Gene in a Chinese Cohort With Stargardt Disease or RT Cone-Rod Dystrophy With a Report on 85 Novel Mutations."; RL Invest. Ophthalmol. Vis. Sci. 57:145-152(2016). RN [50] RP VARIANTS STGD1 ARG-72; PRO-541; VAL-1038; GLU-1091; PRO-1794 AND TRP-2077, RP CHARACTERIZATION OF VARIANTS STGD1 ARG-72; PRO-541; VAL-1038; GLU-1091; RP PRO-1794 AND TRP-2077, MUTAGENESIS OF ALA-1357, FUNCTION, AND SUBCELLULAR RP LOCATION. RX PubMed=29847635; DOI=10.1167/iovs.17-23364; RA Garces F., Jiang K., Molday L.L., Stoehr H., Weber B.H., Lyons C.J., RA Maberley D., Molday R.S.; RT "Correlating the Expression and Functional Activity of ABCA4 Disease RT Variants With the Phenotype of Patients With Stargardt Disease."; RL Invest. Ophthalmol. Vis. Sci. 59:2305-2315(2018). RN [51] RP VARIANTS ALA-863; GLY-863 DEL AND ILE-1868. RX PubMed=30120214; DOI=10.1136/jmedgenet-2018-105364; RA de Bruijn S.E., Verbakel S.K., de Vrieze E., Kremer H., Cremers F.P.M., RA Hoyng C.B., van den Born L.I., Roosing S.; RT "Homozygous variants in KIAA1549, encoding a ciliary protein, are RT associated with autosomal recessive retinitis pigmentosa."; RL J. Med. Genet. 55:705-712(2018). RN [52] RP FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS STGD1 CYS-653; RP HIS-653; ARG-661; SER-686; VAL-690; MET-716; TYR-764; ARG-765; ASN-765; RP ASP-767; PRO-797; GLU-818; ARG-821; THR-824; ARG-840; ALA-849; ASP-851; RP THR-854; LEU-1380; LYS-1399; ASN-1696; GLU-1703; LYS-1703; LEU-1705; RP VAL-1773; ASP-1794; PRO-1794; ASP-1805; ASN-1838; ASP-1838; TYR-1838; RP TRP-1843 AND HIS-1898, CHARACTERIZATION OF VARIANTS HIS-846; GLU-1773; RP ILE-1868 AND CYS-1898, AND MUTAGENESIS OF HIS-1838. RX PubMed=33375396; DOI=10.3390/ijms22010185; RA Garces F.A., Scortecci J.F., Molday R.S.; RT "Functional Characterization of ABCA4 Missense Variants Linked to Stargardt RT Macular Degeneration."; RL Int. J. Mol. Sci. 22:0-0(2020). CC -!- FUNCTION: Flippase that catalyzes in an ATP-dependent manner the CC transport of retinal-phosphatidylethanolamine conjugates like the 11- CC cis and all-trans isomers of N-retinylidene-phosphatidylethanolamine CC from the lumen to the cytoplasmic leaflet of photoreceptor outer CC segment disk membranes, where N-cis-retinylidene- CC phosphatidylethanolamine (N-cis-R-PE) is then isomerized to its all- CC trans isomer (N-trans-R-PE) and reduced by RDH8 to produce all-trans- CC retinol (all-trans-rol) and therefore prevents the accumulation of CC excess of 11-cis-retinal and its schiff-base conjugate and the CC formation of toxic bisretinoid (PubMed:24097981, PubMed:22735453, CC PubMed:23144455, PubMed:20404325, PubMed:10075733, PubMed:29847635, CC PubMed:33375396). May display both ATPase and GTPase activity that is CC strongly influenced by the lipid environment and the presence of CC retinoid compounds (PubMed:22735453). Binds the unprotonated form of N- CC retinylidene-phosphatidylethanolamine with high affinity in the absence CC of ATP, and ATP binding and hydrolysis induce a protein conformational CC change that causes the dissociation of N-retinylidene- CC phosphatidylethanolamine (By similarity). CC {ECO:0000250|UniProtKB:F1MWM0, ECO:0000269|PubMed:10075733, CC ECO:0000269|PubMed:20404325, ECO:0000269|PubMed:22735453, CC ECO:0000269|PubMed:23144455, ECO:0000269|PubMed:24097981, CC ECO:0000269|PubMed:29847635, ECO:0000269|PubMed:33375396}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + N-all-trans- CC retinylidenephosphatidylethanolamine(out) = ADP + H(+) + N-all-trans- CC retinylidenephosphatidylethanolamine(in) + phosphate; CC Xref=Rhea:RHEA:67188, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:167884, CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:22735453}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67189; CC Evidence={ECO:0000305|PubMed:22735453}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + CC phospholipidSide 2.; EC=7.6.2.1; CC Evidence={ECO:0000269|PubMed:24097981}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O CC = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) + CC phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:64612, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:22735453, ECO:0000269|PubMed:24097981}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133; CC Evidence={ECO:0000305|PubMed:24097981}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + N-11-cis-retinylidenephosphatidylethanolamine(out) CC = ADP + H(+) + N-11-cis-retinylidenephosphatidylethanolamine(in) + CC phosphate; Xref=Rhea:RHEA:67192, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:167887, ChEBI:CHEBI:456216; CC Evidence={ECO:0000250|UniProtKB:F1MWM0}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67193; CC Evidence={ECO:0000250|UniProtKB:F1MWM0}; CC -!- ACTIVITY REGULATION: ATPase activity is decreased by cholesterol and CC ceramide. ATPase activity is stimulated by phosphatidylethanolamine. CC Phospholipids translocase activity is highly reduced by berylium CC fluoride and aluminum floride. N-ethylmaleimide inhibits phospholipid CC translocase activity. {ECO:0000269|PubMed:24097981}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=80 uM for ATP {ECO:0000269|PubMed:33605212}; CC Vmax=112.5 nmol/min/mg enzyme (for ATP hydrolysis) CC {ECO:0000269|PubMed:33605212}; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10075733}; Multi- CC pass membrane protein {ECO:0000255}. Endoplasmic reticulum CC {ECO:0000269|PubMed:24097981}. Cytoplasmic vesicle CC {ECO:0000269|PubMed:29847635, ECO:0000269|PubMed:33375396}. Cell CC projection, cilium, photoreceptor outer segment CC {ECO:0000250|UniProtKB:F1MWM0}. Note=Localized to the rim and incisures CC of rod outer segments disks. {ECO:0000250|UniProtKB:F1MWM0}. CC -!- TISSUE SPECIFICITY: Retinal-specific. Seems to be exclusively found in CC the rims of rod photoreceptor cells. CC -!- DOMAIN: The second extracellular domain (ECD2, aa 1395-1680) undergoes CC conformational change in response to its specific interaction with its CC substrate all-trans-retinal (PubMed:20404325). Nucleotide binding CC domain 1 (NBD1, aa 854-1375) binds preferentially and with high CC affinity with the 11-cis retinal (PubMed:23144455). CC {ECO:0000269|PubMed:20404325, ECO:0000269|PubMed:23144455}. CC -!- PTM: Proteolytic cleavage by trypsin leads to a 120-kDa N-terminal CC fragment and a 115-kDa C-terminal fragment that are linked through CC disulfide bonds. {ECO:0000269|PubMed:11320094}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11320094}. CC -!- PTM: Phosphorylation is independent of light exposure and modulates CC ATPase activity. {ECO:0000250|UniProtKB:F1MWM0}. CC -!- DISEASE: Stargardt disease 1 (STGD1) [MIM:248200]: A common hereditary CC macular degeneration. It is characterized by decreased central vision, CC atrophy of the macula and underlying retinal pigment epithelium, and CC frequent presence of prominent flecks in the posterior pole of the CC retina. {ECO:0000269|PubMed:10090887, ECO:0000269|PubMed:10206579, CC ECO:0000269|PubMed:10612508, ECO:0000269|PubMed:10634594, CC ECO:0000269|PubMed:10711710, ECO:0000269|PubMed:10746567, CC ECO:0000269|PubMed:10958763, ECO:0000269|PubMed:11328725, CC ECO:0000269|PubMed:11385708, ECO:0000269|PubMed:11527935, CC ECO:0000269|PubMed:11594993, ECO:0000269|PubMed:15192030, CC ECO:0000269|PubMed:18977788, ECO:0000269|PubMed:19265867, CC ECO:0000269|PubMed:20404325, ECO:0000269|PubMed:22735453, CC ECO:0000269|PubMed:23143460, ECO:0000269|PubMed:23144455, CC ECO:0000269|PubMed:23419329, ECO:0000269|PubMed:24097981, CC ECO:0000269|PubMed:24444108, ECO:0000269|PubMed:24457364, CC ECO:0000269|PubMed:25346251, ECO:0000269|PubMed:26780318, CC ECO:0000269|PubMed:29847635, ECO:0000269|PubMed:33375396, CC ECO:0000269|PubMed:9054934, ECO:0000269|PubMed:9490294, CC ECO:0000269|PubMed:9503029, ECO:0000269|PubMed:9781034, CC ECO:0000269|PubMed:9973280}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Fundus flavimaculatus (FFM) [MIM:248200]: Autosomal recessive CC retinal disorder very similar to Stargardt disease. In contrast to CC Stargardt disease, FFM is characterized by later onset and slowly CC progressive course. {ECO:0000269|PubMed:10634594, CC ECO:0000269|PubMed:11379881, ECO:0000269|PubMed:11385708, CC ECO:0000269|PubMed:9781034}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Macular degeneration, age-related, 2 (ARMD2) [MIM:153800]: A CC form of age-related macular degeneration, a multifactorial eye disease CC and the most common cause of irreversible vision loss in the developed CC world. In most patients, the disease is manifest as ophthalmoscopically CC visible yellowish accumulations of protein and lipid that lie beneath CC the retinal pigment epithelium and within an elastin-containing CC structure known as Bruch membrane. {ECO:0000269|PubMed:19028736, CC ECO:0000269|PubMed:9295268}. Note=Disease susceptibility is associated CC with variants affecting the gene represented in this entry. CC -!- DISEASE: Cone-rod dystrophy 3 (CORD3) [MIM:604116]: An inherited CC retinal dystrophy characterized by retinal pigment deposits visible on CC fundus examination, predominantly in the macular region, and initial CC loss of cone photoreceptors followed by rod degeneration. This leads to CC decreased visual acuity and sensitivity in the central visual field, CC followed by loss of peripheral vision. Severe loss of vision occurs CC earlier than in retinitis pigmentosa, due to cone photoreceptors CC degenerating at a higher rate than rod photoreceptors. CC {ECO:0000269|PubMed:10634594, ECO:0000269|PubMed:10958761, CC ECO:0000269|PubMed:11385708, ECO:0000269|PubMed:11527935, CC ECO:0000269|PubMed:25346251, ECO:0000269|PubMed:26780318}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Retinitis pigmentosa 19 (RP19) [MIM:601718]: A retinal CC dystrophy belonging to the group of pigmentary retinopathies. Retinitis CC pigmentosa is characterized by retinal pigment deposits visible on CC fundus examination and primary loss of rod photoreceptor cells followed CC by secondary loss of cone photoreceptors. Patients typically have night CC vision blindness and loss of midperipheral visual field. As their CC condition progresses, they lose their far peripheral visual field and CC eventually central vision as well. RP19 is characterized by choroidal CC atrophy. {ECO:0000269|PubMed:10634594, ECO:0000269|PubMed:10958763, CC ECO:0000269|PubMed:25346251}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAE06122.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Mutations of the ABCA4 gene; Note=Retina CC International's Scientific Newsletter; CC URL="https://www.retina-international.org/files/sci-news/abcrmut.htm"; CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC proteins; CC URL="http://abcm2.hegelab.org/search"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U88667; AAC51144.1; -; mRNA. DR EMBL; AF000148; AAC23915.1; -; mRNA. DR EMBL; Y15635; CAA75729.1; -; Genomic_DNA. DR EMBL; Y15636; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15637; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15638; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15639; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15640; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15641; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15642; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15643; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15644; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15645; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15646; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15647; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15648; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15649; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15650; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15651; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15652; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15653; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15654; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15655; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15656; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15657; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15658; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15659; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15660; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15661; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15662; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15663; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15664; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15665; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15666; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15667; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15668; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15669; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15670; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15671; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15672; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15673; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15674; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15675; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15676; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15677; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15678; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15679; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15680; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15681; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15682; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15683; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15684; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; AF001945; AAC05632.1; -; mRNA. DR EMBL; AB210040; BAE06122.1; ALT_INIT; mRNA. DR EMBL; AC093579; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC105278; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; DQ426859; ABD90529.1; -; mRNA. DR CCDS; CCDS747.1; -. DR RefSeq; NP_000341.2; NM_000350.2. DR PDB; 7E7I; EM; 3.30 A; A=1-2273. DR PDB; 7E7O; EM; 3.40 A; A=1-2273. DR PDB; 7E7Q; EM; 3.30 A; A=1-2273. DR PDB; 7LKP; EM; 3.27 A; A=1-2273. DR PDB; 7LKZ; EM; 3.27 A; A=1-2273. DR PDB; 7M1P; EM; 3.60 A; A=1-2273. DR PDB; 7M1Q; EM; 2.92 A; A=1-2273. DR PDB; 8F5B; EM; 3.95 A; A=1-2273. DR PDBsum; 7E7I; -. DR PDBsum; 7E7O; -. DR PDBsum; 7E7Q; -. DR PDBsum; 7LKP; -. DR PDBsum; 7LKZ; -. DR PDBsum; 7M1P; -. DR PDBsum; 7M1Q; -. DR PDBsum; 8F5B; -. DR AlphaFoldDB; P78363; -. DR EMDB; EMD-23409; -. DR EMDB; EMD-23410; -. DR EMDB; EMD-23617; -. DR EMDB; EMD-23618; -. DR EMDB; EMD-25838; -. DR EMDB; EMD-27079; -. DR EMDB; EMD-28864; -. DR EMDB; EMD-31000; -. DR EMDB; EMD-31001; -. DR EMDB; EMD-31002; -. DR SMR; P78363; -. DR BioGRID; 106542; 4. DR ELM; P78363; -. DR IntAct; P78363; 2. DR STRING; 9606.ENSP00000359245; -. DR SwissLipids; SLP:000000347; -. DR TCDB; 3.A.1.211.2; the atp-binding cassette (abc) superfamily. DR GlyCosmos; P78363; 8 sites, No reported glycans. DR GlyGen; P78363; 9 sites, 1 O-linked glycan (1 site). DR iPTMnet; P78363; -. DR PhosphoSitePlus; P78363; -. DR BioMuta; ABCA4; -. DR DMDM; 6707663; -. DR EPD; P78363; -. DR MassIVE; P78363; -. DR PaxDb; 9606-ENSP00000359245; -. DR PeptideAtlas; P78363; -. DR ProteomicsDB; 57593; -. DR Antibodypedia; 33661; 214 antibodies from 32 providers. DR DNASU; 24; -. DR Ensembl; ENST00000370225.4; ENSP00000359245.3; ENSG00000198691.14. DR GeneID; 24; -. DR KEGG; hsa:24; -. DR MANE-Select; ENST00000370225.4; ENSP00000359245.3; NM_000350.3; NP_000341.2. DR UCSC; uc001dqh.4; human. DR AGR; HGNC:34; -. DR CTD; 24; -. DR DisGeNET; 24; -. DR GeneCards; ABCA4; -. DR GeneReviews; ABCA4; -. DR HGNC; HGNC:34; ABCA4. DR HPA; ENSG00000198691; Group enriched (choroid plexus, retina). DR MalaCards; ABCA4; -. DR MIM; 153800; phenotype. DR MIM; 248200; phenotype. DR MIM; 601691; gene. DR MIM; 601718; phenotype. DR MIM; 604116; phenotype. DR neXtProt; NX_P78363; -. DR OpenTargets; ENSG00000198691; -. DR Orphanet; 1872; Cone rod dystrophy. DR Orphanet; 279; NON RARE IN EUROPE: Age-related macular degeneration. DR Orphanet; 791; Retinitis pigmentosa. DR Orphanet; 827; Stargardt disease. DR PharmGKB; PA24379; -. DR VEuPathDB; HostDB:ENSG00000198691; -. DR eggNOG; KOG0059; Eukaryota. DR GeneTree; ENSGT00940000155624; -. DR HOGENOM; CLU_000604_19_1_1; -. DR InParanoid; P78363; -. DR OMA; EVHQSMG; -. DR OrthoDB; 6951at2759; -. DR PhylomeDB; P78363; -. DR TreeFam; TF105191; -. DR PathwayCommons; P78363; -. DR Reactome; R-HSA-2453864; Retinoid cycle disease events. DR Reactome; R-HSA-2453902; The canonical retinoid cycle in rods (twilight vision). DR Reactome; R-HSA-382556; ABC-family proteins mediated transport. DR SignaLink; P78363; -. DR BioGRID-ORCS; 24; 13 hits in 1147 CRISPR screens. DR ChiTaRS; ABCA4; human. DR GeneWiki; ABCA4; -. DR GenomeRNAi; 24; -. DR Pharos; P78363; Tbio. DR PRO; PR:P78363; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P78363; Protein. DR Bgee; ENSG00000198691; Expressed in pigmented layer of retina and 104 other cell types or tissues. DR ExpressionAtlas; P78363; baseline and differential. DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0097381; C:photoreceptor disc membrane; TAS:Reactome. DR GO; GO:0001750; C:photoreceptor outer segment; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IEA:InterPro. DR GO; GO:0120202; C:rod photoreceptor disc membrane; ISS:UniProtKB. DR GO; GO:0005502; F:11-cis retinal binding; IDA:UniProtKB. DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro. DR GO; GO:0005503; F:all-trans retinal binding; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; TAS:ProtInc. DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB. DR GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IBA:GO_Central. DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0140327; F:flippase activity; IDA:UniProtKB. DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB. DR GO; GO:0140347; F:N-retinylidene-phosphatidylethanolamine flippase activity; ISS:UniProtKB. DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; IDA:BHF-UCL. DR GO; GO:0005548; F:phospholipid transporter activity; IBA:GO_Central. DR GO; GO:0005501; F:retinoid binding; ISS:UniProtKB. DR GO; GO:0034632; F:retinol transmembrane transporter activity; TAS:Reactome. DR GO; GO:0006869; P:lipid transport; IBA:GO_Central. DR GO; GO:0006649; P:phospholipid transfer to membrane; IEA:Ensembl. DR GO; GO:0045332; P:phospholipid translocation; IDA:BHF-UCL. DR GO; GO:0045494; P:photoreceptor cell maintenance; IEA:Ensembl. DR GO; GO:0007603; P:phototransduction, visible light; TAS:ProtInc. DR GO; GO:0042574; P:retinal metabolic process; IDA:UniProtKB. DR GO; GO:0001523; P:retinoid metabolic process; ISS:UniProtKB. DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome. DR GO; GO:0007601; P:visual perception; TAS:ProtInc. DR CDD; cd03263; ABC_subfamily_A; 2. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR013525; ABC2_TM. DR InterPro; IPR003439; ABC_transporter-like_ATP-bd. DR InterPro; IPR017871; ABC_transporter-like_CS. DR InterPro; IPR026082; ABCA. DR InterPro; IPR005951; ABCA4/ABCR. DR InterPro; IPR027417; P-loop_NTPase. DR NCBIfam; TIGR01257; rim_protein; 1. DR PANTHER; PTHR19229; ATP-BINDING CASSETTE TRANSPORTER SUBFAMILY A ABCA; 1. DR PANTHER; PTHR19229:SF190; RETINAL-SPECIFIC PHOSPHOLIPID-TRANSPORTING ATPASE ABCA4; 1. DR Pfam; PF12698; ABC2_membrane_3; 2. DR Pfam; PF00005; ABC_tran; 2. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. DR Genevisible; P78363; HS. PE 1: Evidence at protein level; KW 3D-structure; Age-related macular degeneration; ATP-binding; KW Cell projection; Cone-rod dystrophy; Cytoplasmic vesicle; Disease variant; KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Membrane; KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; KW Retinitis pigmentosa; Sensory transduction; Stargardt disease; Translocase; KW Transmembrane; Transmembrane helix; Transport; Vision. FT CHAIN 1..2273 FT /note="Retinal-specific phospholipid-transporting ATPase FT ABCA4" FT /id="PRO_0000093301" FT TOPO_DOM 1..21 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 22..42 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 43..646 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:11320094" FT TRANSMEM 647..667 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 668..699 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 700..720 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 721..730 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 731..751 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 752..759 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 760..780 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 781..835 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 836..856 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 857..1376 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 1377..1397 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1398..1727 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:11320094" FT TRANSMEM 1728..1748 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1749..1759 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 1760..1780 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1781..1792 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 1793..1813 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1814..1831 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 1832..1852 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1853..1873 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 1874..1894 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1895..2273 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT DOMAIN 929..1160 FT /note="ABC transporter 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT DOMAIN 1938..2170 FT /note="ABC transporter 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT REGION 891..911 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1284..1345 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2244..2249 FT /note="Essential for ATP binding and ATPase activity" FT /evidence="ECO:0000269|PubMed:31481235" FT COMPBIAS 1327..1341 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 963..970 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434, FT ECO:0000269|PubMed:33605212, ECO:0007744|PDB:7LKZ" FT BINDING 1054 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:33605212, FT ECO:0007744|PDB:7LKZ" FT BINDING 1972..1980 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434, FT ECO:0000269|PubMed:33605212, ECO:0007744|PDB:7LKZ" FT BINDING 2073..2074 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:33605212, FT ECO:0007744|PDB:7LKZ" FT SITE 1309 FT /note="Cleavage; by trypsin" FT /evidence="ECO:0000250|UniProtKB:F1MWM0" FT MOD_RES 901 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:F1MWM0" FT MOD_RES 1185 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:F1MWM0" FT MOD_RES 1313 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:F1MWM0" FT MOD_RES 1317 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:F1MWM0" FT CARBOHYD 98 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:11320094, FT ECO:0000269|PubMed:33605212, ECO:0007744|PDB:7LKP, FT ECO:0007744|PDB:7LKZ" FT CARBOHYD 415 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:11320094, FT ECO:0000269|PubMed:33605212, ECO:0007744|PDB:7LKP, FT ECO:0007744|PDB:7LKZ" FT CARBOHYD 444 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:11320094, FT ECO:0000269|PubMed:33605212, ECO:0007744|PDB:7LKP, FT ECO:0007744|PDB:7LKZ" FT CARBOHYD 504 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:11320094, FT ECO:0000269|PubMed:33605212, ECO:0007744|PDB:7LKP" FT CARBOHYD 1469 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:11320094, FT ECO:0000269|PubMed:33605212, ECO:0007744|PDB:7LKP, FT ECO:0007744|PDB:7LKZ" FT CARBOHYD 1529 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:11320094, FT ECO:0000269|PubMed:33605212, ECO:0007744|PDB:7LKP, FT ECO:0007744|PDB:7LKZ" FT CARBOHYD 1588 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:11320094, FT ECO:0000269|PubMed:33605212, ECO:0007744|PDB:7LKP, FT ECO:0007744|PDB:7LKZ" FT CARBOHYD 1662 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:11320094, FT ECO:0000269|PubMed:33605212, ECO:0007744|PDB:7LKP, FT ECO:0007744|PDB:7LKZ" FT DISULFID 54..81 FT /evidence="ECO:0000269|PubMed:33605212, FT ECO:0007744|PDB:7LKP, ECO:0007744|PDB:7LKZ" FT DISULFID 75..324 FT /evidence="ECO:0000269|PubMed:33605212, FT ECO:0007744|PDB:7LKP, ECO:0007744|PDB:7LKZ" FT DISULFID 370..519 FT /evidence="ECO:0000269|PubMed:33605212, FT ECO:0007744|PDB:7LKP, ECO:0007744|PDB:7LKZ" FT DISULFID 641..1490 FT /note="Interchain" FT /evidence="ECO:0000269|PubMed:33605212, FT ECO:0007744|PDB:7LKP, ECO:0007744|PDB:7LKZ" FT DISULFID 1444..1455 FT /evidence="ECO:0000269|PubMed:33605212, FT ECO:0007744|PDB:7LKP, ECO:0007744|PDB:7LKZ" FT DISULFID 1488..1502 FT /evidence="ECO:0000269|PubMed:33605212, FT ECO:0007744|PDB:7LKP, ECO:0007744|PDB:7LKZ" FT VARIANT 11 FT /note="L -> P (in FFM; dbSNP:rs62645946)" FT /evidence="ECO:0000269|PubMed:9781034" FT /id="VAR_012493" FT VARIANT 13..15 FT /note="Missing (in STGD1)" FT /evidence="ECO:0000269|PubMed:11527935" FT /id="VAR_012494" FT VARIANT 14 FT /note="N -> K (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084833" FT VARIANT 18 FT /note="R -> P (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084834" FT VARIANT 18 FT /note="R -> W (in STGD1; dbSNP:rs121909205)" FT /evidence="ECO:0000269|PubMed:15192030, FT ECO:0000269|PubMed:23419329, ECO:0000269|PubMed:9503029, FT ECO:0000269|PubMed:9781034" FT /id="VAR_008398" FT VARIANT 21..2273 FT /note="Missing (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:19265867" FT /id="VAR_084835" FT VARIANT 24 FT /note="R -> H (in STGD1; uncertain significance; FT dbSNP:rs62645958)" FT /evidence="ECO:0000269|PubMed:23419329, FT ECO:0000269|PubMed:25346251, ECO:0000269|PubMed:26780318" FT /id="VAR_008399" FT VARIANT 53..2273 FT /note="Missing (in CORD3; uncertain significance; FT dbSNP:rs764744217)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084836" FT VARIANT 54 FT /note="C -> Y (in STGD1; dbSNP:rs150774447)" FT /evidence="ECO:0000269|PubMed:10612508, FT ECO:0000269|PubMed:10634594, ECO:0000269|PubMed:11527935, FT ECO:0000269|PubMed:23143460" FT /id="VAR_008400" FT VARIANT 55 FT /note="H -> R (in CORD3; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084837" FT VARIANT 58 FT /note="N -> K (in STGD1; dbSNP:rs61748524)" FT /evidence="ECO:0000269|PubMed:11527935" FT /id="VAR_012495" FT VARIANT 60 FT /note="A -> E (in STGD1)" FT /evidence="ECO:0000269|PubMed:10958763" FT /id="VAR_012496" FT VARIANT 60 FT /note="A -> T (in STGD1; dbSNP:rs61751411)" FT /evidence="ECO:0000269|PubMed:10958763" FT /id="VAR_012497" FT VARIANT 60 FT /note="A -> V (in STGD1; dbSNP:rs55732384)" FT /evidence="ECO:0000269|PubMed:10206579, FT ECO:0000269|PubMed:11527935" FT /id="VAR_008492" FT VARIANT 63 FT /note="S -> P (in CORD3; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084838" FT VARIANT 65 FT /note="G -> E (in STGD1 and CORD3; dbSNP:rs62654395)" FT /evidence="ECO:0000269|PubMed:10958761, FT ECO:0000269|PubMed:10958763, ECO:0000269|PubMed:11527935, FT ECO:0000269|PubMed:25346251" FT /id="VAR_008401" FT VARIANT 68 FT /note="P -> L (in STGD1; dbSNP:rs62654397)" FT /evidence="ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:19265867" FT /id="VAR_012498" FT VARIANT 68 FT /note="P -> R (in STGD1; dbSNP:rs62654397)" FT /evidence="ECO:0000269|PubMed:9973280" FT /id="VAR_012499" FT VARIANT 72 FT /note="G -> R (in STGD1; does not affect intracellular FT vesicle localization; does not affect solubility; FT significantly reduces N-Ret-PE binding; drastically reduces FT basal ATPase activity with little or no all trans retinal FT stimulation; dbSNP:rs61751412)" FT /evidence="ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:29847635" FT /id="VAR_012500" FT VARIANT 72 FT /note="G -> V (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084839" FT VARIANT 75 FT /note="C -> G (in STGD1; dbSNP:rs61748526)" FT /evidence="ECO:0000269|PubMed:9973280" FT /id="VAR_008402" FT VARIANT 77 FT /note="V -> E (in STGD1; dbSNP:rs61748527)" FT /evidence="ECO:0000269|PubMed:11527935" FT /id="VAR_012501" FT VARIANT 89..2273 FT /note="Missing (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:23419329" FT /id="VAR_085009" FT VARIANT 96 FT /note="N -> D (in STGD1; dbSNP:rs61748529)" FT /evidence="ECO:0000269|PubMed:10634594" FT /id="VAR_008403" FT VARIANT 96 FT /note="N -> H (in STGD1; uncertain significance; FT dbSNP:rs61748529)" FT /evidence="ECO:0000269|PubMed:10634594, FT ECO:0000269|PubMed:19265867" FT /id="VAR_008404" FT VARIANT 96 FT /note="N -> K (in STGD1; uncertain significance; FT dbSNP:rs886039297)" FT /evidence="ECO:0000269|PubMed:15192030, FT ECO:0000269|PubMed:19265867" FT /id="VAR_084840" FT VARIANT 97 FT /note="Y -> C (in STGD1; uncertain significance; FT dbSNP:rs755691060)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084841" FT VARIANT 100 FT /note="S -> P (in STGD1; highly decreased protein FT abundance; highly decreased ATPase activity; highly FT decreased phospholipid translocase activity; FT dbSNP:rs61748530)" FT /evidence="ECO:0000269|PubMed:24097981" FT /id="VAR_012502" FT VARIANT 107..2273 FT /note="Missing (in CORD3; uncertain significance; FT dbSNP:rs765429911)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084842" FT VARIANT 108 FT /note="D -> V (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:15192030" FT /id="VAR_084843" FT VARIANT 143 FT /note="P -> L (in STGD1; uncertain significance; FT dbSNP:rs62646860)" FT /evidence="ECO:0000269|PubMed:15192030" FT /id="VAR_084844" FT VARIANT 152 FT /note="R -> Q (in STGD1; dbSNP:rs62646862)" FT /evidence="ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:23143460" FT /id="VAR_012503" FT VARIANT 156 FT /note="I -> V (in STGD1; dbSNP:rs62646863)" FT /evidence="ECO:0000269|PubMed:10634594, FT ECO:0000269|PubMed:18977788" FT /id="VAR_012504" FT VARIANT 172 FT /note="G -> S (in STGD1; uncertain significance; FT dbSNP:rs61748532)" FT /evidence="ECO:0000269|PubMed:19265867" FT /id="VAR_084845" FT VARIANT 184 FT /note="S -> F (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:23143460" FT /id="VAR_084846" FT VARIANT 184 FT /note="S -> R (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:23143460" FT /id="VAR_084847" FT VARIANT 185..2273 FT /note="Missing (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084848" FT VARIANT 190 FT /note="Q -> H (in STGD1; dbSNP:rs281865397)" FT /evidence="ECO:0000269|PubMed:11527935" FT /id="VAR_012505" FT VARIANT 192 FT /note="A -> T (in STGD1; dbSNP:rs61748535)" FT /evidence="ECO:0000269|PubMed:11328725" FT /id="VAR_008405" FT VARIANT 206 FT /note="S -> R (in STGD1; reduced basal and FT retinal-stimulated ATP-hydrolysis; dbSNP:rs61748536)" FT /evidence="ECO:0000269|PubMed:10206579" FT /id="VAR_012506" FT VARIANT 212 FT /note="R -> C (in STGD1 and CORD3; common mutation in FT southern Europe; reduced ATP-binding capacity; FT dbSNP:rs61750200)" FT /evidence="ECO:0000269|PubMed:10711710, FT ECO:0000269|PubMed:10958761, ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:11385708, ECO:0000269|PubMed:18977788, FT ECO:0000269|PubMed:19265867, ECO:0000269|PubMed:23143460, FT ECO:0000269|PubMed:23419329, ECO:0000269|PubMed:24457364, FT ECO:0000269|PubMed:9503029, ECO:0000269|PubMed:9781034" FT /id="VAR_008406" FT VARIANT 212 FT /note="R -> H (in dbSNP:rs6657239)" FT /evidence="ECO:0000269|PubMed:10711710, FT ECO:0000269|PubMed:10958763, ECO:0000269|PubMed:11379881, FT ECO:0000269|PubMed:11384574, ECO:0000269|PubMed:11527935, FT ECO:0000269|PubMed:15192030" FT /id="VAR_012507" FT VARIANT 218..2273 FT /note="Missing (in CORD3; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084849" FT VARIANT 219..2273 FT /note="Missing (found in a patient with chorioretinal FT atrophy; uncertain significance)" FT /evidence="ECO:0000269|PubMed:23143460" FT /id="VAR_084850" FT VARIANT 220 FT /note="R -> C (in STGD1; dbSNP:rs61748538)" FT /evidence="ECO:0000269|PubMed:11328725" FT /id="VAR_012508" FT VARIANT 223 FT /note="K -> Q (in STGD1; uncertain significance; FT dbSNP:rs147619585)" FT /evidence="ECO:0000269|PubMed:15192030" FT /id="VAR_084851" FT VARIANT 224 FT /note="T -> M (in a breast cancer sample; somatic mutation; FT dbSNP:rs373540612)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035736" FT VARIANT 230 FT /note="C -> S (in STGD1; dbSNP:rs1057518767)" FT /evidence="ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:15192030" FT /id="VAR_012509" FT VARIANT 240 FT /note="I -> R (in STGD1; uncertain significance; FT dbSNP:rs1553195472)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084852" FT VARIANT 241 FT /note="E -> D (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:23419329" FT /id="VAR_085010" FT VARIANT 244 FT /note="L -> P (in STGD1; dbSNP:rs62646864)" FT /evidence="ECO:0000269|PubMed:11527935" FT /id="VAR_012510" FT VARIANT 245..2273 FT /note="Missing (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:15192030" FT /id="VAR_084853" FT VARIANT 246 FT /note="A -> T (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:15192030" FT /id="VAR_084854" FT VARIANT 247 FT /note="N -> S (in STGD1; dbSNP:rs62645950)" FT /evidence="ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:25346251" FT /id="VAR_012511" FT VARIANT 249 FT /note="D -> G (in STGD1; dbSNP:rs62646865)" FT /evidence="ECO:0000269|PubMed:9973280" FT /id="VAR_008407" FT VARIANT 290 FT /note="R -> W (in STGD1; uncertain significance; FT dbSNP:rs781716640)" FT /evidence="ECO:0000269|PubMed:23419329" FT /id="VAR_085011" FT VARIANT 291 FT /note="P -> L (in STGD1; uncertain significance; FT dbSNP:rs190540405)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084855" FT VARIANT 300 FT /note="T -> N (in STGD1; dbSNP:rs61748544)" FT /evidence="ECO:0000269|PubMed:10206579" FT /id="VAR_008408" FT VARIANT 309 FT /note="P -> R (in STGD1; dbSNP:rs61748545)" FT /evidence="ECO:0000269|PubMed:11527935" FT /id="VAR_012512" FT VARIANT 320 FT /note="S -> C (in CORD3; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084856" FT VARIANT 326..2273 FT /note="Missing (in STGD1; uncertain significance; FT dbSNP:rs747540967)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084857" FT VARIANT 328 FT /note="E -> V (in STGD1; dbSNP:rs61751419)" FT /evidence="ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:26780318" FT /id="VAR_012513" FT VARIANT 333 FT /note="R -> W (in STGD1; dbSNP:rs61748546)" FT /evidence="ECO:0000269|PubMed:11328725" FT /id="VAR_012514" FT VARIANT 336 FT /note="S -> C (in STGD1; dbSNP:rs61748547)" FT /evidence="ECO:0000269|PubMed:9973280" FT /id="VAR_008409" FT VARIANT 339..2273 FT /note="Missing (in CORD3; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084858" FT VARIANT 339 FT /note="W -> G (in FFM; dbSNP:rs61751420)" FT /evidence="ECO:0000269|PubMed:11379881" FT /id="VAR_012515" FT VARIANT 340 FT /note="Y -> D (in STGD1; dbSNP:rs61748548)" FT /evidence="ECO:0000269|PubMed:10746567" FT /id="VAR_008410" FT VARIANT 345 FT /note="Y -> S (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084859" FT VARIANT 380 FT /note="N -> K (in STGD1; dbSNP:rs61748549)" FT /evidence="ECO:0000269|PubMed:18977788" FT /id="VAR_012516" FT VARIANT 407 FT /note="A -> V (in STGD1 and CORD3; dbSNP:rs61751264)" FT /evidence="ECO:0000269|PubMed:10634594" FT /id="VAR_008411" FT VARIANT 410 FT /note="I -> T (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084860" FT VARIANT 415 FT /note="N -> K (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:19265867" FT /id="VAR_084861" FT VARIANT 418 FT /note="F -> S (in STGD1; uncertain significance; FT dbSNP:rs794726979)" FT /evidence="ECO:0000269|PubMed:23143460" FT /id="VAR_084862" FT VARIANT 423 FT /note="H -> R (in dbSNP:rs3112831)" FT /evidence="ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:11379881, ECO:0000269|PubMed:11384574, FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:12111378, FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:26780318" FT /id="VAR_012517" FT VARIANT 424 FT /note="V -> A (in STGD1 and RP19; uncertain significance)" FT /evidence="ECO:0000269|PubMed:10634594" FT /id="VAR_085012" FT VARIANT 431..2273 FT /note="Missing (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:25346251" FT /id="VAR_084863" FT VARIANT 440 FT /note="Y -> C (in CORD3; uncertain significance; FT dbSNP:rs770439859)" FT /evidence="ECO:0000269|PubMed:25346251" FT /id="VAR_084864" FT VARIANT 445 FT /note="S -> R (in STGD1; dbSNP:rs61748552)" FT /evidence="ECO:0000269|PubMed:10634594" FT /id="VAR_008412" FT VARIANT 455 FT /note="L -> M (in RP19; uncertain significance; FT dbSNP:rs764170051)" FT /evidence="ECO:0000269|PubMed:25346251" FT /id="VAR_084865" FT VARIANT 471 FT /note="E -> K (in ARMD2 and STGD1; uncertain significance; FT ATP-binding capacity and retinal stimulation as in FT wild-type; dbSNP:rs1800548)" FT /evidence="ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:23143460, ECO:0000269|PubMed:9295268" FT /id="VAR_008413" FT VARIANT 498 FT /note="D -> E (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:15192030" FT /id="VAR_084866" FT VARIANT 508 FT /note="R -> C (in STGD1; uncertain significance; FT dbSNP:rs138157885)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084867" FT VARIANT 511 FT /note="R -> C (in STGD1; uncertain significance; FT dbSNP:rs752786160)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084868" FT VARIANT 519 FT /note="C -> R (in STGD1; uncertain significance; FT dbSNP:rs1224959251)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084869" FT VARIANT 523 FT /note="D -> E (in STGD1; dbSNP:rs62646868)" FT /evidence="ECO:0000269|PubMed:9973280" FT /id="VAR_008414" FT VARIANT 525 FT /note="F -> C (in STGD1)" FT /evidence="ECO:0000269|PubMed:11527935" FT /id="VAR_012518" FT VARIANT 533..2273 FT /note="Missing (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084870" FT VARIANT 537 FT /note="R -> C (in STGD1; dbSNP:rs61748556)" FT /evidence="ECO:0000269|PubMed:11527935, FT ECO:0000269|PubMed:26780318" FT /id="VAR_012519" FT VARIANT 541 FT /note="L -> P (in STGD1, FFM and CORD3; reduced ATP-binding FT capacity; abolishes retinal-stimulated ATP hydrolysis; does FT not affect solubility; does not affect intracellular FT vesicle localization; significantly reduces substrate FT binding; drastically reduces basal ATPase activity with FT little or no substrate stimulation; dbSNP:rs61751392)" FT /evidence="ECO:0000269|PubMed:10206579, FT ECO:0000269|PubMed:10958761, ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:15192030, FT ECO:0000269|PubMed:19265867, ECO:0000269|PubMed:24457364, FT ECO:0000269|PubMed:25346251, ECO:0000269|PubMed:29847635, FT ECO:0000269|PubMed:9781034" FT /id="VAR_008415" FT VARIANT 548 FT /note="W -> R (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084871" FT VARIANT 549 FT /note="A -> P (in STGD1; dbSNP:rs61748557)" FT /evidence="ECO:0000269|PubMed:11527935" FT /id="VAR_012520" FT VARIANT 550 FT /note="G -> R (in STGD1; dbSNP:rs61748558)" FT /evidence="ECO:0000269|PubMed:11527935, FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:18977788, FT ECO:0000269|PubMed:26780318" FT /id="VAR_012521" FT VARIANT 552 FT /note="V -> I (in RP19; uncertain significance; FT dbSNP:rs145525174)" FT /evidence="ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:19028736, ECO:0000269|PubMed:25346251" FT /id="VAR_012522" FT VARIANT 572..2273 FT /note="Missing (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:19265867" FT /id="VAR_084872" FT VARIANT 572 FT /note="R -> P (in STGD1; dbSNP:rs61748559)" FT /evidence="ECO:0000269|PubMed:18977788" FT /id="VAR_008416" FT VARIANT 572 FT /note="R -> Q (in STGD1; dbSNP:rs61748559)" FT /evidence="ECO:0000269|PubMed:10746567, FT ECO:0000269|PubMed:10958763, ECO:0000269|PubMed:15192030" FT /id="VAR_008417" FT VARIANT 576 FT /note="D -> H (found in a patient with pattern dystrophy; FT uncertain significance; dbSNP:rs374224955)" FT /evidence="ECO:0000269|PubMed:23143460" FT /id="VAR_084873" FT VARIANT 593 FT /note="P -> L (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084874" FT VARIANT 602 FT /note="R -> Q (in STGD1; dbSNP:rs61749410)" FT /evidence="ECO:0000269|PubMed:11527935" FT /id="VAR_012523" FT VARIANT 602 FT /note="R -> W (in STGD1; dbSNP:rs61749409)" FT /evidence="ECO:0000269|PubMed:10634594, FT ECO:0000269|PubMed:18977788, ECO:0000269|PubMed:23419329, FT ECO:0000269|PubMed:24444108, ECO:0000269|PubMed:26780318" FT /id="VAR_008418" FT VARIANT 603 FT /note="Y -> C (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084875" FT VARIANT 605..2273 FT /note="Missing (in CORD3; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084876" FT VARIANT 607 FT /note="G -> R (in STGD1; dbSNP:rs61749412)" FT /evidence="ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:18977788, FT ECO:0000269|PubMed:25346251, ECO:0000269|PubMed:26780318" FT /id="VAR_012524" FT VARIANT 607 FT /note="G -> W (in STGD1; dbSNP:rs61749412)" FT /evidence="ECO:0000269|PubMed:11328725" FT /id="VAR_012525" FT VARIANT 608 FT /note="F -> I (in STGD1; moderately decreased protein FT abundance; highly decreased ATPase activity; highly FT decreased phospholipid translocase activity; FT dbSNP:rs61752398)" FT /evidence="ECO:0000269|PubMed:24097981" FT /id="VAR_008419" FT VARIANT 616 FT /note="E -> K (in STGD1; uncertain significance; FT dbSNP:rs1557787473)" FT /evidence="ECO:0000269|PubMed:19265867" FT /id="VAR_084877" FT VARIANT 635 FT /note="Q -> K (in STGD1; dbSNP:rs61749414)" FT /evidence="ECO:0000269|PubMed:10958763" FT /id="VAR_012526" FT VARIANT 636 FT /note="Q -> H (in STGD1; dbSNP:rs61752400)" FT /evidence="ECO:0000269|PubMed:9781034" FT /id="VAR_012527" FT VARIANT 636 FT /note="Q -> K (in CORD3; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084878" FT VARIANT 639..2273 FT /note="Missing (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:15192030" FT /id="VAR_084879" FT VARIANT 640 FT /note="P -> L (in STGD1; uncertain significance; FT dbSNP:rs760790294)" FT /evidence="ECO:0000269|PubMed:24457364" FT /id="VAR_085013" FT VARIANT 641 FT /note="C -> S (in STGD1; uncertain significance; FT dbSNP:rs61749416)" FT /evidence="ECO:0000269|PubMed:15192030" FT /id="VAR_084880" FT VARIANT 643 FT /note="V -> G (in CORD3; uncertain significance; FT dbSNP:rs61754024)" FT /evidence="ECO:0000269|PubMed:25346251, FT ECO:0000269|PubMed:9295268" FT /id="VAR_008420" FT VARIANT 643 FT /note="V -> M (in STGD1; dbSNP:rs61749417)" FT /evidence="ECO:0000269|PubMed:11527935, FT ECO:0000269|PubMed:23143460" FT /id="VAR_012528" FT VARIANT 645 FT /note="D -> N (in STGD1; dbSNP:rs61749418)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_008421" FT VARIANT 653 FT /note="R -> C (in STGD1; does not affect solubility; does FT not affect location in cytoplasmic vesicle; does not affect FT both basal and N-Ret-PE-stimulated ATPase activity; very FT low substrate binding; dbSNP:rs61749420)" FT /evidence="ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:18977788, FT ECO:0000269|PubMed:19265867, ECO:0000269|PubMed:23143460, FT ECO:0000269|PubMed:33375396" FT /id="VAR_012529" FT VARIANT 653 FT /note="R -> H (in STGD1; uncertain significance; does not FT affect solubility; does not affect location in cytoplasmic FT vesicle; does not affect both basal and N-Ret-PE-stimulated FT ATPase activity; very low substrate binding; FT dbSNP:rs141823837)" FT /evidence="ECO:0000269|PubMed:25346251, FT ECO:0000269|PubMed:26780318, ECO:0000269|PubMed:33375396" FT /id="VAR_084881" FT VARIANT 661 FT /note="L -> R (in CORD3; uncertain significance; severely FT decreases solubility; loss of cytoplasmic vesicle FT localization;decreases basal ATPase activity below 50%; FT loss of N-Ret-PE-induced stimulation in ATPase activity; FT very low substrate binding)" FT /evidence="ECO:0000269|PubMed:26780318, FT ECO:0000269|PubMed:33375396" FT /id="VAR_084882" FT VARIANT 681..2273 FT /note="Missing (found in a patient with macular dystrophy; FT uncertain significance)" FT /evidence="ECO:0000269|PubMed:25346251" FT /id="VAR_084883" FT VARIANT 686 FT /note="L -> S (in STGD1; severely decreases solubility; FT loss of cytoplasmic vesicle localization;decreases basal FT ATPase activity below 50%; loss of N-Ret-PE-induced FT stimulation in ATPase activity; very low substrate binding; FT dbSNP:rs61752402)" FT /evidence="ECO:0000269|PubMed:11385708, FT ECO:0000269|PubMed:33375396" FT /id="VAR_012530" FT VARIANT 690 FT /note="G -> V (in STGD1; uncertain significance; severely FT decreases solubility; loss of cytoplasmic vesicle FT localization; very low substrate binding)" FT /evidence="ECO:0000269|PubMed:15192030, FT ECO:0000269|PubMed:19265867, ECO:0000269|PubMed:33375396" FT /id="VAR_084884" FT VARIANT 700..2273 FT /note="Missing (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:15192030, FT ECO:0000269|PubMed:19265867" FT /id="VAR_084885" FT VARIANT 716 FT /note="T -> M (in STGD1; does not affect solubility; does FT not affect location in cytoplasmic vesicle; does not affect FT both basal and N-Ret-PE-stimulated ATPase activity; FT decreases N-Ret-PE binding in the range of 40-70%; FT dbSNP:rs61749426)" FT /evidence="ECO:0000269|PubMed:33375396" FT /id="VAR_012531" FT VARIANT 752 FT /note="S -> I (in dbSNP:rs1801369)" FT /id="VAR_014703" FT VARIANT 754 FT /note="F -> S (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084886" FT VARIANT 762 FT /note="A -> E (in ARMD2)" FT /evidence="ECO:0000269|PubMed:19028736" FT /id="VAR_067427" FT VARIANT 764 FT /note="C -> Y (in STGD1; does not affect solubility; does FT not affect location in cytoplasmic vesicle; does not affect FT both basal and N-Ret-PE-stimulated ATPase activity; FT decreases N-Ret-PE binding in the range of 40-70%; FT dbSNP:rs61749428)" FT /evidence="ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:33375396" FT /id="VAR_012532" FT VARIANT 765 FT /note="S -> N (in STGD1; severely decreases solubility; FT loss of cytoplasmic vesicle localization;decreases basal FT ATPase activity below 50%; loss of N-Ret-PE-induced FT stimulation in ATPase activity; very low substrate binding; FT dbSNP:rs61749429)" FT /evidence="ECO:0000269|PubMed:33375396" FT /id="VAR_012534" FT VARIANT 765 FT /note="S -> R (in STGD1; severely decreases solubility; FT loss of cytoplasmic vesicle localization;decreases basal FT ATPase activity below 50%; loss of N-Ret-PE-induced FT stimulation in ATPase activity; very low substrate binding; FT dbSNP:rs61752404)" FT /evidence="ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:33375396" FT /id="VAR_012533" FT VARIANT 767 FT /note="V -> D (in STGD1; also found in a patient with FT macular dystrophy; severely decreases solubility; loss of FT cytoplasmic vesicle localization; decreases basal ATPase FT activity below 50%; severely decreases N-Ret-PE-stimulated FT ATPase activity; very low substrate binding; FT dbSNP:rs61751395)" FT /evidence="ECO:0000269|PubMed:10711710, FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:15192030, FT ECO:0000269|PubMed:18977788, ECO:0000269|PubMed:19265867, FT ECO:0000269|PubMed:24457364, ECO:0000269|PubMed:25346251, FT ECO:0000269|PubMed:33375396" FT /id="VAR_012535" FT VARIANT 779..2273 FT /note="Missing (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:10634594" FT /id="VAR_085014" FT VARIANT 782..2273 FT /note="Missing (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:23143460" FT /id="VAR_084887" FT VARIANT 797 FT /note="L -> P (in STGD1; severely decreases solubility; FT loss of cytoplasmic vesicle localization;decreases basal FT ATPase activity below 50%; loss of N-Ret-PE-induced FT stimulation in ATPase activity; very low substrate binding; FT dbSNP:rs61749432)" FT /evidence="ECO:0000269|PubMed:11527935, FT ECO:0000269|PubMed:33375396" FT /id="VAR_012536" FT VARIANT 808..2273 FT /note="Missing (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084888" FT VARIANT 816 FT /note="G -> V (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084889" FT VARIANT 818 FT /note="G -> E (in STGD1; reduced ATP-binding capacity; FT moderately decreases solubility; loss of cytoplasmic FT vesicle localization; decreases ATPase activity between 50% FT and 80%; decreases modestly N-Ret-PE-stimulated ATPase; FT very low substrate binding; dbSNP:rs61750202)" FT /evidence="ECO:0000269|PubMed:23419329, FT ECO:0000269|PubMed:33375396" FT /id="VAR_008422" FT VARIANT 821 FT /note="W -> R (in STGD1; moderately decreases solubility; FT loss of cytoplasmic vesicle localization; decreases ATPase FT activity between 50% and 80%; decreases modestly FT N-Ret-PE-stimulated ATPase; very low substrate binding; FT dbSNP:rs61749433)" FT /evidence="ECO:0000269|PubMed:11527935, FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:19265867, FT ECO:0000269|PubMed:33375396" FT /id="VAR_008423" FT VARIANT 824 FT /note="I -> T (in STGD1; moderately decreases solubility; FT loss of cytoplasmic vesicle localization; decreases ATPase FT activity between 50% and 80%; decreases modestly FT N-Ret-PE-stimulated ATPase; very low substrate binding)" FT /evidence="ECO:0000269|PubMed:11527935, FT ECO:0000269|PubMed:33375396" FT /id="VAR_012537" FT VARIANT 840 FT /note="M -> R (in STGD1; uncertain significance; severely FT decreases solubility; loss of cytoplasmic vesicle FT localization;decreases basal ATPase activity below 50%; FT loss of N-Ret-PE-induced stimulation in ATPase activity; FT very low substrate binding)" FT /evidence="ECO:0000269|PubMed:19265867, FT ECO:0000269|PubMed:33375396" FT /id="VAR_084890" FT VARIANT 846 FT /note="D -> H (severely decreases solubility; loss of FT cytoplasmic vesicle localization; decreases basal ATPase FT activity below 50%; severely decreases N-Ret-PE-stimulated FT ATPase activity; very low substrate binding; FT dbSNP:rs61754027)" FT /evidence="ECO:0000269|PubMed:33375396, FT ECO:0000269|PubMed:9054934, ECO:0000269|PubMed:9295268" FT /id="VAR_008493" FT VARIANT 849 FT /note="V -> A (in STGD1; does not affect solubility; does FT not affect location in cytoplasmic vesicle; does not affect FT both basal and N-Ret-PE-stimulated ATPase activity; FT decreases N-Ret-PE binding in the range of 40-70%; FT dbSNP:rs61749435)" FT /evidence="ECO:0000269|PubMed:10206579, FT ECO:0000269|PubMed:33375396" FT /id="VAR_012538" FT VARIANT 851 FT /note="G -> D (in STGD1; highly reduced ATP-binding FT capacity; severely decreases solubility; loss of FT cytoplasmic vesicle localization;decreases basal ATPase FT activity below 50%; loss of N-Ret-PE-induced stimulation in FT ATPase activity; very low substrate binding; FT dbSNP:rs61749436)" FT /evidence="ECO:0000269|PubMed:33375396" FT /id="VAR_008424" FT VARIANT 854 FT /note="A -> T (in STGD1; does not affect solubility; does FT not affect location in cytoplasmic vesicle; decreases FT ATPase activity between 50% and 80%; decreases modestly FT N-Ret-PE-stimulated ATPase; decreases N-Ret-PE binding in FT the range of 40-70%; dbSNP:rs61749437)" FT /evidence="ECO:0000269|PubMed:33375396" FT /id="VAR_012539" FT VARIANT 863 FT /note="G -> A (in STGD1, FFM and CORD3; also found in a FT patient with bull's eye maculopathy; mild alteration FT probably leading to disease phenotype only in combination FT with a more severe allele; frequent mutation in northern FT Europe in linkage disequilibrium with the polymorphic FT variant Q-943; reduced ATP-binding capacity and FT retinal-stimulated ATP hydrolysis; significantly attenuates FT 11-cis-retinal binding; decreases about 80% the FT N-retinylidene-phosphatidylethanolamine transport activity; FT stimulates modestely the retinal-stimulated ATPase FT activity; does not affect ATP-independent FT N-retinylidene-phosphatidylethanolamine binding. Does not FT affect ATP-dependent release of FT N-retinylidene-phosphatidylethanolamine; significantly FT reduces phosphatidylethanolamine flippase activity; FT dbSNP:rs76157638)" FT /evidence="ECO:0000269|PubMed:10612508, FT ECO:0000269|PubMed:10634594, ECO:0000269|PubMed:10746567, FT ECO:0000269|PubMed:10958761, ECO:0000269|PubMed:11379881, FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:15192030, FT ECO:0000269|PubMed:22735453, ECO:0000269|PubMed:23143460, FT ECO:0000269|PubMed:23144455, ECO:0000269|PubMed:25346251, FT ECO:0000269|PubMed:30120214, ECO:0000269|PubMed:9295268" FT /id="VAR_008425" FT VARIANT 863 FT /note="Missing (in STGD1 and CORD3; reduced ATP-binding FT capacity and retinal-stimulated ATP hydrolysis)" FT /evidence="ECO:0000269|PubMed:10958761, FT ECO:0000269|PubMed:30120214" FT /id="VAR_012540" FT VARIANT 873 FT /note="F -> L (in STGD1; dbSNP:rs62642570)" FT /evidence="ECO:0000269|PubMed:11328725" FT /id="VAR_012541" FT VARIANT 876..2273 FT /note="Missing (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:15192030" FT /id="VAR_084891" FT VARIANT 897 FT /note="T -> I (in STGD1; dbSNP:rs61749440)" FT /evidence="ECO:0000269|PubMed:10711710, FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:18977788" FT /id="VAR_012542" FT VARIANT 901 FT /note="T -> A (in dbSNP:rs61754030)" FT /evidence="ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:18977788" FT /id="VAR_008426" FT VARIANT 914 FT /note="H -> R" FT /evidence="ECO:0000269|PubMed:10958763" FT /id="VAR_012543" FT VARIANT 931 FT /note="V -> M (in STGD1; dbSNP:rs58331765)" FT /evidence="ECO:0000269|PubMed:18977788, FT ECO:0000269|PubMed:19265867" FT /id="VAR_008427" FT VARIANT 935 FT /note="V -> A (in STGD1; dbSNP:rs61749444)" FT /evidence="ECO:0000269|PubMed:11527935" FT /id="VAR_012544" FT VARIANT 943 FT /note="R -> Q (risk factor for STGD1; risk factor for FT ARMD2; decreases 11-cis-Retinal binding affinity by FT 100-fold; dbSNP:rs1801581)" FT /evidence="ECO:0000269|PubMed:10634594, FT ECO:0000269|PubMed:10746567, ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:11379881, ECO:0000269|PubMed:11385708, FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:11594993, FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:23143460, FT ECO:0000269|PubMed:23144455, ECO:0000269|PubMed:23419329, FT ECO:0000269|PubMed:9054934, ECO:0000269|PubMed:9295268, FT ECO:0000269|Ref.5" FT /id="VAR_008428" FT VARIANT 943 FT /note="R -> W (in STGD1 and FFM; dbSNP:rs61749446)" FT /evidence="ECO:0000269|PubMed:11379881, FT ECO:0000269|PubMed:11527935" FT /id="VAR_012545" FT VARIANT 954 FT /note="Y -> D (in STGD1; uncertain significance; FT dbSNP:rs61749447)" FT /evidence="ECO:0000269|PubMed:15192030" FT /id="VAR_084892" FT VARIANT 957 FT /note="Q -> R (in STGD1; dbSNP:rs61749448)" FT /evidence="ECO:0000269|PubMed:10090887" FT /id="VAR_008429" FT VARIANT 959 FT /note="T -> I (in STGD1; moderately decreased protein FT abundance; highly decreased ATPase activity; highly FT decreased phospholipid translocase activity; FT dbSNP:rs61752409)" FT /evidence="ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:24097981" FT /id="VAR_012546" FT VARIANT 965 FT /note="N -> S (in STGD1; reduced retinal-stimulated ATP FT hydrolysis; moderately decreased protein abundance; highly FT decreased ATPase activity; highly decreased phospholipid FT translocase activity; decreases about 60% the FT N-retinylidene-phosphatidylethanolamine transfer activity; FT stimulates modestly the retinal-stimulated ATPase activity; FT does not affect ATP-independent FT N-retinylidene-phosphatidylethanolamine binding; does not FT affect ATP-dependent release of FT N-retinylidene-phosphatidylethanolamine; significantly FT reduces phosphatidylethanolamine flippase activity; FT dbSNP:rs201471607)" FT /evidence="ECO:0000269|PubMed:10746567, FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:18977788, FT ECO:0000269|PubMed:19265867, ECO:0000269|PubMed:22735453, FT ECO:0000269|PubMed:23419329, ECO:0000269|PubMed:24097981, FT ECO:0000269|PubMed:26780318" FT /id="VAR_008430" FT VARIANT 965 FT /note="N -> Y (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084893" FT VARIANT 970 FT /note="T -> P (in STGD1; uncertain significance; FT dbSNP:rs1570377849)" FT /evidence="ECO:0000269|PubMed:19265867" FT /id="VAR_084894" FT VARIANT 971 FT /note="T -> N (in STGD1; highly reduced ATP-binding FT capacity; abolishes retinal-stimulated ATP hydrolysis; FT dbSNP:rs61749450)" FT /evidence="ECO:0000269|PubMed:11328725" FT /id="VAR_012547" FT VARIANT 972 FT /note="T -> N (in STGD1; uncertain significance; FT dbSNP:rs61749451)" FT /evidence="ECO:0000269|PubMed:11594993" FT /id="VAR_012548" FT VARIANT 973 FT /note="L -> S (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084895" FT VARIANT 974 FT /note="S -> P (in STGD1; dbSNP:rs281865400)" FT /evidence="ECO:0000269|PubMed:10206579" FT /id="VAR_012549" FT VARIANT 977 FT /note="T -> P (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:19265867" FT /id="VAR_084896" FT VARIANT 978 FT /note="G -> C (in STGD1; dbSNP:rs61749452)" FT /id="VAR_008431" FT VARIANT 978 FT /note="G -> D (in STGD1; uncertain significance; FT dbSNP:rs61749453)" FT /evidence="ECO:0000269|PubMed:15192030, FT ECO:0000269|PubMed:19265867" FT /id="VAR_084897" FT VARIANT 989 FT /note="V -> A (in STGD1; dbSNP:rs61749454)" FT /evidence="ECO:0000269|PubMed:11527935, FT ECO:0000269|PubMed:23143460" FT /id="VAR_012550" FT VARIANT 991 FT /note="G -> R (in FFM and STGD1; dbSNP:rs61749455)" FT /evidence="ECO:0000269|PubMed:11379881, FT ECO:0000269|PubMed:23143460" FT /id="VAR_012551" FT VARIANT 1014 FT /note="L -> R (in STGD1; dbSNP:rs61749456)" FT /evidence="ECO:0000269|PubMed:23419329" FT /id="VAR_012552" FT VARIANT 1019 FT /note="T -> A (in STGD1; dbSNP:rs61749457)" FT /evidence="ECO:0000269|PubMed:11328725" FT /id="VAR_012553" FT VARIANT 1019 FT /note="T -> M (in STGD1; dbSNP:rs201855602)" FT /evidence="ECO:0000269|PubMed:18977788, FT ECO:0000269|PubMed:19265867, ECO:0000269|PubMed:23143460, FT ECO:0000269|PubMed:26780318, ECO:0000269|PubMed:9781034" FT /id="VAR_012554" FT VARIANT 1022 FT /note="E -> G (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084898" FT VARIANT 1022 FT /note="E -> K (in STGD1; uncertain significance; FT dbSNP:rs61749459)" FT /evidence="ECO:0000269|PubMed:15192030, FT ECO:0000269|PubMed:23143460" FT /id="VAR_012555" FT VARIANT 1029..2273 FT /note="Missing (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:25346251" FT /id="VAR_084899" FT VARIANT 1031 FT /note="K -> E (in STGD1; dbSNP:rs61750060)" FT /evidence="ECO:0000269|PubMed:11328725" FT /id="VAR_012556" FT VARIANT 1036 FT /note="E -> K (in STGD1; dbSNP:rs61750061)" FT /evidence="ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:26780318" FT /id="VAR_008432" FT VARIANT 1038 FT /note="A -> V (in STGD1, FFM and CORD3; frequent mutation; FT reduced ATP-binding and retinal-stimulated ATP hydrolysis; FT decreases solubility at 70%; does not affect intracellular FT vesicle localization; significantly reduces substrate FT binding in the absence of ATP; reduces basal ATPase FT activity; dbSNP:rs61751374)" FT /evidence="ECO:0000269|PubMed:10206579, FT ECO:0000269|PubMed:10711710, ECO:0000269|PubMed:10746567, FT ECO:0000269|PubMed:10958761, ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:11379881, ECO:0000269|PubMed:11527935, FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:19265867, FT ECO:0000269|PubMed:24457364, ECO:0000269|PubMed:25346251, FT ECO:0000269|PubMed:29847635, ECO:0000269|PubMed:9781034" FT /id="VAR_008433" FT VARIANT 1050 FT /note="G -> D (in STGD1; uncertain significance; FT dbSNP:rs61750062)" FT /evidence="ECO:0000269|PubMed:15192030" FT /id="VAR_084900" FT VARIANT 1055 FT /note="R -> W (in STGD1; dbSNP:rs61752412)" FT /evidence="ECO:0000269|PubMed:11385708, FT ECO:0000269|PubMed:19265867" FT /id="VAR_012557" FT VARIANT 1063 FT /note="S -> P (in STGD1; dbSNP:rs61752413)" FT /evidence="ECO:0000269|PubMed:10958763" FT /id="VAR_012558" FT VARIANT 1071 FT /note="S -> L (in STGD1; reduced ATP-binding capacity; FT dbSNP:rs61750065)" FT /evidence="ECO:0000269|PubMed:9973280" FT /id="VAR_008434" FT VARIANT 1072 FT /note="V -> A (in STGD1)" FT /evidence="ECO:0000269|PubMed:9973280" FT /id="VAR_008435" FT VARIANT 1074 FT /note="I -> L (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084901" FT VARIANT 1078 FT /note="G -> E (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:19265867" FT /id="VAR_084902" FT VARIANT 1087 FT /note="E -> D (in STGD1; dbSNP:rs61752416)" FT /evidence="ECO:0000269|PubMed:10958763" FT /id="VAR_012559" FT VARIANT 1087 FT /note="E -> K (in STGD1; dbSNP:rs61751398)" FT /evidence="ECO:0000269|PubMed:10711710, FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:19265867" FT /id="VAR_008436" FT VARIANT 1091 FT /note="G -> E (in FFM and STGD1; decreases solubilized at FT 70%; does not affect intracellular vesicle localization; FT does not affect substrate binding; drastically reduces FT basal ATPase activity with little or no substrate FT stimulation; dbSNP:rs61752417)" FT /evidence="ECO:0000269|PubMed:29847635, FT ECO:0000269|PubMed:9781034" FT /id="VAR_012560" FT VARIANT 1094 FT /note="P -> T (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084903" FT VARIANT 1097 FT /note="R -> C (in STGD1)" FT /evidence="ECO:0000269|PubMed:10958763" FT /id="VAR_012561" FT VARIANT 1097 FT /note="R -> S (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:23143460" FT /id="VAR_084904" FT VARIANT 1098 FT /note="R -> C (in STGD1; uncertain significance; FT dbSNP:rs756840095)" FT /evidence="ECO:0000269|PubMed:15192030, FT ECO:0000269|PubMed:19265867" FT /id="VAR_084905" FT VARIANT 1099..2273 FT /note="Missing (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:19265867" FT /id="VAR_084906" FT VARIANT 1099 FT /note="S -> P (in STGD1; uncertain significance; FT dbSNP:rs61750119)" FT /evidence="ECO:0000269|PubMed:15192030" FT /id="VAR_084907" FT VARIANT 1102 FT /note="D -> Y (in dbSNP:rs138641544)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084908" FT VARIANT 1108 FT /note="R -> C (in STGD1 and FFM; reduced ATP-binding FT capacity; dbSNP:rs61750120)" FT /evidence="ECO:0000269|PubMed:10206579, FT ECO:0000269|PubMed:10958763, ECO:0000269|PubMed:11379881, FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:15192030, FT ECO:0000269|PubMed:19265867, ECO:0000269|PubMed:23143460, FT ECO:0000269|PubMed:24457364, ECO:0000269|PubMed:9781034" FT /id="VAR_012562" FT VARIANT 1108 FT /note="R -> H (in STGD1; dbSNP:rs61750121)" FT /evidence="ECO:0000269|PubMed:15192030, FT ECO:0000269|PubMed:18977788, ECO:0000269|PubMed:26780318" FT /id="VAR_012563" FT VARIANT 1108 FT /note="R -> L (in STGD1; dbSNP:rs61750121)" FT /evidence="ECO:0000269|PubMed:11527935" FT /id="VAR_012564" FT VARIANT 1112 FT /note="T -> N (in STGD1; dbSNP:rs61750122)" FT /evidence="ECO:0000269|PubMed:10090887" FT /id="VAR_008437" FT VARIANT 1122 FT /note="E -> K (in STGD1 and CORD3; dbSNP:rs61751399)" FT /evidence="ECO:0000269|PubMed:10958761, FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:23143460, FT ECO:0000269|PubMed:26780318" FT /id="VAR_008438" FT VARIANT 1129 FT /note="R -> C (in STGD1; may predispose to develop retinal FT toxicity after treatment with chloroquine and FT hydroxychloroquine; dbSNP:rs779426136)" FT /evidence="ECO:0000269|PubMed:11384574" FT /id="VAR_012565" FT VARIANT 1129 FT /note="R -> L (in ARMD2 and STGD1; also found in patients FT with fundus flavimaculatus; reduced ATP-binding capacity; FT dbSNP:rs1801269)" FT /evidence="ECO:0000269|PubMed:15192030, FT ECO:0000269|PubMed:18977788, ECO:0000269|PubMed:19028736, FT ECO:0000269|PubMed:23143460, ECO:0000269|PubMed:23419329, FT ECO:0000269|PubMed:9295268" FT /id="VAR_008439" FT VARIANT 1130 FT /note="I -> T (in STGD1; uncertain significance; FT dbSNP:rs1064793010)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084909" FT VARIANT 1140 FT /note="C -> W (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084910" FT VARIANT 1145 FT /note="L -> H (in CORD3; uncertain significance)" FT /evidence="ECO:0000269|PubMed:25346251" FT /id="VAR_084911" FT VARIANT 1148 FT /note="K -> T" FT /evidence="ECO:0000269|PubMed:11379881" FT /id="VAR_012566" FT VARIANT 1159 FT /note="L -> S (in STGD1; uncertain significance; FT dbSNP:rs1340749727)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084912" FT VARIANT 1161 FT /note="R -> H (in STGD1; uncertain significance; FT dbSNP:rs768278935)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084913" FT VARIANT 1177..2273 FT /note="Missing (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:19265867" FT /id="VAR_084914" FT VARIANT 1183 FT /note="G -> C (in CORD3; uncertain significance; FT dbSNP:rs75267647)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084915" FT VARIANT 1201 FT /note="L -> R (in STGD1; may predispose to develop retinal FT toxicity after treatment with chloroquine and FT hydroxychloroquine; dbSNP:rs61750126)" FT /evidence="ECO:0000269|PubMed:11384574, FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:23143460" FT /id="VAR_008440" FT VARIANT 1203 FT /note="G -> D (in STGD1)" FT /evidence="ECO:0000269|PubMed:15192030" FT /id="VAR_084916" FT VARIANT 1203 FT /note="G -> E (in CORD3; uncertain significance; FT dbSNP:rs146786552)" FT /evidence="ECO:0000269|PubMed:25346251" FT /id="VAR_084917" FT VARIANT 1203 FT /note="G -> R (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:15192030" FT /id="VAR_084918" FT VARIANT 1204 FT /note="D -> N (in STGD1; uncertain significance; FT dbSNP:rs61750127)" FT /evidence="ECO:0000269|PubMed:15192030" FT /id="VAR_008441" FT VARIANT 1209 FT /note="M -> T (in dbSNP:rs76258939)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084919" FT VARIANT 1250 FT /note="L -> P (in STGD1; dbSNP:rs61750128)" FT /evidence="ECO:0000269|PubMed:11328725" FT /id="VAR_012567" FT VARIANT 1253 FT /note="T -> M (in FFM; uncertain significance; FT dbSNP:rs61752424)" FT /evidence="ECO:0000269|PubMed:11385708" FT /id="VAR_012568" FT VARIANT 1300..2273 FT /note="Missing (in STGD1; uncertain significance; FT dbSNP:rs61752427)" FT /evidence="ECO:0000269|PubMed:15192030, FT ECO:0000269|PubMed:26780318" FT /id="VAR_084920" FT VARIANT 1300 FT /note="R -> Q (in STGD1; uncertain significance; FT dbSNP:rs61750129)" FT /evidence="ECO:0000269|PubMed:11527935, FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:25346251" FT /id="VAR_012569" FT VARIANT 1314 FT /note="P -> T (in dbSNP:rs61754041)" FT /evidence="ECO:0000269|PubMed:11328725" FT /id="VAR_008442" FT VARIANT 1332..2273 FT /note="Missing (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:19265867" FT /id="VAR_084921" FT VARIANT 1368 FT /note="R -> C (in CORD3; uncertain significance; FT dbSNP:rs1183074086)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084922" FT VARIANT 1371 FT /note="K -> N (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084923" FT VARIANT 1380 FT /note="P -> L (in STGD1; also found in a patient with FT chorioretinal atrophy; reduced ATP-binding capacity; FT moderately decreases solubility; loss of cytoplasmic FT vesicle localization; decreases ATPase activity between 50% FT and 80%; decreases modestly N-Ret-PE-stimulated ATPase; FT dbSNP:rs61750130)" FT /evidence="ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:15192030, FT ECO:0000269|PubMed:18977788, ECO:0000269|PubMed:19265867, FT ECO:0000269|PubMed:23143460, ECO:0000269|PubMed:23419329, FT ECO:0000269|PubMed:33375396" FT /id="VAR_008443" FT VARIANT 1388 FT /note="L -> P (in STGD1; dbSNP:rs61750131)" FT /evidence="ECO:0000269|PubMed:11527935" FT /id="VAR_012570" FT VARIANT 1399 FT /note="E -> K (in STGD1; does not affect solubility; does FT not affect location in cytoplasmic vesicle; does not affect FT both basal and N-Ret-PE-stimulated ATPase activity; FT increases N-Ret-PE binding; dbSNP:rs62642573)" FT /evidence="ECO:0000269|PubMed:10711710, FT ECO:0000269|PubMed:10958763, ECO:0000269|PubMed:33375396" FT /id="VAR_012571" FT VARIANT 1406 FT /note="H -> Y (in STGD1; dbSNP:rs61750133)" FT /evidence="ECO:0000269|PubMed:9973280" FT /id="VAR_008444" FT VARIANT 1408..2273 FT /note="Missing (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:19265867" FT /id="VAR_084924" FT VARIANT 1408 FT /note="W -> L (in STGD1; does not affect secondary FT structure; decreases structural flexibility; significantly FT decreases all-trans-retinal binding; dbSNP:rs61750134)" FT /evidence="ECO:0000269|PubMed:10206579, FT ECO:0000269|PubMed:20404325" FT /id="VAR_008445" FT VARIANT 1408 FT /note="W -> R (in STGD1; reduced retinal-stimulated ATP FT hydrolysis; dbSNP:rs61750135)" FT /evidence="ECO:0000269|PubMed:11527935, FT ECO:0000269|PubMed:24457364" FT /id="VAR_008446" FT VARIANT 1416 FT /note="Missing (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:23419329" FT /id="VAR_085015" FT VARIANT 1428 FT /note="T -> M (in dbSNP:rs1800549)" FT /evidence="ECO:0000269|PubMed:26780318, FT ECO:0000269|PubMed:9295268" FT /id="VAR_008447" FT VARIANT 1429 FT /note="V -> A (in STGD1; dbSNP:rs61752432)" FT /evidence="ECO:0000269|PubMed:10634594" FT /id="VAR_008448" FT VARIANT 1430 FT /note="L -> P (in STGD1)" FT /evidence="ECO:0000269|PubMed:10958763" FT /id="VAR_012572" FT VARIANT 1433 FT /note="V -> I (in STGD1; dbSNP:rs56357060)" FT /evidence="ECO:0000269|PubMed:18977788, FT ECO:0000269|PubMed:19265867" FT /id="VAR_008449" FT VARIANT 1439 FT /note="G -> D (in STGD1; dbSNP:rs61750140)" FT /evidence="ECO:0000269|PubMed:9973280" FT /id="VAR_008450" FT VARIANT 1440 FT /note="F -> S (in STGD1; dbSNP:rs61750141)" FT /evidence="ECO:0000269|PubMed:9973280" FT /id="VAR_008451" FT VARIANT 1440 FT /note="F -> V (in STGD1; dbSNP:rs61752433)" FT /evidence="ECO:0000269|PubMed:10958763" FT /id="VAR_012573" FT VARIANT 1442 FT /note="N -> K (in STGD1; uncertain significance; FT dbSNP:rs762150575)" FT /evidence="ECO:0000269|PubMed:23143460" FT /id="VAR_084925" FT VARIANT 1443 FT /note="R -> H (in STGD1; loss of the majority of FT alpha-helical secondary structure; does not bind FT all-trans-retinal; does not affect conformational change; FT dbSNP:rs61750142)" FT /evidence="ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:20404325, ECO:0000269|PubMed:23419329" FT /id="VAR_012574" FT VARIANT 1453..2273 FT /note="Missing (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084926" FT VARIANT 1461..2273 FT /note="Missing (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:19265867" FT /id="VAR_084927" FT VARIANT 1479..2273 FT /note="Missing (in STGD1 and CORD3; uncertain significance; FT dbSNP:rs61752434)" FT /evidence="ECO:0000269|PubMed:19265867, FT ECO:0000269|PubMed:26780318" FT /id="VAR_084928" FT VARIANT 1484 FT /note="P -> S (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:19265867" FT /id="VAR_084929" FT VARIANT 1486 FT /note="P -> L (in STGD1; dbSNP:rs61750145)" FT /evidence="ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:18977788, FT ECO:0000269|PubMed:23143460" FT /id="VAR_008452" FT VARIANT 1488 FT /note="C -> F (in STGD1; dbSNP:rs61750147)" FT /evidence="ECO:0000269|PubMed:11328725" FT /id="VAR_012575" FT VARIANT 1488 FT /note="C -> R (in STGD1 and FFM; also found in a patient FT with chorioretinal atrophy; reduced retinal-stimulated ATP FT hydrolysis; does not affect secondary structure; oss of FT structural flexibility; significantly decreases FT all-trans-retinal binding; dbSNP:rs61750146)" FT /evidence="ECO:0000269|PubMed:10206579, FT ECO:0000269|PubMed:11379881, ECO:0000269|PubMed:11527935, FT ECO:0000269|PubMed:20404325, ECO:0000269|PubMed:23143460" FT /id="VAR_008453" FT VARIANT 1488 FT /note="C -> Y (in STGD1; dbSNP:rs61750147)" FT /evidence="ECO:0000269|PubMed:10958763" FT /id="VAR_012576" FT VARIANT 1490 FT /note="C -> Y (in STGD1 and CORD3; reduced FT retinal-stimulated ATP hydrolysis; dbSNP:rs61751402)" FT /evidence="ECO:0000269|PubMed:10958761, FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:15192030, FT ECO:0000269|PubMed:18977788, ECO:0000269|PubMed:23143460" FT /id="VAR_008454" FT VARIANT 1503 FT /note="P -> L (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084930" FT VARIANT 1508 FT /note="G -> C (in FFM)" FT /evidence="ECO:0000269|PubMed:9781034" FT /id="VAR_012577" FT VARIANT 1511 FT /note="P -> H (in STGD1; uncertain significance; FT dbSNP:rs886046564)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084931" FT VARIANT 1512 FT /note="P -> R (in STGD1; uncertain significance; FT dbSNP:rs61750150)" FT /evidence="ECO:0000269|PubMed:15192030" FT /id="VAR_084932" FT VARIANT 1513 FT /note="Q -> R (in STGD1; dbSNP:rs281865402)" FT /evidence="ECO:0000269|PubMed:11328725" FT /id="VAR_012578" FT VARIANT 1517 FT /note="R -> S (in ARMD2; dbSNP:rs1800550)" FT /evidence="ECO:0000269|PubMed:9295268" FT /id="VAR_008455" FT VARIANT 1525 FT /note="L -> P (in STGD1; dbSNP:rs61750151)" FT /evidence="ECO:0000269|PubMed:11328725" FT /id="VAR_012579" FT VARIANT 1526 FT /note="T -> M (in STGD1; also found in a patient with FT chorioretinal atrophy; reduced retinal-stimulated ATP FT hydrolysis; dbSNP:rs61750152)" FT /evidence="ECO:0000269|PubMed:11527935, FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:19265867, FT ECO:0000269|PubMed:23143460, ECO:0000269|PubMed:26780318" FT /id="VAR_008456" FT VARIANT 1532 FT /note="D -> N (in STGD1; dbSNP:rs62642574)" FT /evidence="ECO:0000269|PubMed:11527935" FT /id="VAR_008457" FT VARIANT 1537 FT /note="T -> M (in STGD1; moderately decreased protein FT abundance; moderately decreased ATPase activity; moderately FT decreased phospholipid translocase activity; FT dbSNP:rs62642575)" FT /evidence="ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:24097981, ECO:0000269|PubMed:25346251" FT /id="VAR_012580" FT VARIANT 1551 FT /note="Missing (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:23419329" FT /id="VAR_085016" FT VARIANT 1556 FT /note="R -> T (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:23419329" FT /id="VAR_085017" FT VARIANT 1557 FT /note="Y -> C (found in a patient with chorioretinal FT atrophy; uncertain significance; dbSNP:rs1401716074)" FT /evidence="ECO:0000269|PubMed:23143460" FT /id="VAR_084933" FT VARIANT 1562 FT /note="I -> T (in STGD1, FFM, ARMD2 and CORD3; uncertain FT significance; dbSNP:rs1762111)" FT /evidence="ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:11379881, ECO:0000269|PubMed:11527935, FT ECO:0000269|PubMed:23143460, ECO:0000269|PubMed:9295268" FT /id="VAR_008458" FT VARIANT 1572 FT /note="T -> M (in dbSNP:rs185093512)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084934" FT VARIANT 1578 FT /note="G -> R (in ARMD2; dbSNP:rs1800551)" FT /evidence="ECO:0000269|PubMed:9295268" FT /id="VAR_008459" FT VARIANT 1591 FT /note="G -> R (in STGD1; uncertain significance; also found FT in a patient with macular dystrophy; uncertain FT significance; dbSNP:rs113106943)" FT /evidence="ECO:0000269|PubMed:25346251, FT ECO:0000269|PubMed:26780318" FT /id="VAR_084935" FT VARIANT 1598 FT /note="A -> D (in CORD3 and STGD1; uncertain significance; FT dbSNP:rs61750155)" FT /evidence="ECO:0000269|PubMed:10958761, FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:19265867, FT ECO:0000269|PubMed:23143460" FT /id="VAR_012581" FT VARIANT 1618..2273 FT /note="Missing" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084936" FT VARIANT 1623 FT /note="G -> V (in dbSNP:rs1571257969)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084937" FT VARIANT 1631 FT /note="L -> P (in STGD1; dbSNP:rs61750158)" FT /evidence="ECO:0000269|PubMed:10090887" FT /id="VAR_008460" FT VARIANT 1637 FT /note="A -> T (in dbSNP:rs61754056)" FT /evidence="ECO:0000269|PubMed:11527935" FT /id="VAR_012582" FT VARIANT 1640 FT /note="R -> Q (in STGD1, FFM and CORD3; dbSNP:rs61751403)" FT /evidence="ECO:0000269|PubMed:10711710, FT ECO:0000269|PubMed:11379881, ECO:0000269|PubMed:11527935, FT ECO:0000269|PubMed:18977788, ECO:0000269|PubMed:24457364, FT ECO:0000269|PubMed:26780318" FT /id="VAR_012583" FT VARIANT 1640 FT /note="R -> W (in STGD1 and CORD3; dbSNP:rs61751404)" FT /evidence="ECO:0000269|PubMed:10634594, FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:18977788, FT ECO:0000269|PubMed:24457364, ECO:0000269|PubMed:25346251, FT ECO:0000269|PubMed:9781034" FT /id="VAR_008461" FT VARIANT 1650..2273 FT /note="Missing (in CORD3; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084938" FT VARIANT 1652..2273 FT /note="Missing (in STGD1 and FFM; uncertain significance)" FT /evidence="ECO:0000269|PubMed:15192030, FT ECO:0000269|PubMed:26780318" FT /id="VAR_084939" FT VARIANT 1652 FT /note="Y -> D (in STGD1; dbSNP:rs61750560)" FT /evidence="ECO:0000269|PubMed:10206579" FT /id="VAR_008462" FT VARIANT 1681..1685 FT /note="Missing (in STGD1; highly reduced ATP-binding FT capacity)" FT /evidence="ECO:0000269|PubMed:23419329" FT /id="VAR_012584" FT VARIANT 1689 FT /note="S -> P (in STGD1; dbSNP:rs61753020)" FT /evidence="ECO:0000269|PubMed:10958763" FT /id="VAR_012585" FT VARIANT 1693 FT /note="V -> I (in STGD1; dbSNP:rs61750563)" FT /evidence="ECO:0000269|PubMed:11328725" FT /id="VAR_012586" FT VARIANT 1696 FT /note="S -> N (in STGD1; uncertain significance; does not FT affect solubility; does not affect location in cytoplasmic FT vesicle; does not affect both basal and N-Ret-PE-stimulated FT ATPase activity; increases N-Ret-PE binding; FT dbSNP:rs61750564)" FT /evidence="ECO:0000269|PubMed:19265867, FT ECO:0000269|PubMed:33375396" FT /id="VAR_008463" FT VARIANT 1703 FT /note="Q -> E (in STGD1; uncertain significance; does not FT affect solubility; does not affect location in cytoplasmic FT vesicle;decreases basal ATPase activity below 50%; loss of FT N-Ret-PE-induced stimulation in ATPase activity; FT dbSNP:rs61750565)" FT /evidence="ECO:0000269|PubMed:10634594, FT ECO:0000269|PubMed:33375396" FT /id="VAR_085018" FT VARIANT 1703 FT /note="Q -> K (in STGD1; moderately decreases solubility; FT loss of cytoplasmic vesicle localization;decreases basal FT ATPase activity below 50%; loss of N-Ret-PE-induced FT stimulation in ATPase activity)" FT /evidence="ECO:0000269|PubMed:33375396" FT /id="VAR_008464" FT VARIANT 1705 FT /note="R -> L (in STGD1; moderately decreases solubility; FT loss of cytoplasmic vesicle localization; decreases ATPase FT activity between 50% and 80%; decreases modestly FT N-Ret-PE-stimulated ATPase; dbSNP:rs61753021)" FT /evidence="ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:33375396" FT /id="VAR_012587" FT VARIANT 1705 FT /note="R -> Q (in STGD1; uncertain significance; FT dbSNP:rs61753021)" FT /evidence="ECO:0000269|PubMed:23419329" FT /id="VAR_085019" FT VARIANT 1724..2273 FT /note="Missing (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084940" FT VARIANT 1724 FT /note="W -> C (in ARMD2)" FT /evidence="ECO:0000269|PubMed:19028736" FT /id="VAR_067428" FT VARIANT 1729 FT /note="L -> P (in STGD1; dbSNP:rs61750567)" FT /evidence="ECO:0000269|PubMed:10206579" FT /id="VAR_008465" FT VARIANT 1733 FT /note="M -> T (in STGD1; dbSNP:rs765563320)" FT /evidence="ECO:0000269|PubMed:10958763" FT /id="VAR_012588" FT VARIANT 1736 FT /note="S -> P (in STGD1; dbSNP:rs61750568)" FT /evidence="ECO:0000269|PubMed:11328725" FT /id="VAR_012589" FT VARIANT 1748 FT /note="G -> R (in STGD1; dbSNP:rs61753025)" FT /evidence="ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:18977788" FT /id="VAR_012590" FT VARIANT 1754 FT /note="Y -> D (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:23143460" FT /id="VAR_084941" FT VARIANT 1761..1763 FT /note="Missing (in STGD1; highly reduced ATP-binding FT capacity)" FT /evidence="ECO:0000269|PubMed:9973280" FT /id="VAR_012591" FT VARIANT 1762 FT /note="A -> D (in STGD1; uncertain significance; FT dbSNP:rs121909206)" FT /evidence="ECO:0000269|PubMed:15192030" FT /id="VAR_084942" FT VARIANT 1763 FT /note="L -> P (in STGD1; dbSNP:rs61753028)" FT /evidence="ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:25346251" FT /id="VAR_012592" FT VARIANT 1773 FT /note="A -> E (found in a patient with chorioretinal FT atrophy; uncertain significance; severely decreases FT solubility; loss of cytoplasmic vesicle localization; FT decreases basal ATPase activity below 50%; loss of FT N-Ret-PE-induced stimulation in ATPase activity)" FT /evidence="ECO:0000269|PubMed:23143460, FT ECO:0000269|PubMed:33375396" FT /id="VAR_084943" FT VARIANT 1773 FT /note="A -> V (in STGD1; uncertain significance; severely FT decreases solubility; loss of cytoplasmic vesicle FT localization; decreases basal ATPase activity below 50%; FT loss of N-Ret-PE-induced stimulation in ATPase activity; FT dbSNP:rs760549861)" FT /evidence="ECO:0000269|PubMed:23419329, FT ECO:0000269|PubMed:26780318, ECO:0000269|PubMed:33375396" FT /id="VAR_084944" FT VARIANT 1775 FT /note="I -> N (in STGD1; uncertain significance; FT dbSNP:rs771742619)" FT /evidence="ECO:0000269|PubMed:23419329" FT /id="VAR_085020" FT VARIANT 1776 FT /note="P -> L (in STGD1; dbSNP:rs1553187939)" FT /evidence="ECO:0000269|PubMed:11527935, FT ECO:0000269|PubMed:26780318" FT /id="VAR_012593" FT VARIANT 1779..2273 FT /note="Missing (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:10634594" FT /id="VAR_085021" FT VARIANT 1779 FT /note="Y -> H (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:23419329" FT /id="VAR_085022" FT VARIANT 1780 FT /note="P -> A (in STGD1; dbSNP:rs121909207)" FT /evidence="ECO:0000269|PubMed:10746567" FT /id="VAR_012594" FT VARIANT 1794 FT /note="A -> D (in STGD1; also found in a patient with FT bull's eye maculopathy; uncertain significance; moderately FT decreases solubility; loss of cytoplasmic vesicle FT localization; decreases basal ATPase activity below 50%; FT severely decreases N-Ret-PE-stimulated ATPase activity; FT dbSNP:rs61751406)" FT /evidence="ECO:0000269|PubMed:23143460, FT ECO:0000269|PubMed:33375396" FT /id="VAR_008466" FT VARIANT 1794 FT /note="A -> P (in STGD1; uncertain significance; loss of FT cytoplasmic vesicle localization; decreases ATPase activity FT between 50% and 80%; decreases modestly N-Ret-PE-stimulated FT ATPase; decreases solubility below 50%; significantly FT reduces N-Ret-PE binding in the absence of ATP; FT dbSNP:rs1571252997)" FT /evidence="ECO:0000269|PubMed:29847635, FT ECO:0000269|PubMed:33375396" FT /id="VAR_085023" FT VARIANT 1799 FT /note="N -> D (in STGD1; dbSNP:rs61750574)" FT /evidence="ECO:0000269|PubMed:11385708, FT ECO:0000269|PubMed:18977788" FT /id="VAR_012595" FT VARIANT 1805 FT /note="N -> D (in STGD1; does not affect solubility; does FT not affect location in cytoplasmic vesicle; decreases FT ATPase activity between 50% and 80%; decreases modestly FT N-Ret-PE-stimulated ATPase; dbSNP:rs61753029)" FT /evidence="ECO:0000269|PubMed:11385708, FT ECO:0000269|PubMed:33375396" FT /id="VAR_012596" FT VARIANT 1817 FT /note="E -> D" FT /evidence="ECO:0000269|PubMed:9054934, FT ECO:0000269|PubMed:9503029" FT /id="VAR_012597" FT VARIANT 1820 FT /note="R -> P (in STGD1; dbSNP:rs62646875)" FT /evidence="ECO:0000269|PubMed:9973280" FT /id="VAR_008467" FT VARIANT 1838 FT /note="H -> D (in STGD1; uncertain significance; moderately FT decreases solubility; loss of cytoplasmic vesicle FT localization; decreases basal ATPase activity below 50%; FT decreases modestly N-Ret-PE-stimulated ATPase; FT dbSNP:rs62642562)" FT /evidence="ECO:0000269|PubMed:24457364, FT ECO:0000269|PubMed:33375396" FT /id="VAR_085024" FT VARIANT 1838 FT /note="H -> N (in STGD1; uncertain significance; does not FT affect solubility; does not affect location in cytoplasmic FT vesicle; decreases basal ATPase activity between 50% and FT 80%; decreases modestly N-Ret-PE-stimulated ATPase; FT dbSNP:rs62642562)" FT /evidence="ECO:0000269|PubMed:15192030, FT ECO:0000269|PubMed:33375396" FT /id="VAR_084945" FT VARIANT 1838 FT /note="H -> Y (in STGD1; moderately decreases solubility; FT loss of cytoplasmic vesicle localization; decreases basal FT ATPase activity below 50%; severely decreases FT N-Ret-PE-stimulated ATPase activity; dbSNP:rs62642562)" FT /evidence="ECO:0000269|PubMed:15192030, FT ECO:0000269|PubMed:33375396" FT /id="VAR_008468" FT VARIANT 1843 FT /note="R -> W (in STGD1; does not affect solubility; does FT not affect location in cytoplasmic vesicle; decreases FT ATPase activity between 50% and 80%; decreases modestly FT N-Ret-PE-stimulated ATPase; does not affect N-Ret-PE FT binding; dbSNP:rs62642576)" FT /evidence="ECO:0000269|PubMed:26780318, FT ECO:0000269|PubMed:33375396" FT /id="VAR_008469" FT VARIANT 1846 FT /note="I -> T (in STGD1; dbSNP:rs61750575)" FT /evidence="ECO:0000269|PubMed:11527935, FT ECO:0000269|PubMed:23143460" FT /id="VAR_008494" FT VARIANT 1868 FT /note="N -> I (risk factor for STGD1; slightly reduced FT retinal-stimulated ATP hydrolysis; does not affect FT solubility; does not affect location in cytoplasmic FT vesicle; does not affect both basal and N-Ret-PE-stimulated FT ATPase activity; does not affect N-Ret-PE binding; FT dbSNP:rs1801466)" FT /evidence="ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:11379881, ECO:0000269|PubMed:11384574, FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:11594993, FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:23419329, FT ECO:0000269|PubMed:26780318, ECO:0000269|PubMed:30120214, FT ECO:0000269|PubMed:33375396" FT /id="VAR_008470" FT VARIANT 1882 FT /note="M -> I (in CORD3; uncertain significance; FT dbSNP:rs752160946)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084946" FT VARIANT 1884 FT /note="V -> E (in STGD1; dbSNP:rs62642578)" FT /evidence="ECO:0000269|PubMed:11328725" FT /id="VAR_012598" FT VARIANT 1885 FT /note="E -> K (in STGD1; dbSNP:rs62642563)" FT /evidence="ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:26780318" FT /id="VAR_012599" FT VARIANT 1886 FT /note="G -> E (in STGD1; highly reduced ATP-binding FT capacity; dbSNP:rs62642579)" FT /evidence="ECO:0000269|PubMed:9973280" FT /id="VAR_008471" FT VARIANT 1890 FT /note="Missing (in STGD1; dbSNP:rs61750635)" FT /id="VAR_008472" FT VARIANT 1896 FT /note="V -> D (in STGD1; dbSNP:rs61750636)" FT /evidence="ECO:0000269|PubMed:11328725" FT /id="VAR_012600" FT VARIANT 1898 FT /note="R -> C (does not affect solubility; does not affect FT location in cytoplasmic vesicle; does not affect both basal FT and N-Ret-PE-stimulated ATPase activity; FT dbSNP:rs201357151)" FT /evidence="ECO:0000269|PubMed:33375396" FT /id="VAR_085025" FT VARIANT 1898 FT /note="R -> H (in STGD1 and ARMD2; does not affect FT solubility; does not affect location in cytoplasmic FT vesicle; does not affect both basal and N-Ret-PE-stimulated FT ATPase activity; Increases N-Ret-PE binding; FT dbSNP:rs1800552)" FT /evidence="ECO:0000269|PubMed:10746567, FT ECO:0000269|PubMed:10958763, ECO:0000269|PubMed:25346251, FT ECO:0000269|PubMed:33375396, ECO:0000269|PubMed:9295268" FT /id="VAR_008473" FT VARIANT 1921 FT /note="V -> G (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084947" FT VARIANT 1921 FT /note="V -> M (in STGD1; dbSNP:rs61753032)" FT /evidence="ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:26780318" FT /id="VAR_012601" FT VARIANT 1940 FT /note="L -> P (in STGD1 and FFM; dbSNP:rs61753033)" FT /evidence="ECO:0000269|PubMed:11385708, FT ECO:0000269|PubMed:18977788" FT /id="VAR_012602" FT VARIANT 1942 FT /note="E -> Q (in STGD1; uncertain significance; FT dbSNP:rs760353830)" FT /evidence="ECO:0000269|PubMed:23419329" FT /id="VAR_085026" FT VARIANT 1948 FT /note="P -> L (in dbSNP:rs56142141)" FT /evidence="ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:11385708, ECO:0000269|PubMed:11527935, FT ECO:0000269|PubMed:11594993, ECO:0000269|PubMed:15192030" FT /id="VAR_008474" FT VARIANT 1948 FT /note="P -> S" FT /evidence="ECO:0000269|PubMed:10634594" FT /id="VAR_085027" FT VARIANT 1961 FT /note="G -> E (in STGD1, FFM and CORD3; risk factor for FT ARMD2; also found in patients with cone dystrophy and with FT macular dystrophy; inhibition of ATP hydrolysis by retinal; FT dbSNP:rs1800553)" FT /evidence="ECO:0000269|PubMed:10206579, FT ECO:0000269|PubMed:10711710, ECO:0000269|PubMed:10880298, FT ECO:0000269|PubMed:10958763, ECO:0000269|PubMed:11346402, FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:15192030, FT ECO:0000269|PubMed:18977788, ECO:0000269|PubMed:19265867, FT ECO:0000269|PubMed:23143460, ECO:0000269|PubMed:24457364, FT ECO:0000269|PubMed:25346251, ECO:0000269|PubMed:9295268" FT /id="VAR_008475" FT VARIANT 1961 FT /note="G -> R (in STGD1; uncertain significance; FT dbSNP:rs142253670)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084948" FT VARIANT 1970 FT /note="L -> F (in ARMD2, FFM and STGD1; also found in a FT patient with cone dystrophy; dbSNP:rs28938473)" FT /evidence="ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:19265867, FT ECO:0000269|PubMed:25346251, ECO:0000269|PubMed:9295268, FT ECO:0000269|PubMed:9781034" FT /id="VAR_008476" FT VARIANT 1971 FT /note="L -> R (in FFM; highly reduced ATP-binding capacity; FT abolishes basal and retinal-stimulated ATP hydrolysis; FT dbSNP:rs61753034)" FT /evidence="ECO:0000269|PubMed:9781034" FT /id="VAR_012603" FT VARIANT 1975 FT /note="G -> R (in STGD1; dbSNP:rs61753036)" FT /evidence="ECO:0000269|PubMed:10958763" FT /id="VAR_012604" FT VARIANT 1977 FT /note="G -> S (in STGD1 and ARMD2; highly reduced FT ATP-binding capacity; inhibition of ATP hydrolysis by FT retinal; dbSNP:rs61750639)" FT /evidence="ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:18977788, FT ECO:0000269|PubMed:19028736, ECO:0000269|PubMed:19265867, FT ECO:0000269|PubMed:26780318, ECO:0000269|PubMed:9781034" FT /id="VAR_008477" FT VARIANT 2017 FT /note="C -> Y (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084949" FT VARIANT 2023 FT /note="I -> T (in STGD1; uncertain significance; FT dbSNP:rs150633517)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084950" FT VARIANT 2027 FT /note="L -> F (in STGD1 and FFM; also found in a patient FT with chorioretinal atrophy; highly reduced ATP-binding FT capacity; dbSNP:rs61751408)" FT /evidence="ECO:0000269|PubMed:11379881, FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:15192030, FT ECO:0000269|PubMed:18977788, ECO:0000269|PubMed:23143460, FT ECO:0000269|PubMed:25346251" FT /id="VAR_008478" FT VARIANT 2030..2273 FT /note="Missing (in STGD1 and CORD3; uncertain significance; FT dbSNP:rs61751383)" FT /evidence="ECO:0000269|PubMed:10634594, FT ECO:0000269|PubMed:19265867, ECO:0000269|PubMed:26780318" FT /id="VAR_084951" FT VARIANT 2030 FT /note="R -> Q (in STGD1 and FFM; dbSNP:rs61750641)" FT /evidence="ECO:0000269|PubMed:11379881, FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:15192030, FT ECO:0000269|PubMed:23143460, ECO:0000269|PubMed:25346251" FT /id="VAR_008480" FT VARIANT 2032 FT /note="H -> R (in STGD1; uncertain significance; FT dbSNP:rs1242866408)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084952" FT VARIANT 2033 FT /note="L -> R (in STGD1; uncertain significance; FT dbSNP:rs1553186896)" FT /evidence="ECO:0000269|PubMed:25346251" FT /id="VAR_084953" FT VARIANT 2035 FT /note="L -> P (in STGD1; dbSNP:rs61750642)" FT /evidence="ECO:0000269|PubMed:11527935" FT /id="VAR_012605" FT VARIANT 2038 FT /note="R -> W (in STGD1; highly reduced ATP-binding FT capacity; dbSNP:rs61750643)" FT /evidence="ECO:0000269|PubMed:10206579, FT ECO:0000269|PubMed:26780318" FT /id="VAR_008495" FT VARIANT 2040..2273 FT /note="Missing (in STGD1; uncertain significance; also FT found in a patient with chorioretinal atrophy; uncertain FT significance; dbSNP:rs61753038)" FT /evidence="ECO:0000269|PubMed:23143460, FT ECO:0000269|PubMed:26780318" FT /id="VAR_084954" FT VARIANT 2040 FT /note="R -> Q (in STGD1; uncertain significance; FT dbSNP:rs148460146)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084955" FT VARIANT 2042 FT /note="V -> G (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084956" FT VARIANT 2043 FT /note="P -> S (in CORD3; uncertain significance; FT dbSNP:rs763230559)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084957" FT VARIANT 2047 FT /note="I -> N (in ARMD2)" FT /evidence="ECO:0000269|PubMed:19028736" FT /id="VAR_067429" FT VARIANT 2050 FT /note="V -> L (in STGD1 and CORD3; may act as a modifier of FT macular dystrophy in patients who also have a Trp-172 FT mutation in PRPH2; dbSNP:rs41292677)" FT /evidence="ECO:0000269|PubMed:11527935, FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:20335603, FT ECO:0000269|PubMed:25346251" FT /id="VAR_008481" FT VARIANT 2059 FT /note="G -> A" FT /evidence="ECO:0000269|PubMed:10958763" FT /id="VAR_012606" FT VARIANT 2060 FT /note="L -> R (in CORD3; dbSNP:rs61753039)" FT /evidence="ECO:0000269|PubMed:11385708, FT ECO:0000269|PubMed:18977788" FT /id="VAR_012607" FT VARIANT 2064 FT /note="A -> T (in STGD1; uncertain significance; FT dbSNP:rs61753040)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084958" FT VARIANT 2071 FT /note="Y -> F (in STGD1)" FT /evidence="ECO:0000269|PubMed:11328725" FT /id="VAR_012608" FT VARIANT 2074 FT /note="G -> V (in STGD1; uncertain significance; FT dbSNP:rs367839100)" FT /evidence="ECO:0000269|PubMed:23419329" FT /id="VAR_085028" FT VARIANT 2077 FT /note="R -> G (in STGD1; dbSNP:rs61750645)" FT /evidence="ECO:0000269|PubMed:10958763" FT /id="VAR_012609" FT VARIANT 2077 FT /note="R -> W (in STGD1; highly reduced ATP-binding FT capacity; decreases solubility at 50 %; loss of FT intracellular vesicle localization; drastically reduced FT basal activity with little or no substrate stimulation; FT dbSNP:rs61750645)" FT /evidence="ECO:0000269|PubMed:10206579, FT ECO:0000269|PubMed:10958763, ECO:0000269|PubMed:29847635" FT /id="VAR_008482" FT VARIANT 2078 FT /note="K -> E (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084959" FT VARIANT 2096 FT /note="E -> K (in STGD1; inhibition of ATP hydrolysis by FT retinal; dbSNP:rs61750646)" FT /evidence="ECO:0000269|PubMed:19265867" FT /id="VAR_008483" FT VARIANT 2097 FT /note="P -> S (in STGD1; uncertain significance; FT dbSNP:rs1166357291)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084960" FT VARIANT 2106 FT /note="R -> C (in STGD1 and FFM; reduced ATP-binding FT capacity; dbSNP:rs61750648)" FT /evidence="ECO:0000269|PubMed:11379881, FT ECO:0000269|PubMed:23143460" FT /id="VAR_008484" FT VARIANT 2107 FT /note="R -> C (in STGD1; uncertain significance; FT dbSNP:rs2297669)" FT /evidence="ECO:0000269|PubMed:11527935, FT ECO:0000269|PubMed:23143460" FT /id="VAR_012610" FT VARIANT 2107 FT /note="R -> H (in STGD1 and CORD3; may predispose to FT develop retinal toxicity after treatment with chloroquine FT and hydroxychloroquine; dbSNP:rs62642564)" FT /evidence="ECO:0000269|PubMed:10206579, FT ECO:0000269|PubMed:11384574, ECO:0000269|PubMed:11385708, FT ECO:0000269|PubMed:11527935, ECO:0000269|PubMed:15192030, FT ECO:0000269|PubMed:18977788, ECO:0000269|PubMed:24457364, FT ECO:0000269|PubMed:26780318, ECO:0000269|PubMed:9781034" FT /id="VAR_008485" FT VARIANT 2128 FT /note="H -> R (in STGD1; dbSNP:rs61750651)" FT /evidence="ECO:0000269|PubMed:10206579, FT ECO:0000269|PubMed:23419329" FT /id="VAR_008486" FT VARIANT 2131 FT /note="E -> K (in STGD1; uncertain significance; FT dbSNP:rs61750652)" FT /evidence="ECO:0000269|PubMed:23143460" FT /id="VAR_008487" FT VARIANT 2137 FT /note="C -> Y (in ARMD2)" FT /evidence="ECO:0000269|PubMed:19028736" FT /id="VAR_067430" FT VARIANT 2139 FT /note="R -> W (in STGD1; dbSNP:rs61750653)" FT /evidence="ECO:0000269|PubMed:11527935, FT ECO:0000269|PubMed:15192030" FT /id="VAR_008488" FT VARIANT 2140 FT /note="L -> Q (in STGD1; uncertain significance; FT dbSNP:rs774475956)" FT /evidence="ECO:0000269|PubMed:19265867" FT /id="VAR_084961" FT VARIANT 2146 FT /note="G -> D (in CORD3; dbSNP:rs61753044)" FT /evidence="ECO:0000269|PubMed:11527935, FT ECO:0000269|PubMed:26780318" FT /id="VAR_012611" FT VARIANT 2149 FT /note="R -> L (in STGD1; dbSNP:rs61750655)" FT /evidence="ECO:0000269|PubMed:15192030" FT /id="VAR_012612" FT VARIANT 2150 FT /note="C -> R (in STGD1; dbSNP:rs61750656)" FT /evidence="ECO:0000269|PubMed:11527935, FT ECO:0000269|PubMed:26780318" FT /id="VAR_012613" FT VARIANT 2150 FT /note="C -> Y (in STGD1 and CORD3; dbSNP:rs61751384)" FT /evidence="ECO:0000269|PubMed:10206579, FT ECO:0000269|PubMed:10634594, ECO:0000269|PubMed:11527935, FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:18977788, FT ECO:0000269|PubMed:23143460" FT /id="VAR_008489" FT VARIANT 2160 FT /note="K -> R (in STGD1; dbSNP:rs281865405)" FT /evidence="ECO:0000269|PubMed:10634594" FT /id="VAR_008490" FT VARIANT 2177 FT /note="D -> N (in CORD3, ARMD2 and STGD1; uncertain FT significance; increased retinal-stimulated ATP hydrolysis; FT dbSNP:rs1800555)" FT /evidence="ECO:0000269|PubMed:10880298, FT ECO:0000269|PubMed:10958763, ECO:0000269|PubMed:11346402, FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:25346251, FT ECO:0000269|PubMed:9295268" FT /id="VAR_008491" FT VARIANT 2188 FT /note="F -> S (in STGD1; uncertain significance; FT dbSNP:rs61750658)" FT /evidence="ECO:0000269|PubMed:26780318" FT /id="VAR_084962" FT VARIANT 2216 FT /note="A -> V (in dbSNP:rs886044763)" FT /evidence="ECO:0000269|PubMed:10958763" FT /id="VAR_012614" FT VARIANT 2221 FT /note="L -> P (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:19265867" FT /id="VAR_084963" FT VARIANT 2229 FT /note="L -> P (in STGD1; dbSNP:rs61750659)" FT /evidence="ECO:0000269|PubMed:11328725" FT /id="VAR_012615" FT VARIANT 2237 FT /note="T -> P (in STGD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:23143460" FT /id="VAR_084964" FT VARIANT 2241 FT /note="L -> V (in STGD1; dbSNP:rs61748521)" FT /evidence="ECO:0000269|PubMed:10958763, FT ECO:0000269|PubMed:15192030, ECO:0000269|PubMed:18977788" FT /id="VAR_012616" FT VARIANT 2255 FT /note="S -> I (in dbSNP:rs6666652)" FT /evidence="ECO:0000269|PubMed:11379881, FT ECO:0000269|PubMed:11384574, ECO:0000269|PubMed:11385708, FT ECO:0000269|PubMed:23419329, ECO:0000269|PubMed:26780318, FT ECO:0000269|PubMed:9295268" FT /id="VAR_009157" FT VARIANT 2263 FT /note="R -> L (in STGD1; dbSNP:rs281865407)" FT /evidence="ECO:0000269|PubMed:11328725" FT /id="VAR_012617" FT MUTAGEN 940 FT /note="P->R: Decreases 11-cis-Retinal binding affinity by FT 50%." FT /evidence="ECO:0000269|PubMed:23144455" FT MUTAGEN 966 FT /note="G->D: Abolishes basal and retinal-stimulated ATP FT hydrolysis." FT /evidence="ECO:0000269|PubMed:11017087" FT MUTAGEN 969 FT /note="K->M: Abolishes basal and retinal-stimulated ATP FT hydrolysis." FT /evidence="ECO:0000269|PubMed:11017087" FT MUTAGEN 969 FT /note="K->M: Inhibits ATPase activity; when associated with FT M-1978. Decreases translocase activity; when associated FT with M-1978. Does not affect protein subcellular FT localization in endoplasmic reticulum; when associated with FT M-1978. Loss of ATP-dependent all-trans-retinal transport; FT when associated with M-1978. Loss in N-retinylidene-PE FT transfer activity. Inhibits ATPase activity with increasing FT retinal concentration. Does not affect N-retinylidene-PE FT binding. Impairs ATP-dependent release of FT N-retinylidene-PE. Significantly reduces PE flippase FT activity." FT /evidence="ECO:0000269|PubMed:22735453, FT ECO:0000269|PubMed:24097981" FT MUTAGEN 1087 FT /note="E->Q: Does not affect protein folding; when FT associated with Q-2096. Loss of ATPase activity; when FT associated with Q-2096." FT /evidence="ECO:0000269|PubMed:33605212" FT MUTAGEN 1357 FT /note="A->T: Decreases solubility at 50%. Loss of FT intracellular vesicle localization. Does not affect FT substrate binding. Reduces basal ATPase activity." FT /evidence="ECO:0000269|PubMed:29847635" FT MUTAGEN 1502 FT /note="C->R: Moderately decreased protein abundance. FT Moderately decreased ATPase activity. Moderately decreased FT phospholipid translocase activity." FT /evidence="ECO:0000269|PubMed:24097981" FT MUTAGEN 1838 FT /note="H->R: Severely decreases solubility. Loss of FT cytoplasmic vesicle localization. Decreases basal ATPase FT activity below 50%. Loss of N-Ret-PE-induced stimulation in FT ATPase activity." FT /evidence="ECO:0000269|PubMed:33375396" FT MUTAGEN 1975 FT /note="G->D: Inhibition of retinal-stimulated ATP FT hydrolysis." FT /evidence="ECO:0000269|PubMed:11017087" FT MUTAGEN 1978 FT /note="K->M: Inhibits ATPase activity; when associated with FT M-969. Decreases translocase activity; when associated with FT M-969. Does not affect protein subcellular localization in FT endoplasmic reticulum; when associated with M-969. Loss of FT ATP-dependent all-trans-retinal transport; when associated FT with M-1978. Loss in N-retinylidene-PE transfer activity. FT Inhibits ATPase activity with increasing retinal FT concentration. Does not affect ATP-independent FT N-retinylidene-PE binding. Does not affect ATP-dependent of FT N-retinylidene-PE release. Significantly reduces PE FT flippase activity. Inhibition of retinal-stimulated ATP FT hydrolysis." FT /evidence="ECO:0000269|PubMed:11017087, FT ECO:0000269|PubMed:22735453, ECO:0000269|PubMed:24097981" FT MUTAGEN 2096 FT /note="E->Q: Does not affect protein folding; when FT associated with Q-1087. Loss of ATPase activity; when FT associated with Q-1087." FT /evidence="ECO:0000269|PubMed:33605212" FT MUTAGEN 2107 FT /note="R->P: Highly decreased protein abundance. Highly FT decreased ATPase activity. Highly decreased phospholipid FT translocase activity." FT /evidence="ECO:0000269|PubMed:24097981" FT MUTAGEN 2180 FT /note="P->L: Does not affect protein abundance. Does not FT affect ATPase activity. Moderately decreased phospholipid FT translocase activity." FT /evidence="ECO:0000269|PubMed:24097981" FT CONFLICT 722 FT /note="G -> V (in Ref. 2; AAC23915)" FT /evidence="ECO:0000305" FT CONFLICT 849 FT /note="V -> C (in Ref. 1; AAC51144)" FT /evidence="ECO:0000305" FT CONFLICT 882 FT /note="G -> S (in Ref. 1; AAC51144 and 3; CAA75729)" FT /evidence="ECO:0000305" FT CONFLICT 941 FT /note="C -> S (in Ref. 2; AAC23915)" FT /evidence="ECO:0000305" FT CONFLICT 1116 FT /note="S -> P (in Ref. 1; AAC51144)" FT /evidence="ECO:0000305" FT CONFLICT 1125..1126 FT /note="LL -> HQ (in Ref. 1; AAC51144)" FT /evidence="ECO:0000305" FT CONFLICT 1395 FT /note="P -> L (in Ref. 1; AAC51144 and 3; CAA75729)" FT /evidence="ECO:0000305" FT CONFLICT 1465 FT /note="S -> C (in Ref. 4; AAC05632)" FT /evidence="ECO:0000305" FT CONFLICT 1518 FT /note="S -> T (in Ref. 4; AAC05632)" FT /evidence="ECO:0000305" FT CONFLICT 1733 FT /note="M -> V (in Ref. 2; AAC23915)" FT /evidence="ECO:0000305" FT CONFLICT 1989 FT /note="T -> N (in Ref. 2; AAC23915)" FT /evidence="ECO:0000305" FT CONFLICT 2119 FT /note="E -> K (in Ref. 1; AAC51144)" FT /evidence="ECO:0000305" FT HELIX 4..21 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 24..44 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 48..51 FT /evidence="ECO:0007829|PDB:7E7I" FT STRAND 58..60 FT /evidence="ECO:0007829|PDB:7LKP" FT HELIX 62..64 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 66..75 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 76..78 FT /evidence="ECO:0007829|PDB:7LKZ" FT STRAND 81..84 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 87..89 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 90..92 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 101..112 FT /evidence="ECO:0007829|PDB:7M1Q" FT TURN 113..115 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 116..118 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 119..137 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 140..142 FT /evidence="ECO:0007829|PDB:7E7I" FT STRAND 147..149 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 151..154 FT /evidence="ECO:0007829|PDB:7M1Q" FT TURN 157..159 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 170..172 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 175..177 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 210..217 FT /evidence="ECO:0007829|PDB:7E7I" FT TURN 234..238 FT /evidence="ECO:0007829|PDB:7E7I" FT STRAND 240..245 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 246..248 FT /evidence="ECO:0007829|PDB:7E7I" FT STRAND 249..251 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 260..263 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 264..266 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 272..276 FT /evidence="ECO:0007829|PDB:7M1Q" FT TURN 277..279 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 280..289 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 291..300 FT /evidence="ECO:0007829|PDB:7M1Q" FT TURN 301..304 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 313..323 FT /evidence="ECO:0007829|PDB:7M1Q" FT TURN 328..330 FT /evidence="ECO:0007829|PDB:7E7Q" FT HELIX 339..342 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 345..349 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 364..366 FT /evidence="ECO:0007829|PDB:7LKP" FT HELIX 368..379 FT /evidence="ECO:0007829|PDB:7M1Q" FT TURN 381..383 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 384..394 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 397..401 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 405..414 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 416..429 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 431..442 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 447..456 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 458..460 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 462..467 FT /evidence="ECO:0007829|PDB:7LKP" FT STRAND 471..473 FT /evidence="ECO:0007829|PDB:7E7O" FT HELIX 474..477 FT /evidence="ECO:0007829|PDB:7M1Q" FT TURN 478..481 FT /evidence="ECO:0007829|PDB:7M1Q" FT TURN 483..486 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 488..490 FT /evidence="ECO:0007829|PDB:7LKP" FT HELIX 499..517 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 525..527 FT /evidence="ECO:0007829|PDB:7M1Q" FT TURN 531..536 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 537..543 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 547..552 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 565..572 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 575..577 FT /evidence="ECO:0007829|PDB:7M1Q" FT TURN 597..599 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 602..605 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 608..624 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 632..636 FT /evidence="ECO:0007829|PDB:7LKP" FT STRAND 642..646 FT /evidence="ECO:0007829|PDB:7E7I" FT HELIX 647..679 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 683..689 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 695..721 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 724..727 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 730..754 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 758..781 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 783..785 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 790..794 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 798..814 FT /evidence="ECO:0007829|PDB:7M1Q" FT TURN 821..825 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 828..831 FT /evidence="ECO:0007829|PDB:7LKZ" FT HELIX 837..860 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 863..865 FT /evidence="ECO:0007829|PDB:7M1Q" FT TURN 872..876 FT /evidence="ECO:0007829|PDB:7LKZ" FT STRAND 877..879 FT /evidence="ECO:0007829|PDB:7LKZ" FT STRAND 923..925 FT /evidence="ECO:0007829|PDB:7E7Q" FT STRAND 927..934 FT /evidence="ECO:0007829|PDB:7LKP" FT HELIX 939..941 FT /evidence="ECO:0007829|PDB:7LKZ" FT STRAND 945..949 FT /evidence="ECO:0007829|PDB:7LKZ" FT STRAND 956..960 FT /evidence="ECO:0007829|PDB:7M1Q" FT TURN 965..968 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 969..977 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 978..980 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 986..989 FT /evidence="ECO:0007829|PDB:7LKP" FT TURN 993..995 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 1001..1004 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 1005..1008 FT /evidence="ECO:0007829|PDB:7LKZ" FT STRAND 1016..1018 FT /evidence="ECO:0007829|PDB:7LKZ" FT HELIX 1020..1030 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 1035..1043 FT /evidence="ECO:0007829|PDB:7M1Q" FT TURN 1049..1054 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 1055..1058 FT /evidence="ECO:0007829|PDB:7M1Q" FT TURN 1059..1061 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 1064..1073 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 1074..1076 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 1077..1079 FT /evidence="ECO:0007829|PDB:7LKP" FT STRAND 1081..1084 FT /evidence="ECO:0007829|PDB:7LKP" FT STRAND 1086..1091 FT /evidence="ECO:0007829|PDB:7LKP" FT HELIX 1094..1106 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 1113..1115 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 1121..1123 FT /evidence="ECO:0007829|PDB:7M1Q" FT TURN 1134..1137 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 1144..1148 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 1156..1158 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 1159..1161 FT /evidence="ECO:0007829|PDB:7E7I" FT STRAND 1201..1203 FT /evidence="ECO:0007829|PDB:7LKZ" FT HELIX 1205..1215 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 1223..1225 FT /evidence="ECO:0007829|PDB:7LKP" FT STRAND 1228..1230 FT /evidence="ECO:0007829|PDB:7LKP" FT STRAND 1231..1233 FT /evidence="ECO:0007829|PDB:7E7Q" FT STRAND 1236..1238 FT /evidence="ECO:0007829|PDB:7E7O" FT HELIX 1240..1254 FT /evidence="ECO:0007829|PDB:7M1Q" FT TURN 1255..1258 FT /evidence="ECO:0007829|PDB:7LKZ" FT STRAND 1259..1262 FT /evidence="ECO:0007829|PDB:7E7Q" FT STRAND 1263..1265 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 1269..1276 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 1349..1368 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 1371..1374 FT /evidence="ECO:0007829|PDB:7M1Q" FT TURN 1375..1378 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 1379..1393 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 1407..1409 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 1410..1412 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 1414..1419 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 1425..1435 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 1436..1438 FT /evidence="ECO:0007829|PDB:7E7O" FT STRAND 1440..1442 FT /evidence="ECO:0007829|PDB:7LKP" FT STRAND 1451..1453 FT /evidence="ECO:0007829|PDB:7E7O" FT HELIX 1468..1476 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 1481..1483 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 1493..1495 FT /evidence="ECO:0007829|PDB:7M1Q" FT TURN 1504..1507 FT /evidence="ECO:0007829|PDB:7LKP" FT STRAND 1513..1515 FT /evidence="ECO:0007829|PDB:7LKZ" FT TURN 1517..1519 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 1520..1524 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 1526..1528 FT /evidence="ECO:0007829|PDB:7LKP" FT HELIX 1530..1545 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 1548..1551 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 1558..1562 FT /evidence="ECO:0007829|PDB:7M1Q" FT TURN 1570..1573 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 1574..1586 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 1593..1599 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 1602..1609 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 1612..1619 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 1627..1641 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 1645..1647 FT /evidence="ECO:0007829|PDB:7M1Q" FT TURN 1649..1651 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 1653..1658 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 1665..1690 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 1692..1706 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 1709..1716 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 1720..1747 FT /evidence="ECO:0007829|PDB:7M1Q" FT TURN 1748..1750 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 1752..1755 FT /evidence="ECO:0007829|PDB:7M1Q" FT TURN 1757..1759 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 1760..1778 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 1781..1784 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 1788..1813 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 1817..1820 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 1821..1829 FT /evidence="ECO:0007829|PDB:7M1Q" FT TURN 1830..1832 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 1833..1835 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 1837..1860 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 1870..1875 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 1876..1896 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 1919..1929 FT /evidence="ECO:0007829|PDB:7LKP" FT STRAND 1931..1933 FT /evidence="ECO:0007829|PDB:7E7O" FT STRAND 1937..1946 FT /evidence="ECO:0007829|PDB:7LKP" FT TURN 1948..1950 FT /evidence="ECO:0007829|PDB:7LKP" FT STRAND 1952..1958 FT /evidence="ECO:0007829|PDB:7LKP" FT STRAND 1967..1969 FT /evidence="ECO:0007829|PDB:7LKZ" FT STRAND 1974..1976 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 1978..1985 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 1986..1988 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 1993..1998 FT /evidence="ECO:0007829|PDB:7LKP" FT STRAND 2003..2005 FT /evidence="ECO:0007829|PDB:7LKP" FT TURN 2009..2011 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 2013..2020 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 2025..2028 FT /evidence="ECO:0007829|PDB:7LKP" FT HELIX 2034..2040 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 2044..2046 FT /evidence="ECO:0007829|PDB:7LKP" FT TURN 2050..2053 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 2055..2058 FT /evidence="ECO:0007829|PDB:7M1Q" FT TURN 2062..2065 FT /evidence="ECO:0007829|PDB:7M1Q" FT TURN 2068..2070 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 2073..2084 FT /evidence="ECO:0007829|PDB:7M1Q" FT TURN 2085..2087 FT /evidence="ECO:0007829|PDB:7LKZ" FT STRAND 2090..2097 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 2103..2119 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 2122..2126 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 2131..2133 FT /evidence="ECO:0007829|PDB:7M1Q" FT TURN 2134..2136 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 2138..2152 FT /evidence="ECO:0007829|PDB:7LKP" FT HELIX 2154..2160 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 2166..2169 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 2179..2192 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 2197..2202 FT /evidence="ECO:0007829|PDB:7LKP" FT STRAND 2205..2209 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 2217..2224 FT /evidence="ECO:0007829|PDB:7M1Q" FT TURN 2225..2228 FT /evidence="ECO:0007829|PDB:7M1Q" FT STRAND 2235..2237 FT /evidence="ECO:0007829|PDB:7M1Q" FT HELIX 2241..2252 FT /evidence="ECO:0007829|PDB:7LKP" SQ SEQUENCE 2273 AA; 255944 MW; 6E7012D3041CD043 CRC64; MGFVRQIQLL LWKNWTLRKR QKIRFVVELV WPLSLFLVLI WLRNANPLYS HHECHFPNKA MPSAGMLPWL QGIFCNVNNP CFQSPTPGES PGIVSNYNNS ILARVYRDFQ ELLMNAPESQ HLGRIWTELH ILSQFMDTLR THPERIAGRG IRIRDILKDE ETLTLFLIKN IGLSDSVVYL LINSQVRPEQ FAHGVPDLAL KDIACSEALL ERFIIFSQRR GAKTVRYALC SLSQGTLQWI EDTLYANVDF FKLFRVLPTL LDSRSQGINL RSWGGILSDM SPRIQEFIHR PSMQDLLWVT RPLMQNGGPE TFTKLMGILS DLLCGYPEGG GSRVLSFNWY EDNNYKAFLG IDSTRKDPIY SYDRRTTSFC NALIQSLESN PLTKIAWRAA KPLLMGKILY TPDSPAARRI LKNANSTFEE LEHVRKLVKA WEEVGPQIWY FFDNSTQMNM IRDTLGNPTV KDFLNRQLGE EGITAEAILN FLYKGPRESQ ADDMANFDWR DIFNITDRTL RLVNQYLECL VLDKFESYND ETQLTQRALS LLEENMFWAG VVFPDMYPWT SSLPPHVKYK IRMDIDVVEK TNKIKDRYWD SGPRADPVED FRYIWGGFAY LQDMVEQGIT RSQVQAEAPV GIYLQQMPYP CFVDDSFMII LNRCFPIFMV LAWIYSVSMT VKSIVLEKEL RLKETLKNQG VSNAVIWCTW FLDSFSIMSM SIFLLTIFIM HGRILHYSDP FILFLFLLAF STATIMLCFL LSTFFSKASL AAACSGVIYF TLYLPHILCF AWQDRMTAEL KKAVSLLSPV AFGFGTEYLV RFEEQGLGLQ WSNIGNSPTE GDEFSFLLSM QMMLLDAAVY GLLAWYLDQV FPGDYGTPLP WYFLLQESYW LGGEGCSTRE ERALEKTEPL TEETEDPEHP EGIHDSFFER EHPGWVPGVC VKNLVKIFEP CGRPAVDRLN ITFYENQITA FLGHNGAGKT TTLSILTGLL PPTSGTVLVG GRDIETSLDA VRQSLGMCPQ HNILFHHLTV AEHMLFYAQL KGKSQEEAQL EMEAMLEDTG LHHKRNEEAQ DLSGGMQRKL SVAIAFVGDA KVVILDEPTS GVDPYSRRSI WDLLLKYRSG RTIIMSTHHM DEADLLGDRI AIIAQGRLYC SGTPLFLKNC FGTGLYLTLV RKMKNIQSQR KGSEGTCSCS SKGFSTTCPA HVDDLTPEQV LDGDVNELMD VVLHHVPEAK LVECIGQELI FLLPNKNFKH RAYASLFREL EETLADLGLS SFGISDTPLE EIFLKVTEDS DSGPLFAGGA QQKRENVNPR HPCLGPREKA GQTPQDSNVC SPGAPAAHPE GQPPPEPECP GPQLNTGTQL VLQHVQALLV KRFQHTIRSH KDFLAQIVLP ATFVFLALML SIVIPPFGEY PALTLHPWIY GQQYTFFSMD EPGSEQFTVL ADVLLNKPGF GNRCLKEGWL PEYPCGNSTP WKTPSVSPNI TQLFQKQKWT QVNPSPSCRC STREKLTMLP ECPEGAGGLP PPQRTQRSTE ILQDLTDRNI SDFLVKTYPA LIRSSLKSKF WVNEQRYGGI SIGGKLPVVP ITGEALVGFL SDLGRIMNVS GGPITREASK EIPDFLKHLE TEDNIKVWFN NKGWHALVSF LNVAHNAILR ASLPKDRSPE EYGITVISQP LNLTKEQLSE ITVLTTSVDA VVAICVIFSM SFVPASFVLY LIQERVNKSK HLQFISGVSP TTYWVTNFLW DIMNYSVSAG LVVGIFIGFQ KKAYTSPENL PALVALLLLY GWAVIPMMYP ASFLFDVPST AYVALSCANL FIGINSSAIT FILELFENNR TLLRFNAVLR KLLIVFPHFC LGRGLIDLAL SQAVTDVYAR FGEEHSANPF HWDLIGKNLF AMVVEGVVYF LLTLLVQRHF FLSQWIAEPT KEPIVDEDDD VAEERQRIIT GGNKTDILRL HELTKIYPGT SSPAVDRLCV GVRPGECFGL LGVNGAGKTT TFKMLTGDTT VTSGDATVAG KSILTNISEV HQNMGYCPQF DAIDELLTGR EHLYLYARLR GVPAEEIEKV ANWSIKSLGL TVYADCLAGT YSGGNKRKLS TAIALIGCPP LVLLDEPTTG MDPQARRMLW NVIVSIIREG RAVVLTSHSM EECEALCTRL AIMVKGAFRC MGTIQHLKSK FGDGYIVTMK IKSPKDDLLP DLNPVEQFFQ GNFPGSVQRE RHYNMLQFQV SSSSLARIFQ LLLSHKDSLL IEEYSVTQTT LDQVFVNFAK QQTESHDLPL HPRAAGASRQ AQD //