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Interphotoreceptor matrix proteoglycan 2 (Interphotoreceptor matrix proteoglycan of 200 kDa) (IPM 200) (Sialoprotein associated with cones and rods proteoglycan) (Spacrcan)

 IMPG2_HUMAN             Reviewed;        1241 AA.
Q9BZV3; A8MWT5; Q9UKD4; Q9UKK5;
26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 3.
07-NOV-2018, entry version 114.
RecName: Full=Interphotoreceptor matrix proteoglycan 2;
AltName: Full=Interphotoreceptor matrix proteoglycan of 200 kDa;
Short=IPM 200;
AltName: Full=Sialoprotein associated with cones and rods proteoglycan;
Short=Spacrcan;
Flags: Precursor;
Name=IMPG2; Synonyms=IPM200;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND
VARIANT ILE-674.
PubMed=10542133; DOI=10.1006/mcbr.1999.0161;
Kuehn M.H., Hageman G.S.;
"Molecular characterization and genomic mapping of human IPM 200, a
second member of a novel family of proteoglycans.";
Mol. Cell Biol. Res. Commun. 2:103-110(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 82-86; 123-127 AND
582-593, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY,
FUNCTION, GLYCOSYLATION, AND VARIANT ILE-674.
PubMed=10702256; DOI=10.1074/jbc.275.10.6945;
Acharya S., Foletta V.C., Lee J.W., Rayborn M.E., Rodriguez I.R.,
Young W.S. III, Hollyfield J.G.;
"SPACRCAN, a novel human interphotoreceptor matrix hyaluronan-binding
proteoglycan synthesized by photoreceptors and pinealocytes.";
J. Biol. Chem. 275:6945-6955(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[4]
VARIANTS ILE-674 AND LEU-1013.
PubMed=11726612;
Kuehn M.H., Stone E.M., Hageman G.S.;
"Organization of the human IMPG2 gene and its evaluation as a
candidate gene in age-related macular degeneration and other retinal
degenerative disorders.";
Invest. Ophthalmol. Vis. Sci. 42:3123-3129(2001).
[5]
INVOLVEMENT IN RP56, INVOLVEMENT IN VMD5, AND VARIANT VMD5 LEU-124.
PubMed=20673862; DOI=10.1016/j.ajhg.2010.07.004;
Bandah-Rozenfeld D., Collin R.W., Banin E., van den Born L.I.,
Coene K.L., Siemiatkowska A.M., Zelinger L., Khan M.I., Lefeber D.J.,
Erdinest I., Testa F., Simonelli F., Voesenek K., Blokland E.A.,
Strom T.M., Klaver C.C., Qamar R., Banfi S., Cremers F.P., Sharon D.,
den Hollander A.I.;
"Mutations in IMPG2, encoding interphotoreceptor matrix proteoglycan
2, cause autosomal-recessive retinitis pigmentosa.";
Am. J. Hum. Genet. 87:199-208(2010).
[6]
INVOLVEMENT IN VMD5, AND VARIANT VMD5 PHE-1077.
PubMed=25085631; DOI=10.1016/j.ophtha.2014.06.028;
Meunier I., Manes G., Bocquet B., Marquette V., Baudoin C., Puech B.,
Defoort-Dhellemmes S., Audo I., Verdet R., Arndt C., Zanlonghi X.,
Le Meur G., Dhaenens C.M., Hamel C.P.;
"Frequency and clinical pattern of vitelliform macular dystrophy
caused by mutations of interphotoreceptor matrix IMPG1 and IMPG2
genes.";
Ophthalmology 121:2406-2414(2014).
-!- FUNCTION: Chondroitin sulfate- and hyaluronan-binding proteoglycan
involved in the organization of interphotoreceptor matrix; may
participate in the maturation and maintenance of the light-
sensitive photoreceptor outer segment. Binds heparin.
{ECO:0000269|PubMed:10702256}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed in the retina. Expressed by
photoreceptors of the interphotoreceptor matrix (IPM) surrounding
both rods and cones. IPM occupies the subretinal space between the
apices of the retinal pigment epithelium and the neural retina.
Detected in the pineal gland. {ECO:0000269|PubMed:10542133,
ECO:0000269|PubMed:10702256}.
-!- PTM: Highly glycosylated (N- and O-linked carbohydrates).
{ECO:0000269|PubMed:10702256}.
-!- DISEASE: Retinitis pigmentosa 56 (RP56) [MIM:613581]: A retinal
dystrophy belonging to the group of pigmentary retinopathies.
Retinitis pigmentosa is characterized by retinal pigment deposits
visible on fundus examination and primary loss of rod
photoreceptor cells followed by secondary loss of cone
photoreceptors. Patients typically have night vision blindness and
loss of midperipheral visual field. As their condition progresses,
they lose their far peripheral visual field and eventually central
vision as well. {ECO:0000269|PubMed:20673862}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Macular dystrophy, vitelliform, 5 (VMD5) [MIM:616152]: A
form of macular dystrophy, a retinal disease in which various
forms of deposits, pigmentary changes, and atrophic lesions are
observed in the macula lutea. Vitelliform macular dystrophies are
characterized by yellow, lipofuscin-containing deposits, usually
localized at the center of the macula. VMD5 features include late-
onset moderate visual impairment and preservation of retinal
pigment epithelium reflectivity. {ECO:0000269|PubMed:20673862,
ECO:0000269|PubMed:25085631}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; AF173155; AAF06999.1; -; mRNA.
EMBL; AF271379; AAG49889.1; -; Genomic_DNA.
EMBL; AF271363; AAG49889.1; JOINED; Genomic_DNA.
EMBL; AF271364; AAG49889.1; JOINED; Genomic_DNA.
EMBL; AF271365; AAG49889.1; JOINED; Genomic_DNA.
EMBL; AF271366; AAG49889.1; JOINED; Genomic_DNA.
EMBL; AF271367; AAG49889.1; JOINED; Genomic_DNA.
EMBL; AF271368; AAG49889.1; JOINED; Genomic_DNA.
EMBL; AF271369; AAG49889.1; JOINED; Genomic_DNA.
EMBL; AF271370; AAG49889.1; JOINED; Genomic_DNA.
EMBL; AF271371; AAG49889.1; JOINED; Genomic_DNA.
EMBL; AF271372; AAG49889.1; JOINED; Genomic_DNA.
EMBL; AF271373; AAG49889.1; JOINED; Genomic_DNA.
EMBL; AF271374; AAG49889.1; JOINED; Genomic_DNA.
EMBL; AF271375; AAG49889.1; JOINED; Genomic_DNA.
EMBL; AF271376; AAG49889.1; JOINED; Genomic_DNA.
EMBL; AF271377; AAG49889.1; JOINED; Genomic_DNA.
EMBL; AF271378; AAG49889.1; JOINED; Genomic_DNA.
EMBL; AF157624; AAF13154.1; -; mRNA.
EMBL; AC068764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS2940.1; -.
RefSeq; NP_057331.2; NM_016247.3.
UniGene; Hs.209249; -.
ProteinModelPortal; Q9BZV3; -.
SMR; Q9BZV3; -.
STRING; 9606.ENSP00000193391; -.
DrugBank; DB08818; Hyaluronic acid.
iPTMnet; Q9BZV3; -.
PhosphoSitePlus; Q9BZV3; -.
BioMuta; IMPG2; -.
DMDM; 296439325; -.
PaxDb; Q9BZV3; -.
PeptideAtlas; Q9BZV3; -.
PRIDE; Q9BZV3; -.
ProteomicsDB; 79907; -.
Ensembl; ENST00000193391; ENSP00000193391; ENSG00000081148.
GeneID; 50939; -.
KEGG; hsa:50939; -.
UCSC; uc003duq.3; human.
CTD; 50939; -.
DisGeNET; 50939; -.
EuPathDB; HostDB:ENSG00000081148.11; -.
GeneCards; IMPG2; -.
GeneReviews; IMPG2; -.
H-InvDB; HIX0030730; -.
HGNC; HGNC:18362; IMPG2.
HPA; HPA008779; -.
HPA; HPA015907; -.
MalaCards; IMPG2; -.
MIM; 607056; gene.
MIM; 613581; phenotype.
MIM; 616152; phenotype.
neXtProt; NX_Q9BZV3; -.
OpenTargets; ENSG00000081148; -.
Orphanet; 99000; Adult-onset foveomacular vitelliform dystrophy.
Orphanet; 791; Retinitis pigmentosa.
PharmGKB; PA29866; -.
eggNOG; ENOG410IH0G; Eukaryota.
eggNOG; ENOG410Y9FF; LUCA.
GeneTree; ENSGT00530000063503; -.
HOGENOM; HOG000113064; -.
HOVERGEN; HBG108006; -.
InParanoid; Q9BZV3; -.
KO; K19017; -.
OMA; EELPCQS; -.
OrthoDB; EOG091G00XU; -.
PhylomeDB; Q9BZV3; -.
TreeFam; TF331340; -.
ChiTaRS; IMPG2; human.
GenomeRNAi; 50939; -.
PRO; PR:Q9BZV3; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000081148; Expressed in 40 organ(s), highest expression level in oviduct epithelium.
CleanEx; HS_IMPG2; -.
ExpressionAtlas; Q9BZV3; baseline and differential.
Genevisible; Q9BZV3; HS.
GO; GO:0031012; C:extracellular matrix; TAS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0033165; C:interphotoreceptor matrix; IEA:InterPro.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0005201; F:extracellular matrix structural constituent; TAS:UniProtKB.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0005540; F:hyaluronic acid binding; TAS:UniProtKB.
GO; GO:0007601; P:visual perception; TAS:UniProtKB.
Gene3D; 3.30.70.960; -; 1.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR039861; IMPG.
InterPro; IPR032975; IMPG2.
InterPro; IPR000082; SEA_dom.
InterPro; IPR036364; SEA_dom_sf.
PANTHER; PTHR12199; PTHR12199; 1.
PANTHER; PTHR12199:SF4; PTHR12199:SF4; 1.
Pfam; PF01390; SEA; 2.
SMART; SM00200; SEA; 2.
SUPFAM; SSF82671; SSF82671; 2.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 2.
PROSITE; PS50024; SEA; 2.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disease mutation;
Disulfide bond; EGF-like domain; Glycoprotein; Heparin-binding;
Membrane; Polymorphism; Receptor; Reference proteome; Repeat;
Retinitis pigmentosa; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 1241 Interphotoreceptor matrix proteoglycan 2.
/FTId=PRO_0000320149.
TOPO_DOM 23 1099 Extracellular. {ECO:0000255}.
TRANSMEM 1100 1120 Helical. {ECO:0000255}.
TOPO_DOM 1121 1241 Cytoplasmic. {ECO:0000255}.
DOMAIN 239 353 SEA 1. {ECO:0000255|PROSITE-
ProRule:PRU00188}.
DOMAIN 897 1010 SEA 2. {ECO:0000255|PROSITE-
ProRule:PRU00188}.
DOMAIN 1010 1051 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1052 1093 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REGION 259 267 Hyaluronan-binding motif involved in
chondroitin sulfate A-binding.
{ECO:0000250}.
REGION 1080 1088 Hyaluronan-binding motif involved in
chondroitin sulfate C-binding.
{ECO:0000250}.
REGION 1125 1133 Hyaluronan-binding motif involved in
chondroitin sulfate A- and C-binding.
{ECO:0000250}.
REGION 1136 1145 Hyaluronan-binding motif involved in
chondroitin sulfate C-binding.
{ECO:0000250}.
REGION 1210 1218 Hyaluronan-binding motif involved in
chondroitin sulfate A- and C-binding
motif. {ECO:0000250}.
CARBOHYD 154 154 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 190 190 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 192 192 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 301 301 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 320 320 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 370 370 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 544 544 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 556 556 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 942 942 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 956 956 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 1014 1025 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1019 1036 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1038 1050 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1054 1067 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1061 1077 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1079 1092 {ECO:0000255|PROSITE-ProRule:PRU00076}.
VARIANT 124 124 F -> L (in VMD5; dbSNP:rs201893545).
{ECO:0000269|PubMed:20673862}.
/FTId=VAR_064336.
VARIANT 344 344 K -> N (in dbSNP:rs34375459).
/FTId=VAR_039144.
VARIANT 674 674 T -> I (in dbSNP:rs571391).
{ECO:0000269|PubMed:10542133,
ECO:0000269|PubMed:10702256,
ECO:0000269|PubMed:11726612}.
/FTId=VAR_039145.
VARIANT 1013 1013 P -> L (in dbSNP:rs116450347).
{ECO:0000269|PubMed:11726612}.
/FTId=VAR_039146.
VARIANT 1077 1077 C -> F (in VMD5; dbSNP:rs713993049).
{ECO:0000269|PubMed:25085631}.
/FTId=VAR_072671.
CONFLICT 5 5 P -> L (in Ref. 2; AAF13154).
{ECO:0000305}.
CONFLICT 77 77 I -> T (in Ref. 2; AAF13154).
{ECO:0000305}.
CONFLICT 668 668 E -> V (in Ref. 2; AAF13154).
{ECO:0000305}.
CONFLICT 715 715 Y -> C (in Ref. 1; AAF06999).
{ECO:0000305}.
CONFLICT 1012 1012 N -> T (in Ref. 1; AAG49889).
{ECO:0000305}.
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


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