IMPG1_HUMAN
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 03-AUG-2022, entry version 118.
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},
GN SPACR {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.
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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 GlyGen; Q17R60; 12 sites.
DR iPTMnet; Q17R60; -.
DR PhosphoSitePlus; Q17R60; -.
DR BioMuta; IMPG1; -.
DR DMDM; 115502232; -.
DR MassIVE; Q17R60; -.
DR PaxDb; Q17R60; -.
DR PeptideAtlas; Q17R60; -.
DR PRIDE; Q17R60; -.
DR ProteomicsDB; 61136; -. [Q17R60-1]
DR ProteomicsDB; 66053; -.
DR Antibodypedia; 55141; 41 antibodies from 11 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 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; FCIFDIG; -.
DR OrthoDB; 112459at2759; -.
DR PhylomeDB; Q17R60; -.
DR TreeFam; TF331340; -.
DR PathwayCommons; Q17R60; -.
DR BioGRID-ORCS; 3617; 4 hits in 1060 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 nucleus accumbens and 88 other tissues.
DR ExpressionAtlas; Q17R60; baseline and differential.
DR Genevisible; Q17R60; HS.
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; -; 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; PTHR12199; 1.
DR Pfam; PF01390; SEA; 2.
DR SMART; SM00200; SEA; 2.
DR SUPFAM; SSF82671; SSF82671; 2.
DR PROSITE; PS50024; SEA; 2.
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; unknown pathological 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; unknown pathological 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)"
FT /evidence="ECO:0000269|PubMed:14691150,
FT ECO:0000269|PubMed:32817297"
FT /id="VAR_072670"
FT VARIANT 613
FT /note="L -> P (in RP91; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:32817297"
FT /id="VAR_086246"
FT VARIANT 626
FT /note="L -> F (in RP91; unknown pathological significance)"
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
