ID   IMPG2_HUMAN             Reviewed;        1241 AA.
AC   Q9BZV3; A8MWT5; Q9UKD4; Q9UKK5;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 3.
DT   24-JAN-2024, entry version 143.
DE   RecName: Full=Interphotoreceptor matrix proteoglycan 2;
DE   AltName: Full=Interphotoreceptor matrix proteoglycan of 200 kDa;
DE            Short=IPM 200;
DE   AltName: Full=Sialoprotein associated with cones and rods proteoglycan;
DE            Short=Spacrcan;
DE   Flags: Precursor;
GN   Name=IMPG2; Synonyms=IPM200;
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 [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND VARIANT
RP   ILE-674.
RX   PubMed=10542133; DOI=10.1006/mcbr.1999.0161;
RA   Kuehn M.H., Hageman G.S.;
RT   "Molecular characterization and genomic mapping of human IPM 200, a second
RT   member of a novel family of proteoglycans.";
RL   Mol. Cell Biol. Res. Commun. 2:103-110(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 82-86; 123-127 AND 582-593,
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, GLYCOSYLATION, AND VARIANT ILE-674.
RX   PubMed=10702256; DOI=10.1074/jbc.275.10.6945;
RA   Acharya S., Foletta V.C., Lee J.W., Rayborn M.E., Rodriguez I.R.,
RA   Young W.S. III, Hollyfield J.G.;
RT   "SPACRCAN, a novel human interphotoreceptor matrix hyaluronan-binding
RT   proteoglycan synthesized by photoreceptors and pinealocytes.";
RL   J. Biol. Chem. 275:6945-6955(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [4]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=29777959; DOI=10.1016/j.actbio.2018.05.023;
RA   Felemban M., Dorgau B., Hunt N.C., Hallam D., Zerti D., Bauer R., Ding Y.,
RA   Collin J., Steel D., Krasnogor N., Al-Aama J., Lindsay S., Mellough C.,
RA   Lako M.;
RT   "Extracellular matrix component expression in human pluripotent stem cell-
RT   derived retinal organoids recapitulates retinogenesis in vivo and reveals
RT   an important role for IMPG1 and CD44 in the development of photoreceptors
RT   and interphotoreceptor matrix.";
RL   Acta Biomater. 74:207-221(2018).
RN   [5]
RP   VARIANTS ILE-674 AND LEU-1013.
RX   PubMed=11726612;
RA   Kuehn M.H., Stone E.M., Hageman G.S.;
RT   "Organization of the human IMPG2 gene and its evaluation as a candidate
RT   gene in age-related macular degeneration and other retinal degenerative
RT   disorders.";
RL   Invest. Ophthalmol. Vis. Sci. 42:3123-3129(2001).
RN   [6]
RP   INVOLVEMENT IN RP56, INVOLVEMENT IN VMD5, AND VARIANT VMD5 LEU-124.
RX   PubMed=20673862; DOI=10.1016/j.ajhg.2010.07.004;
RA   Bandah-Rozenfeld D., Collin R.W., Banin E., van den Born L.I., Coene K.L.,
RA   Siemiatkowska A.M., Zelinger L., Khan M.I., Lefeber D.J., Erdinest I.,
RA   Testa F., Simonelli F., Voesenek K., Blokland E.A., Strom T.M.,
RA   Klaver C.C., Qamar R., Banfi S., Cremers F.P., Sharon D.,
RA   den Hollander A.I.;
RT   "Mutations in IMPG2, encoding interphotoreceptor matrix proteoglycan 2,
RT   cause autosomal-recessive retinitis pigmentosa.";
RL   Am. J. Hum. Genet. 87:199-208(2010).
RN   [7]
RP   VARIANTS RP56 127-ALA--VAL-1241 DEL; 171-LEU--VAL-1241 DEL;
RP   212-SER--VAL-1241 DEL; 560-TYR--VAL-1241 DEL; 906-ARG--VAL-1241 DEL;
RP   964-ARG--VAL-1241 DEL; 1008-ARG--VAL-1241 DEL AND 296-ARG--ASP-302 DEL, AND
RP   VARIANT PRO-379.
RX   PubMed=24876279; DOI=10.1167/iovs.14-14129;
RA   van Huet R.A., Collin R.W., Siemiatkowska A.M., Klaver C.C., Hoyng C.B.,
RA   Simonelli F., Khan M.I., Qamar R., Banin E., Cremers F.P., Theelen T.,
RA   den Hollander A.I., van den Born L.I., Klevering B.J.;
RT   "IMPG2-associated retinitis pigmentosa displays relatively early macular
RT   involvement.";
RL   Invest. Ophthalmol. Vis. Sci. 55:3939-3953(2014).
RN   [8]
RP   INVOLVEMENT IN VMD5, AND VARIANT VMD5 PHE-1077.
RX   PubMed=25085631; DOI=10.1016/j.ophtha.2014.06.028;
RA   Meunier I., Manes G., Bocquet B., Marquette V., Baudoin C., Puech B.,
RA   Defoort-Dhellemmes S., Audo I., Verdet R., Arndt C., Zanlonghi X.,
RA   Le Meur G., Dhaenens C.M., Hamel C.P.;
RT   "Frequency and clinical pattern of vitelliform macular dystrophy caused by
RT   mutations of interphotoreceptor matrix IMPG1 and IMPG2 genes.";
RL   Ophthalmology 121:2406-2414(2014).
RN   [9]
RP   VARIANTS VMD5 226-GLU--VAL-1241 DEL; 522-SER--VAL-1241 DEL;
RP   856-GLN--VAL-1241 DEL AND PHE-1077, AND VARIANTS PRO-243; ASP-1008;
RP   SER-1016 AND CYS-1042.
RX   PubMed=28644393; DOI=10.3390/genes8070170;
RA   Brandl C., Schulz H.L., Charbel Issa P., Birtel J., Bergholz R., Lange C.,
RA   Dahlke C., Zobor D., Weber B.H.F., Stoehr H.;
RT   "Mutations in the Genes for Interphotoreceptor Matrix Proteoglycans, IMPG1
RT   and IMPG2, in Patients with Vitelliform Macular Lesions.";
RL   Genes (Basel) 8:0-0(2017).
CC   -!- FUNCTION: Chondroitin sulfate- and hyaluronan-binding proteoglycan
CC       involved in the organization of interphotoreceptor matrix; may
CC       participate in the maturation and maintenance of the light-sensitive
CC       photoreceptor outer segment. Binds heparin.
CC       {ECO:0000269|PubMed:10702256}.
CC   -!- SUBCELLULAR LOCATION: Photoreceptor outer segment membrane
CC       {ECO:0000269|PubMed:29777959}; Single-pass type I membrane protein
CC       {ECO:0000255}. Photoreceptor inner segment membrane
CC       {ECO:0000250|UniProtKB:Q80XH2}; Single-pass type I membrane protein
CC       {ECO:0000255}. Secreted, extracellular space, extracellular matrix,
CC       interphotoreceptor matrix {ECO:0000269|PubMed:10702256}.
CC   -!- TISSUE SPECIFICITY: Expressed in the retina (at protein level)
CC       (PubMed:10702256, PubMed:29777959). Expressed by photoreceptors of the
CC       interphotoreceptor matrix (IPM) surrounding both rods and cones (at
CC       protein level) (PubMed:10542133, PubMed:29777959). IPM occupies the
CC       subretinal space between the apices of the retinal pigment epithelium
CC       and the neural retina (PubMed:10542133). Expressed in the pineal gland
CC       (at protein level) (PubMed:10702256). {ECO:0000269|PubMed:10542133,
CC       ECO:0000269|PubMed:10702256, ECO:0000269|PubMed:29777959}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the retina 17 weeks post-conception
CC       (at protein level) (PubMed:29777959). Expressed in the outer
CC       neuroblastic zone and retinal pigment epithelium (at protein level)
CC       (PubMed:29777959). {ECO:0000269|PubMed:29777959}.
CC   -!- PTM: Highly glycosylated (N- and O-linked carbohydrates).
CC       {ECO:0000269|PubMed:10702256}.
CC   -!- DISEASE: Retinitis pigmentosa 56 (RP56) [MIM:613581]: 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. {ECO:0000269|PubMed:20673862,
CC       ECO:0000269|PubMed:24876279}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Macular dystrophy, vitelliform, 5 (VMD5) [MIM:616152]: A form
CC       of macular dystrophy, a retinal disease in which various forms of
CC       deposits, pigmentary changes, and atrophic lesions are observed in the
CC       macula lutea. Vitelliform macular dystrophies are characterized by
CC       yellow, lipofuscin-containing deposits, usually localized at the center
CC       of the macula. VMD5 features include late-onset moderate visual
CC       impairment and preservation of retinal pigment epithelium reflectivity.
CC       {ECO:0000269|PubMed:20673862, ECO:0000269|PubMed:25085631,
CC       ECO:0000269|PubMed:28644393}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
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DR   EMBL; AF173155; AAF06999.1; -; mRNA.
DR   EMBL; AF271379; AAG49889.1; -; Genomic_DNA.
DR   EMBL; AF271363; AAG49889.1; JOINED; Genomic_DNA.
DR   EMBL; AF271364; AAG49889.1; JOINED; Genomic_DNA.
DR   EMBL; AF271365; AAG49889.1; JOINED; Genomic_DNA.
DR   EMBL; AF271366; AAG49889.1; JOINED; Genomic_DNA.
DR   EMBL; AF271367; AAG49889.1; JOINED; Genomic_DNA.
DR   EMBL; AF271368; AAG49889.1; JOINED; Genomic_DNA.
DR   EMBL; AF271369; AAG49889.1; JOINED; Genomic_DNA.
DR   EMBL; AF271370; AAG49889.1; JOINED; Genomic_DNA.
DR   EMBL; AF271371; AAG49889.1; JOINED; Genomic_DNA.
DR   EMBL; AF271372; AAG49889.1; JOINED; Genomic_DNA.
DR   EMBL; AF271373; AAG49889.1; JOINED; Genomic_DNA.
DR   EMBL; AF271374; AAG49889.1; JOINED; Genomic_DNA.
DR   EMBL; AF271375; AAG49889.1; JOINED; Genomic_DNA.
DR   EMBL; AF271376; AAG49889.1; JOINED; Genomic_DNA.
DR   EMBL; AF271377; AAG49889.1; JOINED; Genomic_DNA.
DR   EMBL; AF271378; AAG49889.1; JOINED; Genomic_DNA.
DR   EMBL; AF157624; AAF13154.1; -; mRNA.
DR   EMBL; AC068764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS2940.1; -.
DR   RefSeq; NP_057331.2; NM_016247.3.
DR   AlphaFoldDB; Q9BZV3; -.
DR   STRING; 9606.ENSP00000193391; -.
DR   DrugBank; DB08818; Hyaluronic acid.
DR   GlyCosmos; Q9BZV3; 10 sites, No reported glycans.
DR   GlyGen; Q9BZV3; 10 sites.
DR   iPTMnet; Q9BZV3; -.
DR   PhosphoSitePlus; Q9BZV3; -.
DR   BioMuta; IMPG2; -.
DR   DMDM; 296439325; -.
DR   jPOST; Q9BZV3; -.
DR   MassIVE; Q9BZV3; -.
DR   PaxDb; 9606-ENSP00000193391; -.
DR   PeptideAtlas; Q9BZV3; -.
DR   ProteomicsDB; 79907; -.
DR   Antibodypedia; 32271; 63 antibodies from 20 providers.
DR   DNASU; 50939; -.
DR   Ensembl; ENST00000193391.8; ENSP00000193391.6; ENSG00000081148.12.
DR   GeneID; 50939; -.
DR   KEGG; hsa:50939; -.
DR   MANE-Select; ENST00000193391.8; ENSP00000193391.6; NM_016247.4; NP_057331.2.
DR   UCSC; uc003duq.3; human.
DR   AGR; HGNC:18362; -.
DR   CTD; 50939; -.
DR   DisGeNET; 50939; -.
DR   GeneCards; IMPG2; -.
DR   GeneReviews; IMPG2; -.
DR   HGNC; HGNC:18362; IMPG2.
DR   HPA; ENSG00000081148; Tissue enriched (retina).
DR   MalaCards; IMPG2; -.
DR   MIM; 607056; gene.
DR   MIM; 613581; phenotype.
DR   MIM; 616152; phenotype.
DR   neXtProt; NX_Q9BZV3; -.
DR   OpenTargets; ENSG00000081148; -.
DR   Orphanet; 99000; Adult-onset foveomacular vitelliform dystrophy.
DR   Orphanet; 791; Retinitis pigmentosa.
DR   PharmGKB; PA29866; -.
DR   VEuPathDB; HostDB:ENSG00000081148; -.
DR   eggNOG; ENOG502QT6W; Eukaryota.
DR   GeneTree; ENSGT00530000063503; -.
DR   HOGENOM; CLU_005111_0_0_1; -.
DR   InParanoid; Q9BZV3; -.
DR   OMA; ESSIWPW; -.
DR   OrthoDB; 4244504at2759; -.
DR   PhylomeDB; Q9BZV3; -.
DR   TreeFam; TF331340; -.
DR   PathwayCommons; Q9BZV3; -.
DR   BioGRID-ORCS; 50939; 9 hits in 1146 CRISPR screens.
DR   ChiTaRS; IMPG2; human.
DR   GenomeRNAi; 50939; -.
DR   Pharos; Q9BZV3; Tbio.
DR   PRO; PR:Q9BZV3; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q9BZV3; Protein.
DR   Bgee; ENSG00000081148; Expressed in right uterine tube and 63 other cell types or tissues.
DR   ExpressionAtlas; Q9BZV3; baseline and differential.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR   GO; GO:0031012; C:extracellular matrix; TAS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0033165; C:interphotoreceptor matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043235; C:receptor complex; IDA:MGI.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; TAS:UniProtKB.
DR   GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR   GO; GO:0005540; F:hyaluronic acid binding; IBA:GO_Central.
DR   GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR   GO; GO:0008104; P:protein localization; IEA:Ensembl.
DR   GO; GO:0060042; P:retina morphogenesis in camera-type eye; IEA:Ensembl.
DR   GO; GO:0007601; P:visual perception; TAS:UniProtKB.
DR   Gene3D; 3.30.70.960; SEA domain; 1.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR039861; IMPG.
DR   InterPro; IPR000082; SEA_dom.
DR   InterPro; IPR036364; SEA_dom_sf.
DR   PANTHER; PTHR12199; INTERPHOTORECEPTOR MATRIX PROTEOGLYCAN; 1.
DR   PANTHER; PTHR12199:SF4; INTERPHOTORECEPTOR MATRIX PROTEOGLYCAN 2; 1.
DR   Pfam; PF01390; SEA; 2.
DR   SMART; SM00200; SEA; 2.
DR   SUPFAM; SSF82671; SEA domain; 2.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS50024; SEA; 2.
DR   Genevisible; Q9BZV3; HS.
PE   1: Evidence at protein level;
KW   Cell projection; Direct protein sequencing; Disease variant;
KW   Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein;
KW   Heparin-binding; Membrane; Receptor; Reference proteome; Repeat;
KW   Retinitis pigmentosa; Secreted; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..1241
FT                   /note="Interphotoreceptor matrix proteoglycan 2"
FT                   /id="PRO_0000320149"
FT   TOPO_DOM        23..1099
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1100..1120
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1121..1241
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          239..353
FT                   /note="SEA 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT   DOMAIN          897..1010
FT                   /note="SEA 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT   DOMAIN          1010..1051
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1052..1093
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REGION          180..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          259..267
FT                   /note="Hyaluronan-binding motif involved in chondroitin
FT                   sulfate A-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          660..684
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1080..1088
FT                   /note="Hyaluronan-binding motif involved in chondroitin
FT                   sulfate C-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          1125..1133
FT                   /note="Hyaluronan-binding motif involved in chondroitin
FT                   sulfate A- and C-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          1136..1145
FT                   /note="Hyaluronan-binding motif involved in chondroitin
FT                   sulfate C-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          1210..1218
FT                   /note="Hyaluronan-binding motif involved in chondroitin
FT                   sulfate A- and C-binding motif"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        180..198
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        660..678
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        154
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        190
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        192
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        301
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        320
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        370
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        544
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        556
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        942
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        956
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        1014..1025
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        1019..1036
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        1038..1050
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        1054..1067
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        1061..1077
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        1079..1092
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   VARIANT         124
FT                   /note="F -> L (in VMD5; dbSNP:rs201893545)"
FT                   /evidence="ECO:0000269|PubMed:20673862"
FT                   /id="VAR_064336"
FT   VARIANT         127..1241
FT                   /note="Missing (in RP56)"
FT                   /evidence="ECO:0000269|PubMed:24876279"
FT                   /id="VAR_082176"
FT   VARIANT         171..1241
FT                   /note="Missing (in RP56)"
FT                   /evidence="ECO:0000269|PubMed:24876279"
FT                   /id="VAR_082177"
FT   VARIANT         212..1241
FT                   /note="Missing (in RP56)"
FT                   /evidence="ECO:0000269|PubMed:24876279"
FT                   /id="VAR_082178"
FT   VARIANT         226..1241
FT                   /note="Missing (in VMD5)"
FT                   /evidence="ECO:0000269|PubMed:28644393"
FT                   /id="VAR_082179"
FT   VARIANT         243
FT                   /note="A -> P (found in a patient with vitelliform macular
FT                   dystrophy; uncertain significance; dbSNP:rs1706811719)"
FT                   /evidence="ECO:0000269|PubMed:28644393"
FT                   /id="VAR_082180"
FT   VARIANT         296..302
FT                   /note="Missing (in RP56)"
FT                   /evidence="ECO:0000269|PubMed:24876279"
FT                   /id="VAR_082181"
FT   VARIANT         344
FT                   /note="K -> N (in dbSNP:rs34375459)"
FT                   /id="VAR_039144"
FT   VARIANT         379
FT                   /note="S -> P (found in a patient with retinitis
FT                   pigmentosa; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:24876279"
FT                   /id="VAR_082182"
FT   VARIANT         522..1241
FT                   /note="Missing (in VMD5)"
FT                   /evidence="ECO:0000269|PubMed:28644393"
FT                   /id="VAR_082183"
FT   VARIANT         560..1241
FT                   /note="Missing (in RP56)"
FT                   /evidence="ECO:0000269|PubMed:24876279"
FT                   /id="VAR_082184"
FT   VARIANT         674
FT                   /note="T -> I (in dbSNP:rs571391)"
FT                   /evidence="ECO:0000269|PubMed:10542133,
FT                   ECO:0000269|PubMed:10702256, ECO:0000269|PubMed:11726612"
FT                   /id="VAR_039145"
FT   VARIANT         856..1241
FT                   /note="Missing (in VMD5)"
FT                   /evidence="ECO:0000269|PubMed:28644393"
FT                   /id="VAR_082185"
FT   VARIANT         906..1241
FT                   /note="Missing (in RP56)"
FT                   /evidence="ECO:0000269|PubMed:24876279"
FT                   /id="VAR_082186"
FT   VARIANT         964..1241
FT                   /note="Missing (in RP56)"
FT                   /evidence="ECO:0000269|PubMed:24876279"
FT                   /id="VAR_082187"
FT   VARIANT         1008
FT                   /note="G -> D (found in a patient with vitelliform macular
FT                   dystrophy; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:28644393"
FT                   /id="VAR_082188"
FT   VARIANT         1013
FT                   /note="P -> L (in dbSNP:rs116450347)"
FT                   /evidence="ECO:0000269|PubMed:11726612"
FT                   /id="VAR_039146"
FT   VARIANT         1016
FT                   /note="F -> S (found in a patient with VMD5; uncertain
FT                   significance)"
FT                   /evidence="ECO:0000269|PubMed:28644393"
FT                   /id="VAR_082189"
FT   VARIANT         1042
FT                   /note="Y -> C (found in a patient with vitelliform macular
FT                   dystophy; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:28644393"
FT                   /id="VAR_082190"
FT   VARIANT         1077
FT                   /note="C -> F (in VMD5; dbSNP:rs713993049)"
FT                   /evidence="ECO:0000269|PubMed:25085631,
FT                   ECO:0000269|PubMed:28644393"
FT                   /id="VAR_072671"
FT   VARIANT         1088..1241
FT                   /note="Missing (in RP56)"
FT                   /evidence="ECO:0000269|PubMed:24876279"
FT                   /id="VAR_082191"
FT   CONFLICT        5
FT                   /note="P -> L (in Ref. 2; AAF13154)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        77
FT                   /note="I -> T (in Ref. 2; AAF13154)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        668
FT                   /note="E -> V (in Ref. 2; AAF13154)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        715
FT                   /note="Y -> C (in Ref. 1; AAF06999)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1012
FT                   /note="N -> T (in Ref. 1; AAG49889)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1241 AA;  138621 MW;  E72D7BFB84824078 CRC64;
     MIMFPLFGKI SLGILIFVLI EGDFPSLTAQ TYLSIEEIQE PKSAVSFLLP EESTDLSLAT
     KKKQPLDRRE TERQWLIRRR RSILFPNGVK ICPDESVAEA VANHVKYFKV RVCQEAVWEA
     FRTFWDRLPG REEYHYWMNL CEDGVTSIFE MGTNFSESVE HRSLIMKKLT YAKETVSSSE
     LSSPVPVGDT STLGDTTLSV PHPEVDAYEG ASESSLERPE ESISNEIENV IEEATKPAGE
     QIAEFSIHLL GKQYREELQD SSSFHHQHLE EEFISEVENA FTGLPGYKEI RVLEFRSPKE
     NDSGVDVYYA VTFNGEAISN TTWDLISLHS NKVENHGLVE LDDKPTVVYT ISNFRDYIAE
     TLQQNFLLGN SSLNPDPDSL QLINVRGVLR HQTEDLVWNT QSSSLQATPS SILDNTFQAA
     WPSADESITS SIPPLDFSSG PPSATGRELW SESPLGDLVS THKLAFPSKM GLSSSPEVLE
     VSSLTLHSVT PAVLQTGLPV ASEERTSGSH LVEDGLANVE ESEDFLSIDS LPSSSFTQPV
     PKETIPSMED SDVSLTSSPY LTSSIPFGLD SLTSKVKDQL KVSPFLPDAS MEKELIFDGG
     LGSGSGQKVD LITWPWSETS SEKSAEPLSK PWLEDDDSLL PAEIEDKKLV LVDKMDSTDQ
     ISKHSKYEHD DRSTHFPEEE PLSGPAVPIF ADTAAESASL TLPKHISEVP GVDDYSVTKA
     PLILTSVAIS ASTDKSDQAD AILREDMEQI TESSNYEWFD SEVSMVKPDM QTLWTILPES
     ERVWTRTSSL EKLSRDILAS TPQSADRLWL SVTQSTKLPP TTISTLLEDE VIMGVQDISL
     ELDRIGTDYY QPEQVQEQNG KVGSYVEMST SVHSTEMVSV AWPTEGGDDL SYTQTSGALV
     VFFSLRVTNM MFSEDLFNKN SLEYKALEQR FLELLVPYLQ SNLTGFQNLE ILNFRNGSIV
     VNSRMKFANS VPPNVNNAVY MILEDFCTTA YNTMNLAIDK YSLDVESGDE ANPCKFQACN
     EFSECLVNPW SGEAKCRCFP GYLSVEERPC QSLCDLQPDF CLNDGKCDIM PGHGAICRCR
     VGENWWYRGK HCEEFVSEPV IIGITIASVV GLLVIFSAII YFFIRTLQAH HDRSERESPF
     SGSSRQPDSL SSIENAVKYN PVYESHRAGC EKYEGPYPQH PFYSSASGDV IGGLSREEIR
     QMYESSELSR EEIQERMRVL ELYANDPEFA AFVREQQVEE V
//