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 15-FEB-2017, entry version 105. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND RP VARIANT 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 RT second 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 RP 582-593, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, RP FUNCTION, 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., RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., RA 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., RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., RA Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [4] 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 RT candidate gene in age-related macular degeneration and other retinal RT degenerative disorders."; RL Invest. Ophthalmol. Vis. Sci. 42:3123-3129(2001). RN [5] 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., RA Coene K.L., Siemiatkowska A.M., Zelinger L., Khan M.I., Lefeber D.J., RA Erdinest I., Testa F., Simonelli F., Voesenek K., Blokland E.A., RA Strom T.M., 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 RT 2, cause autosomal-recessive retinitis pigmentosa."; RL Am. J. Hum. Genet. 87:199-208(2010). RN [6] 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 RT caused by mutations of interphotoreceptor matrix IMPG1 and IMPG2 RT genes."; RL Ophthalmology 121:2406-2414(2014). 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- CC sensitive photoreceptor outer segment. Binds heparin. CC {ECO:0000269|PubMed:10702256}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Expressed in the retina. Expressed by CC photoreceptors of the interphotoreceptor matrix (IPM) surrounding CC both rods and cones. IPM occupies the subretinal space between the CC apices of the retinal pigment epithelium and the neural retina. CC Detected in the pineal gland. {ECO:0000269|PubMed:10542133, CC ECO:0000269|PubMed:10702256}. 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. CC Retinitis pigmentosa is characterized by retinal pigment deposits CC visible on fundus examination and primary loss of rod CC photoreceptor cells followed by secondary loss of cone CC photoreceptors. Patients typically have night vision blindness and CC loss of midperipheral visual field. As their condition progresses, CC they lose their far peripheral visual field and eventually central CC vision as well. {ECO:0000269|PubMed:20673862}. Note=The disease is CC caused by mutations affecting the gene represented in this entry. CC -!- DISEASE: Macular dystrophy, vitelliform, 5 (VMD5) [MIM:616152]: A CC form of macular dystrophy, a retinal disease in which various CC forms of deposits, pigmentary changes, and atrophic lesions are CC observed in the macula lutea. Vitelliform macular dystrophies are CC characterized by yellow, lipofuscin-containing deposits, usually CC localized at the center of the macula. VMD5 features include late- CC onset moderate visual impairment and preservation of retinal CC pigment epithelium reflectivity. {ECO:0000269|PubMed:20673862, CC ECO:0000269|PubMed:25085631}. Note=The disease is caused by CC mutations 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; 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 UniGene; Hs.209249; -. DR ProteinModelPortal; Q9BZV3; -. DR SMR; Q9BZV3; -. DR STRING; 9606.ENSP00000193391; -. DR DrugBank; DB08818; Hyaluronic acid. DR iPTMnet; Q9BZV3; -. DR PhosphoSitePlus; Q9BZV3; -. DR BioMuta; IMPG2; -. DR DMDM; 296439325; -. DR PaxDb; Q9BZV3; -. DR PeptideAtlas; Q9BZV3; -. DR PRIDE; Q9BZV3; -. DR Ensembl; ENST00000193391; ENSP00000193391; ENSG00000081148. DR GeneID; 50939; -. DR KEGG; hsa:50939; -. DR UCSC; uc003duq.3; human. DR CTD; 50939; -. DR DisGeNET; 50939; -. DR GeneCards; IMPG2; -. DR GeneReviews; IMPG2; -. DR H-InvDB; HIX0030730; -. DR HGNC; HGNC:18362; IMPG2. DR HPA; HPA008779; -. DR HPA; HPA015907; -. DR MalaCards; IMPG2; -. DR MIM; 607056; gene. DR MIM; 613581; phenotype. DR MIM; 616152; phenotype. DR neXtProt; NX_Q9BZV3; -. DR OpenTargets; ENSG00000081148; -. DR Orphanet; 791; Retinitis pigmentosa. DR PharmGKB; PA29866; -. DR eggNOG; ENOG410IH0G; Eukaryota. DR eggNOG; ENOG410Y9FF; LUCA. DR GeneTree; ENSGT00530000063503; -. DR HOGENOM; HOG000113064; -. DR HOVERGEN; HBG108006; -. DR InParanoid; Q9BZV3; -. DR KO; K19017; -. DR OMA; WNTQSSS; -. DR OrthoDB; EOG091G00XU; -. DR PhylomeDB; Q9BZV3; -. DR TreeFam; TF331340; -. DR ChiTaRS; IMPG2; human. DR GenomeRNAi; 50939; -. DR PRO; PR:Q9BZV3; -. DR Proteomes; UP000005640; Chromosome 3. DR Bgee; ENSG00000081148; -. DR CleanEx; HS_IMPG2; -. DR ExpressionAtlas; Q9BZV3; baseline and differential. DR Genevisible; Q9BZV3; HS. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0033165; C:interphotoreceptor matrix; IEA:InterPro. DR GO; GO:0005578; C:proteinaceous extracellular matrix; TAS:UniProtKB. 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; IEA:UniProtKB-KW. DR GO; GO:0005540; F:hyaluronic acid binding; TAS:UniProtKB. DR GO; GO:0007601; P:visual perception; TAS:UniProtKB. DR Gene3D; 3.30.70.960; -; 2. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR032975; IMPG2. DR InterPro; IPR000082; SEA_dom. DR PANTHER; PTHR12199:SF13; PTHR12199:SF13; 1. DR Pfam; PF01390; SEA; 2. DR SMART; SM00200; SEA; 2. DR SUPFAM; SSF82671; SSF82671; 2. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 2. DR PROSITE; PS50024; SEA; 2. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Disease mutation; KW Disulfide bond; EGF-like domain; Glycoprotein; Heparin-binding; KW Membrane; Polymorphism; Receptor; Reference proteome; Repeat; KW Retinitis pigmentosa; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1 22 {ECO:0000255}. FT CHAIN 23 1241 Interphotoreceptor matrix proteoglycan 2. FT /FTId=PRO_0000320149. FT TOPO_DOM 23 1099 Extracellular. {ECO:0000255}. FT TRANSMEM 1100 1120 Helical. {ECO:0000255}. FT TOPO_DOM 1121 1241 Cytoplasmic. {ECO:0000255}. FT DOMAIN 239 353 SEA 1. {ECO:0000255|PROSITE- FT ProRule:PRU00188}. FT DOMAIN 897 1010 SEA 2. {ECO:0000255|PROSITE- FT ProRule:PRU00188}. FT DOMAIN 1010 1051 EGF-like 1. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 1052 1093 EGF-like 2. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT REGION 259 267 Hyaluronan-binding motif involved in FT chondroitin sulfate A-binding. FT {ECO:0000250}. FT REGION 1080 1088 Hyaluronan-binding motif involved in FT chondroitin sulfate C-binding. FT {ECO:0000250}. FT REGION 1125 1133 Hyaluronan-binding motif involved in FT chondroitin sulfate A- and C-binding. FT {ECO:0000250}. FT REGION 1136 1145 Hyaluronan-binding motif involved in FT chondroitin sulfate C-binding. FT {ECO:0000250}. FT REGION 1210 1218 Hyaluronan-binding motif involved in FT chondroitin sulfate A- and C-binding FT motif. {ECO:0000250}. FT CARBOHYD 154 154 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 190 190 O-linked (GalNAc...). {ECO:0000255}. FT CARBOHYD 192 192 O-linked (GalNAc...). {ECO:0000255}. FT CARBOHYD 301 301 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 320 320 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 370 370 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 544 544 O-linked (GalNAc...). {ECO:0000255}. FT CARBOHYD 556 556 O-linked (GalNAc...). {ECO:0000255}. FT CARBOHYD 942 942 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 956 956 N-linked (GlcNAc...). {ECO:0000255}. FT DISULFID 1014 1025 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 1019 1036 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 1038 1050 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 1054 1067 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 1061 1077 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 1079 1092 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT VARIANT 124 124 F -> L (in VMD5; dbSNP:rs201893545). FT {ECO:0000269|PubMed:20673862}. FT /FTId=VAR_064336. FT VARIANT 344 344 K -> N (in dbSNP:rs34375459). FT /FTId=VAR_039144. FT VARIANT 674 674 T -> I (in dbSNP:rs571391). FT {ECO:0000269|PubMed:10542133, FT ECO:0000269|PubMed:10702256, FT ECO:0000269|PubMed:11726612}. FT /FTId=VAR_039145. FT VARIANT 1013 1013 P -> L (in dbSNP:rs116450347). FT {ECO:0000269|PubMed:11726612}. FT /FTId=VAR_039146. FT VARIANT 1077 1077 C -> F (in VMD5; dbSNP:rs713993049). FT {ECO:0000269|PubMed:25085631}. FT /FTId=VAR_072671. FT CONFLICT 5 5 P -> L (in Ref. 2; AAF13154). FT {ECO:0000305}. FT CONFLICT 77 77 I -> T (in Ref. 2; AAF13154). FT {ECO:0000305}. FT CONFLICT 668 668 E -> V (in Ref. 2; AAF13154). FT {ECO:0000305}. FT CONFLICT 715 715 Y -> C (in Ref. 1; AAF06999). FT {ECO:0000305}. FT CONFLICT 1012 1012 N -> T (in Ref. 1; AAG49889). FT {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 //