ID IMPG1_HUMAN Reviewed; 797 AA. AC Q17R60; A6NNZ6; O43686; O95094; Q68D53; Q9BWZ1; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2006, sequence version 2. DT 27-MAR-2024, entry version 126. DE RecName: Full=Interphotoreceptor matrix proteoglycan 1; DE AltName: Full=Interphotoreceptor matrix proteoglycan of 150 kDa; DE Short=IPM-150; DE AltName: Full=Sialoprotein associated with cones and rods; DE Flags: Precursor; GN Name=IMPG1 {ECO:0000312|EMBL:AAI17453.1}; GN Synonyms=IPM150 {ECO:0000312|EMBL:AAC68835.1}, SPACR GN {ECO:0000303|PubMed:9813076}; 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] {ECO:0000312|EMBL:AAC68835.1} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9691169; DOI=10.1159/000015001; RA Felbor U., Gehrig A., Sauer C.G., Marquardt A., Koehler M., Schmid M., RA Weber B.H.F.; RT "Genomic organization and chromosomal localization of the RT interphotoreceptor matrix proteoglycan-1 (IMPG1) gene: a candidate for 6q- RT linked retinopathies."; RL Cytogenet. Cell Genet. 81:12-17(1998). RN [2] {ECO:0000305, ECO:0000312|EMBL:AAC03789.2} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 71-90, AND RP TISSUE SPECIFICITY. RC TISSUE=Retina {ECO:0000312|EMBL:AAC03789.2}; RX PubMed=10601738; DOI=10.1016/s0945-053x(99)00043-8; RA Kuehn M.H., Hageman G.S.; RT "Expression and characterization of the IPM 150 gene (IMPG1) product, a RT novel human photoreceptor cell-associated chondroitin-sulfate RT proteoglycan."; RL Matrix Biol. 18:509-518(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Retina; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [4] {ECO:0000312|EMBL:AL356962} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000305, ECO:0000312|EMBL:AAI17451.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ASP-518 RP AND TRP-704. RC TISSUE=Brain {ECO:0000312|EMBL:AAI17451.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] {ECO:0000305} RP PROTEIN SEQUENCE OF 71-79; 101-111; 249-265 AND 622-629, FUNCTION, RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=9813076; DOI=10.1074/jbc.273.47.31599; RA Acharya S., Rodriguez I.R., Moreira E.F., Midura R.J., Misono K., RA Todres E., Hollyfield J.G.; RT "SPACR, a novel interphotoreceptor matrix glycoprotein in human retina that RT interacts with hyaluronan."; RL J. Biol. Chem. 273:31599-31606(1998). RN [8] {ECO:0000305} RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION. RX PubMed=9719680; DOI=10.1093/glycob/8.10.997; RA Acharya S., Rayborn M.E., Hollyfield J.G.; RT "Characterization of SPACR, a sialoprotein associated with cones and rods RT present in the interphotoreceptor matrix of the human retina: immunological RT and lectin binding analysis."; RL Glycobiology 8:997-1006(1998). RN [9] 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 [10] RP INVOLVEMENT IN RP91, AND VARIANT RP91 PRO-579. RX PubMed=14691150; DOI=10.1167/iovs.03-0392; RA van Lith-Verhoeven J.J., Hoyng C.B., van den Helm B., Deutman A.F., RA Brink H.M., Kemperman M.H., de Jong W.H., Kremer H., Cremers F.P.; RT "The benign concentric annular macular dystrophy locus maps to 6p12.3- RT q16."; RL Invest. Ophthalmol. Vis. Sci. 45:30-35(2004). RN [11] RP INVOLVEMENT IN VMD4, AND VARIANTS VMD4 PRO-154 AND ARG-238. RX PubMed=23993198; DOI=10.1016/j.ajhg.2013.07.018; RA Manes G., Meunier I., Avila-Fernandez A., Banfi S., Le Meur G., RA Zanlonghi X., Corton M., Simonelli F., Brabet P., Labesse G., Audo I., RA Mohand-Said S., Zeitz C., Sahel J.A., Weber M., Dollfus H., Dhaenens C.M., RA Allorge D., De Baere E., Koenekoop R.K., Kohl S., Cremers F.P., RA Hollyfield J.G., Senechal A., Hebrard M., Bocquet B., Ayuso Garcia C., RA Hamel C.P.; RT "Mutations in IMPG1 cause vitelliform macular dystrophies."; RL Am. J. Hum. Genet. 93:571-578(2013). RN [12] RP VARIANT VMD4 ARG-238. 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 [13] RP VARIANT PRO-238. 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). RN [14] RP INVOLVEMENT IN RP91, AND VARIANTS RP91 PRO-579; PRO-613 AND PHE-626. RX PubMed=32817297; DOI=10.1136/jmedgenet-2020-107150; RA Olivier G., Corton M., Intartaglia D., Verbakel S.K., Sergouniotis P.I., RA Le Meur G., Dhaenens C.M., Naacke H., Avila-Fernandez A., Hoyng C.B., RA Klevering J., Bocquet B., Roubertie A., Senechal A., Banfi S., Muller A., RA Hamel C.L., Black G.C., Conte I., Roosing S., Zanlonghi X., Ayuso C., RA Meunier I., Manes G.; RT "Pathogenic variants in IMPG1 cause autosomal dominant and autosomal RT recessive retinitis pigmentosa."; RL J. Med. Genet. 58:570-578(2021). RN [15] RP VARIANT VMD4 PRO-154. RX PubMed=30688845; DOI=10.1097/icb.0000000000000843; RA Gupta M.P., Brodie S.E., Freund K.B.; RT "Unusual early-onset vitelliform dystrophy possibly linked to the RT interphotoreceptor matrix proteoglycan-1 p.Leu154Pro mutation."; RL Retin. Cases Brief Rep. 15:527-531(2021). CC -!- FUNCTION: Chondroitin sulfate-, heparin- and hyaluronan-binding protein CC (By similarity). May serve to form a basic macromolecular scaffold CC comprising the insoluble interphotoreceptor matrix (PubMed:9813076). CC {ECO:0000250|UniProtKB:Q8JIR8, ECO:0000269|PubMed:9813076}. CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, photoreceptor outer CC segment {ECO:0000269|PubMed:29777959}. Secreted, extracellular space, CC extracellular matrix, interphotoreceptor matrix CC {ECO:0000269|PubMed:29777959, ECO:0000269|PubMed:9719680, CC ECO:0000269|PubMed:9813076}. Photoreceptor inner segment CC {ECO:0000250|UniProtKB:Q8R1W8}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q17R60-1; Sequence=Displayed; CC Name=2; CC IsoId=Q17R60-2; Sequence=VSP_055981, VSP_055982, VSP_055983; CC -!- TISSUE SPECIFICITY: Expressed in the retina (at protein level) CC (PubMed:10601738, PubMed:29777959). In the retina, specifically CC expressed by cone and rod photoreceptor cells (PubMed:9813076). CC Localizes to cone and rod photoreceptor cells surrounding the CC interphotoreceptor matrix of the retina (PubMed:9719680). CC {ECO:0000269|PubMed:10601738, ECO:0000269|PubMed:29777959, CC ECO:0000269|PubMed:9719680, ECO:0000269|PubMed:9813076}. CC -!- DEVELOPMENTAL STAGE: Expressed in the retina lens at 6 weeks post- CC conception (WPC) (at protein level) (PubMed:29777959). Expressed in the CC neural retinal between 6 and 19 WPC (at protein level) CC (PubMed:29777959). Expressed in developing photoreceptors and emerging CC interphotoreceptor matrix between 12 and 19 WPC (at protein level) CC (PubMed:29777959). {ECO:0000269|PubMed:29777959}. CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:9719680}. CC -!- PTM: Highly glycosylated (N- and O-linked carbohydrates and sialic CC acid). {ECO:0000269|PubMed:9719680}. CC -!- DISEASE: Macular dystrophy, vitelliform, 4 (VMD4) [MIM:616151]: 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. VMD4 features include late-onset moderate visual CC impairment, small satellite drusen-like lesions in the foveal area, and CC preservation of retinal pigment epithelium reflectivity. CC {ECO:0000269|PubMed:23993198, ECO:0000269|PubMed:25085631, CC ECO:0000269|PubMed:30688845}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Retinitis pigmentosa 91 (RP91) [MIM:153870]: A form of CC retinitis pigmentosa, a retinal dystrophy belonging to the group of CC pigmentary retinopathies. Retinitis pigmentosa is characterized by CC retinal pigment deposits visible on fundus examination and primary loss CC of rod photoreceptor cells followed by secondary loss of cone CC photoreceptors. Patients typically have night vision blindness and loss CC of midperipheral visual field. RP91 is an autosomal dominant form with CC bone-spicule pigmentation, attenuation of retinal vessels, and optic CC disk pallor on funduscopy. Patients may also experience early macular CC involvement, with photophobia and reduced visual acuity, and some show CC a bull's eye pattern of macular atrophy. {ECO:0000269|PubMed:14691150, CC ECO:0000269|PubMed:32817297}. Note=The disease is caused by variants CC affecting the gene represented in this entry. 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; AF017776; AAC68835.1; -; Genomic_DNA. DR EMBL; AF017760; AAC68835.1; JOINED; Genomic_DNA. DR EMBL; AF017761; AAC68835.1; JOINED; Genomic_DNA. DR EMBL; AF017762; AAC68835.1; JOINED; Genomic_DNA. DR EMBL; AF017763; AAC68835.1; JOINED; Genomic_DNA. DR EMBL; AF017764; AAC68835.1; JOINED; Genomic_DNA. DR EMBL; AF017765; AAC68835.1; JOINED; Genomic_DNA. DR EMBL; AF017766; AAC68835.1; JOINED; Genomic_DNA. DR EMBL; AF017767; AAC68835.1; JOINED; Genomic_DNA. DR EMBL; AF017768; AAC68835.1; JOINED; Genomic_DNA. DR EMBL; AF017769; AAC68835.1; JOINED; Genomic_DNA. DR EMBL; AF017770; AAC68835.1; JOINED; Genomic_DNA. DR EMBL; AF017771; AAC68835.1; JOINED; Genomic_DNA. DR EMBL; AF017772; AAC68835.1; JOINED; Genomic_DNA. DR EMBL; AF017773; AAC68835.1; JOINED; Genomic_DNA. DR EMBL; AF017774; AAC68835.1; JOINED; Genomic_DNA. DR EMBL; AF017775; AAC68835.1; JOINED; Genomic_DNA. DR EMBL; AF047492; AAC03789.2; -; mRNA. DR EMBL; CR749572; CAH18367.1; -; mRNA. DR EMBL; AL356962; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL392166; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471051; EAW48726.1; -; Genomic_DNA. DR EMBL; BC117450; AAI17451.1; -; mRNA. DR EMBL; BC117452; AAI17453.1; -; mRNA. DR CCDS; CCDS4985.1; -. [Q17R60-1] DR RefSeq; NP_001269297.1; NM_001282368.1. DR RefSeq; NP_001554.2; NM_001563.3. [Q17R60-1] DR AlphaFoldDB; Q17R60; -. DR BioGRID; 109830; 3. DR STRING; 9606.ENSP00000358966; -. DR GlyCosmos; Q17R60; 12 sites, No reported glycans. DR GlyGen; Q17R60; 12 sites. DR iPTMnet; Q17R60; -. DR PhosphoSitePlus; Q17R60; -. DR BioMuta; IMPG1; -. DR DMDM; 115502232; -. DR MassIVE; Q17R60; -. DR PaxDb; 9606-ENSP00000358966; -. DR PeptideAtlas; Q17R60; -. DR ProteomicsDB; 61136; -. [Q17R60-1] DR ProteomicsDB; 66053; -. DR Antibodypedia; 55141; 58 antibodies from 12 providers. DR DNASU; 3617; -. DR Ensembl; ENST00000369950.8; ENSP00000358966.3; ENSG00000112706.12. [Q17R60-1] DR GeneID; 3617; -. DR KEGG; hsa:3617; -. DR MANE-Select; ENST00000369950.8; ENSP00000358966.3; NM_001563.4; NP_001554.2. DR UCSC; uc003pik.3; human. [Q17R60-1] DR AGR; HGNC:6055; -. DR CTD; 3617; -. DR DisGeNET; 3617; -. DR GeneCards; IMPG1; -. DR HGNC; HGNC:6055; IMPG1. DR HPA; ENSG00000112706; Tissue enriched (retina). DR MalaCards; IMPG1; -. DR MIM; 153870; phenotype. DR MIM; 602870; gene. DR MIM; 616151; phenotype. DR neXtProt; NX_Q17R60; -. DR OpenTargets; ENSG00000112706; -. DR Orphanet; 99000; Adult-onset foveomacular vitelliform dystrophy. DR Orphanet; 251287; Benign concentric annular macular dystrophy. DR Orphanet; 791; Retinitis pigmentosa. DR PharmGKB; PA29865; -. DR VEuPathDB; HostDB:ENSG00000112706; -. DR eggNOG; ENOG502QTXX; Eukaryota. DR GeneTree; ENSGT00530000063503; -. DR HOGENOM; CLU_005111_1_0_1; -. DR InParanoid; Q17R60; -. DR OMA; SECVMNE; -. DR OrthoDB; 4244504at2759; -. DR PhylomeDB; Q17R60; -. DR TreeFam; TF331340; -. DR PathwayCommons; Q17R60; -. DR BioGRID-ORCS; 3617; 4 hits in 1138 CRISPR screens. DR ChiTaRS; IMPG1; human. DR GeneWiki; IMPG1; -. DR GenomeRNAi; 3617; -. DR Pharos; Q17R60; Tbio. DR PRO; PR:Q17R60; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q17R60; Protein. DR Bgee; ENSG00000112706; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 89 other cell types or tissues. DR ExpressionAtlas; Q17R60; baseline and differential. DR GO; GO:0031012; C:extracellular matrix; TAS:ProtInc. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW. DR GO; GO:0033165; C:interphotoreceptor matrix; IEA:UniProtKB-SubCell. DR GO; GO:0001917; C:photoreceptor inner segment; IEA:UniProtKB-SubCell. DR GO; GO:0001750; C:photoreceptor outer segment; IEA:UniProtKB-SubCell. DR GO; GO:0035374; F:chondroitin sulfate binding; ISS:UniProtKB. DR GO; GO:0005201; F:extracellular matrix structural constituent; TAS:ProtInc. DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB. DR GO; GO:0005540; F:hyaluronic acid binding; ISS:UniProtKB. DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl. DR GO; GO:0007601; P:visual perception; TAS:ProtInc. DR Gene3D; 3.30.70.960; SEA domain; 2. 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:SF3; INTERPHOTORECEPTOR MATRIX PROTEOGLYCAN 1; 1. DR Pfam; PF01390; SEA; 2. DR SMART; SM00200; SEA; 2. DR SUPFAM; SSF82671; SEA domain; 2. DR PROSITE; PS50024; SEA; 2. DR Genevisible; Q17R60; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cell projection; Direct protein sequencing; KW Disease variant; Extracellular matrix; Glycoprotein; Heparin-binding; KW Hyaluronic acid; Receptor; Reference proteome; Repeat; KW Retinitis pigmentosa; Secreted; Sialic acid; Signal. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..797 FT /note="Interphotoreceptor matrix proteoglycan 1" FT /evidence="ECO:0000255" FT /id="PRO_0000252238" FT DOMAIN 232..354 FT /note="SEA 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188" FT DOMAIN 571..684 FT /note="SEA 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188" FT MOTIF 621..629 FT /note="Heparin- and hyaluronan-binding" FT /evidence="ECO:0000250|UniProtKB:Q8JIR8" FT CARBOHYD 42 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 143 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 191 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 215 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 403 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000255" FT CARBOHYD 421 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000255" FT CARBOHYD 432 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000255" FT CARBOHYD 442 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000255" FT CARBOHYD 592 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 616 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 630 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 648 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 23..100 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_055981" FT VAR_SEQ 188..225 FT /note="DVANVSLGPFPLTPDDTLLNEILDNTLNDTKMPTTERE -> EKNKGKTKPF FT NILQFGNNHHEHLLPIFCLLSSIIYTYY (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_055982" FT VAR_SEQ 226..797 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_055983" FT VARIANT 154 FT /note="L -> P (in VMD4; uncertain significance; FT dbSNP:rs713993047)" FT /evidence="ECO:0000269|PubMed:23993198, FT ECO:0000269|PubMed:30688845" FT /id="VAR_072668" FT VARIANT 238 FT /note="L -> P (found in a patient with vitelliform macular FT dystrophy; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28644393" FT /id="VAR_082192" FT VARIANT 238 FT /note="L -> R (in VMD4; dbSNP:rs713993045)" FT /evidence="ECO:0000269|PubMed:23993198, FT ECO:0000269|PubMed:25085631" FT /id="VAR_072669" FT VARIANT 463 FT /note="G -> V (in dbSNP:rs9443201)" FT /id="VAR_051069" FT VARIANT 518 FT /note="H -> D (in dbSNP:rs3734311)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_027793" FT VARIANT 569 FT /note="K -> R (in dbSNP:rs3734312)" FT /id="VAR_051070" FT VARIANT 579 FT /note="L -> P (in RP91; dbSNP:rs1782008883)" FT /evidence="ECO:0000269|PubMed:14691150, FT ECO:0000269|PubMed:32817297" FT /id="VAR_072670" FT VARIANT 613 FT /note="L -> P (in RP91; uncertain significance; FT dbSNP:rs1781948884)" FT /evidence="ECO:0000269|PubMed:32817297" FT /id="VAR_086246" FT VARIANT 626 FT /note="L -> F (in RP91; uncertain significance; FT dbSNP:rs1051579797)" FT /evidence="ECO:0000269|PubMed:32817297" FT /id="VAR_086247" FT VARIANT 704 FT /note="R -> W (in dbSNP:rs10943299)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_027794" FT VARIANT 711 FT /note="R -> H (in dbSNP:rs3734313)" FT /id="VAR_051071" FT VARIANT 761 FT /note="S -> N (in dbSNP:rs3778005)" FT /id="VAR_051072" SQ SEQUENCE 797 AA; 89387 MW; D017ED090C78D521 CRC64; MYLETRRAIF VFWIFLQVQG TKDISINIYH SETKDIDNPP RNETTESTEK MYKMSTMRRI FDLAKHRTKR SAFFPTGVKV CPQESMKQIL DSLQAYYRLR VCQEAVWEAY RIFLDRIPDT GEYQDWVSIC QQETFCLFDI GKNFSNSQEH LDLLQQRIKQ RSFPDRKDEI SAEKTLGEPG ETIVISTDVA NVSLGPFPLT PDDTLLNEIL DNTLNDTKMP TTERETEFAV LEEQRVELSV SLVNQKFKAE LADSQSPYYQ ELAGKSQLQM QKIFKKLPGF KKIHVLGFRP KKEKDGSSST EMQLTAIFKR HSAEAKSPAS DLLSFDSNKI ESEEVYHGTM EEDKQPEIYL TATDLKRLIS KALEEEQSLD VGTIQFTDEI AGSLPAFGPD TQSELPTSFA VITEDATLSP ELPPVEPQLE TVDGAEHGLP DTSWSPPAMA STSLSEAPPF FMASSIFSLT DQGTTDTMAT DQTMLVPGLT IPTSDYSAIS QLALGISHPP ASSDDSRSSA GGEDMVRHLD EMDLSDTPAP SEVPELSEYV SVPDHFLEDT TPVSALQYIT TSSMTIAPKG RELVVFFSLR VANMAFSNDL FNKSSLEYRA LEQQFTQLLV PYLRSNLTGF KQLEILNFRN GSVIVNSKMK FAKSVPYNLT KAVHGVLEDF RSAAAQQLHL EIDSYSLNIE PADQADPCKF LACGEFAQCV KNERTEEAEC RCKPGYDSQG SLDGLEPGLC GPGTKECEVL QGKGAPCRLP DHSENQAYKT SVKKFQNQQN NKVISKRNSE LLTVEYEEFN HQDWEGN //