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Interphotoreceptor matrix proteoglycan 1 (Interphotoreceptor matrix proteoglycan of 150 kDa) (IPM-150) (Sialoprotein associated with cones and rods)

 IMPG1_HUMAN             Reviewed;         797 AA.
Q17R60; A6NNZ6; O43686; O95094; Q68D53; Q9BWZ1;
03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
03-OCT-2006, sequence version 2.
07-NOV-2018, entry version 98.
RecName: Full=Interphotoreceptor matrix proteoglycan 1;
AltName: Full=Interphotoreceptor matrix proteoglycan of 150 kDa;
Short=IPM-150;
AltName: Full=Sialoprotein associated with cones and rods;
Flags: Precursor;
Name=IMPG1 {ECO:0000312|EMBL:AAI17453.1};
Synonyms=IPM150 {ECO:0000312|EMBL:AAC68835.1},
SPACR {ECO:0000303|PubMed:9813076};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000312|EMBL:AAC68835.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9691169;
Felbor U., Gehrig A., Sauer C.G., Marquardt A., Koehler M., Schmid M.,
Weber B.H.F.;
"Genomic organization and chromosomal localization of the
interphotoreceptor matrix proteoglycan-1 (IMPG1) gene: a candidate for
6q-linked retinopathies.";
Cytogenet. Cell Genet. 81:12-17(1998).
[2] {ECO:0000305, ECO:0000312|EMBL:AAC03789.2}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 71-90, AND
TISSUE SPECIFICITY.
TISSUE=Retina {ECO:0000312|EMBL:AAC03789.2};
PubMed=10601738; DOI=10.1016/S0945-053X(99)00043-8;
Kuehn M.H., Hageman G.S.;
"Expression and characterization of the IPM 150 gene (IMPG1) product,
a novel human photoreceptor cell-associated chondroitin-sulfate
proteoglycan.";
Matrix Biol. 18:509-518(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Retina;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4] {ECO:0000312|EMBL:AL356962}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000305, ECO:0000312|EMBL:AAI17451.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
ASP-518 AND TRP-704.
TISSUE=Brain {ECO:0000312|EMBL:AAI17451.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7] {ECO:0000305}
PROTEIN SEQUENCE OF 71-79; 101-111; 249-265 AND 622-629, FUNCTION,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=9813076; DOI=10.1074/jbc.273.47.31599;
Acharya S., Rodriguez I.R., Moreira E.F., Midura R.J., Misono K.,
Todres E., Hollyfield J.G.;
"SPACR, a novel interphotoreceptor matrix glycoprotein in human retina
that interacts with hyaluronan.";
J. Biol. Chem. 273:31599-31606(1998).
[8] {ECO:0000305}
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
PubMed=9719680; DOI=10.1093/glycob/8.10.997;
Acharya S., Rayborn M.E., Hollyfield J.G.;
"Characterization of SPACR, a sialoprotein associated with cones and
rods present in the interphotoreceptor matrix of the human retina:
immunological and lectin binding analysis.";
Glycobiology 8:997-1006(1998).
[9]
VARIANT PRO-579.
PubMed=14691150; DOI=10.1167/iovs.03-0392;
van Lith-Verhoeven J.J., Hoyng C.B., van den Helm B., Deutman A.F.,
Brink H.M., Kemperman M.H., de Jong W.H., Kremer H., Cremers F.P.;
"The benign concentric annular macular dystrophy locus maps to 6p12.3-
q16.";
Invest. Ophthalmol. Vis. Sci. 45:30-35(2004).
[10]
INVOLVEMENT IN VMD4, AND VARIANTS VMD4 PRO-154 AND ARG-238.
PubMed=23993198; DOI=10.1016/j.ajhg.2013.07.018;
Manes G., Meunier I., Avila-Fernandez A., Banfi S., Le Meur G.,
Zanlonghi X., Corton M., Simonelli F., Brabet P., Labesse G., Audo I.,
Mohand-Said S., Zeitz C., Sahel J.A., Weber M., Dollfus H.,
Dhaenens C.M., Allorge D., De Baere E., Koenekoop R.K., Kohl S.,
Cremers F.P., Hollyfield J.G., Senechal A., Hebrard M., Bocquet B.,
Ayuso Garcia C., Hamel C.P.;
"Mutations in IMPG1 cause vitelliform macular dystrophies.";
Am. J. Hum. Genet. 93:571-578(2013).
-!- FUNCTION: May interact with hyaluronan which may serve to form a
basic macromolecular scaffold comprising the insoluble
interphotoreceptor matrix. {ECO:0000269|PubMed:9813076}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q17R60-1; Sequence=Displayed;
Name=2;
IsoId=Q17R60-2; Sequence=VSP_055981, VSP_055982, VSP_055983;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Abundantly expressed in retina where it is
specifically expressed by cone and rod photoreceptor cells.
Localizes to cone and rod photoreceptor cells surrounding the
interphotoreceptor matrix of the retina.
{ECO:0000269|PubMed:10601738, ECO:0000269|PubMed:9719680,
ECO:0000269|PubMed:9813076}.
-!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:9719680}.
-!- PTM: Highly glycosylated (N- and O-linked carbohydrates and sialic
acid). {ECO:0000269|PubMed:9719680}.
-!- DISEASE: Macular dystrophy, vitelliform, 4 (VMD4) [MIM:616151]: 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. VMD4 features include late-
onset moderate visual impairment, small satellite drusen-like
lesions in the foveal area, and preservation of retinal pigment
epithelium reflectivity. {ECO:0000269|PubMed:23993198}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
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EMBL; AF017776; AAC68835.1; -; Genomic_DNA.
EMBL; AF017760; AAC68835.1; JOINED; Genomic_DNA.
EMBL; AF017761; AAC68835.1; JOINED; Genomic_DNA.
EMBL; AF017762; AAC68835.1; JOINED; Genomic_DNA.
EMBL; AF017763; AAC68835.1; JOINED; Genomic_DNA.
EMBL; AF017764; AAC68835.1; JOINED; Genomic_DNA.
EMBL; AF017765; AAC68835.1; JOINED; Genomic_DNA.
EMBL; AF017766; AAC68835.1; JOINED; Genomic_DNA.
EMBL; AF017767; AAC68835.1; JOINED; Genomic_DNA.
EMBL; AF017768; AAC68835.1; JOINED; Genomic_DNA.
EMBL; AF017769; AAC68835.1; JOINED; Genomic_DNA.
EMBL; AF017770; AAC68835.1; JOINED; Genomic_DNA.
EMBL; AF017771; AAC68835.1; JOINED; Genomic_DNA.
EMBL; AF017772; AAC68835.1; JOINED; Genomic_DNA.
EMBL; AF017773; AAC68835.1; JOINED; Genomic_DNA.
EMBL; AF017774; AAC68835.1; JOINED; Genomic_DNA.
EMBL; AF017775; AAC68835.1; JOINED; Genomic_DNA.
EMBL; AF047492; AAC03789.2; -; mRNA.
EMBL; CR749572; CAH18367.1; -; mRNA.
EMBL; AL356962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL392166; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471051; EAW48726.1; -; Genomic_DNA.
EMBL; BC117450; AAI17451.1; -; mRNA.
EMBL; BC117452; AAI17453.1; -; mRNA.
CCDS; CCDS4985.1; -. [Q17R60-1]
RefSeq; NP_001269297.1; NM_001282368.1.
RefSeq; NP_001554.2; NM_001563.3. [Q17R60-1]
UniGene; Hs.590893; -.
ProteinModelPortal; Q17R60; -.
SMR; Q17R60; -.
BioGrid; 109830; 2.
STRING; 9606.ENSP00000358966; -.
iPTMnet; Q17R60; -.
PhosphoSitePlus; Q17R60; -.
BioMuta; IMPG1; -.
DMDM; 115502232; -.
PaxDb; Q17R60; -.
PeptideAtlas; Q17R60; -.
PRIDE; Q17R60; -.
ProteomicsDB; 61136; -.
DNASU; 3617; -.
Ensembl; ENST00000369950; ENSP00000358966; ENSG00000112706. [Q17R60-1]
GeneID; 3617; -.
KEGG; hsa:3617; -.
UCSC; uc003pik.3; human. [Q17R60-1]
CTD; 3617; -.
DisGeNET; 3617; -.
EuPathDB; HostDB:ENSG00000112706.11; -.
GeneCards; IMPG1; -.
HGNC; HGNC:6055; IMPG1.
HPA; HPA027142; -.
HPA; HPA030332; -.
HPA; HPA030333; -.
MalaCards; IMPG1; -.
MIM; 602870; gene.
MIM; 616151; phenotype.
neXtProt; NX_Q17R60; -.
OpenTargets; ENSG00000112706; -.
Orphanet; 99000; Adult-onset foveomacular vitelliform dystrophy.
PharmGKB; PA29865; -.
eggNOG; ENOG410IH0G; Eukaryota.
eggNOG; ENOG410Y9FF; LUCA.
GeneTree; ENSGT00530000063503; -.
HOGENOM; HOG000113063; -.
HOVERGEN; HBG081793; -.
InParanoid; Q17R60; -.
KO; K19016; -.
OMA; EIHVLGF; -.
OrthoDB; EOG091G094N; -.
PhylomeDB; Q17R60; -.
TreeFam; TF331340; -.
ChiTaRS; IMPG1; human.
GeneWiki; IMPG1; -.
GenomeRNAi; 3617; -.
PRO; PR:Q17R60; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000112706; Expressed in 87 organ(s), highest expression level in caudate nucleus.
CleanEx; HS_IMPG1; -.
ExpressionAtlas; Q17R60; baseline and differential.
Genevisible; Q17R60; HS.
GO; GO:0031012; C:extracellular matrix; TAS:ProtInc.
GO; GO:0005201; F:extracellular matrix structural constituent; TAS:ProtInc.
GO; GO:0007601; P:visual perception; TAS:ProtInc.
Gene3D; 3.30.70.960; -; 2.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR039861; IMPG.
InterPro; IPR000082; SEA_dom.
InterPro; IPR036364; SEA_dom_sf.
PANTHER; PTHR12199; PTHR12199; 1.
Pfam; PF01390; SEA; 2.
SMART; SM00200; SEA; 2.
SUPFAM; SSF82671; SSF82671; 2.
PROSITE; PS50024; SEA; 2.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Direct protein sequencing;
Disease mutation; Glycoprotein; Polymorphism; Receptor;
Reference proteome; Repeat; Secreted; Sialic acid; Signal.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 797 Interphotoreceptor matrix proteoglycan 1.
{ECO:0000255}.
/FTId=PRO_0000252238.
DOMAIN 232 354 SEA 1. {ECO:0000255|PROSITE-
ProRule:PRU00188}.
DOMAIN 571 684 SEA 2. {ECO:0000255|PROSITE-
ProRule:PRU00188}.
CARBOHYD 42 42 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 143 143 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 191 191 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 215 215 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 403 403 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 421 421 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 432 432 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 442 442 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 592 592 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 616 616 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 630 630 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 648 648 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 23 100 Missing (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_055981.
VAR_SEQ 188 225 DVANVSLGPFPLTPDDTLLNEILDNTLNDTKMPTTERE ->
EKNKGKTKPFNILQFGNNHHEHLLPIFCLLSSIIYTYY
(in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_055982.
VAR_SEQ 226 797 Missing (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_055983.
VARIANT 154 154 L -> P (in VMD4; dbSNP:rs713993047).
{ECO:0000269|PubMed:23993198}.
/FTId=VAR_072668.
VARIANT 238 238 L -> R (in VMD4; dbSNP:rs713993045).
{ECO:0000269|PubMed:23993198}.
/FTId=VAR_072669.
VARIANT 463 463 G -> V (in dbSNP:rs9443201).
/FTId=VAR_051069.
VARIANT 518 518 H -> D (in dbSNP:rs3734311).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_027793.
VARIANT 569 569 K -> R (in dbSNP:rs3734312).
/FTId=VAR_051070.
VARIANT 579 579 L -> P (found in a family with benign
concentric annular macular dystrophy;
unknown pathological significance).
{ECO:0000269|PubMed:14691150}.
/FTId=VAR_072670.
VARIANT 704 704 R -> W (in dbSNP:rs10943299).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_027794.
VARIANT 711 711 R -> H (in dbSNP:rs3734313).
/FTId=VAR_051071.
VARIANT 761 761 S -> N (in dbSNP:rs3778005).
/FTId=VAR_051072.
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


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