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Q9BZV3

- IMPG2_HUMAN

UniProt

Q9BZV3 - IMPG2_HUMAN

Protein

Interphotoreceptor matrix proteoglycan 2

Gene

IMPG2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 3 (18 May 2010)
      Previous versions | rss
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    Functioni

    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.1 Publication

    GO - Molecular functioni

    1. extracellular matrix structural constituent Source: UniProtKB
    2. heparin binding Source: UniProtKB-KW
    3. hyaluronic acid binding Source: UniProtKB

    GO - Biological processi

    1. visual perception Source: UniProtKB

    Keywords - Molecular functioni

    Receptor

    Keywords - Ligandi

    Heparin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Interphotoreceptor matrix proteoglycan 2
    Alternative name(s):
    Interphotoreceptor matrix proteoglycan of 200 kDa
    Short name:
    IPM 200
    Sialoprotein associated with cones and rods proteoglycan
    Short name:
    Spacrcan
    Gene namesi
    Name:IMPG2
    Synonyms:IPM200
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:18362. IMPG2.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. proteinaceous extracellular matrix Source: UniProtKB
    3. receptor complex Source: MGI

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Maculopathy, IMPG2-related (MACLP-IMPG2) [MIM:613581]: A mild maculopathy characterized by full-field electroretinogram responses within normal limits, normal color vision, elevation of the photoreceptor layer in the foveal region and mild nuclear sclerosis.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti124 – 1241F → L in MACLP-IMPG2. 1 Publication
    VAR_064336

    Keywords - Diseasei

    Disease mutation, Retinitis pigmentosa

    Organism-specific databases

    MIMi613581. phenotype.
    Orphaneti791. Retinitis pigmentosa.
    PharmGKBiPA29866.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 12411219Interphotoreceptor matrix proteoglycan 2PRO_0000320149Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi154 – 1541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi190 – 1901O-linked (GalNAc...)Sequence Analysis
    Glycosylationi192 – 1921O-linked (GalNAc...)Sequence Analysis
    Glycosylationi301 – 3011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi320 – 3201N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi370 – 3701N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi544 – 5441O-linked (GalNAc...)Sequence Analysis
    Glycosylationi556 – 5561O-linked (GalNAc...)Sequence Analysis
    Glycosylationi942 – 9421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi956 – 9561N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1014 ↔ 1025PROSITE-ProRule annotation
    Disulfide bondi1019 ↔ 1036PROSITE-ProRule annotation
    Disulfide bondi1038 ↔ 1050PROSITE-ProRule annotation
    Disulfide bondi1054 ↔ 1067PROSITE-ProRule annotation
    Disulfide bondi1061 ↔ 1077PROSITE-ProRule annotation
    Disulfide bondi1079 ↔ 1092PROSITE-ProRule annotation

    Post-translational modificationi

    Highly glycosylated (N- and O-linked carbohydrates).1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9BZV3.
    PRIDEiQ9BZV3.

    PTM databases

    PhosphoSiteiQ9BZV3.

    Expressioni

    Tissue specificityi

    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.2 Publications

    Gene expression databases

    ArrayExpressiQ9BZV3.
    BgeeiQ9BZV3.
    CleanExiHS_IMPG2.
    GenevestigatoriQ9BZV3.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000193391.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BZV3.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini23 – 10991077ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1121 – 1241121CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1100 – 112021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini239 – 353115SEA 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini897 – 1010114SEA 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1010 – 105142EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1052 – 109342EGF-like 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni259 – 2679Hyaluronan-binding motif involved in chondroitin sulfate A-bindingBy similarity
    Regioni1080 – 10889Hyaluronan-binding motif involved in chondroitin sulfate C-bindingBy similarity
    Regioni1125 – 11339Hyaluronan-binding motif involved in chondroitin sulfate A- and C-bindingBy similarity
    Regioni1136 – 114510Hyaluronan-binding motif involved in chondroitin sulfate C-bindingBy similarity
    Regioni1210 – 12189Hyaluronan-binding motif involved in chondroitin sulfate A- and C-binding motifBy similarity

    Sequence similaritiesi

    Contains 2 EGF-like domains.PROSITE-ProRule annotation
    Contains 2 SEA domains.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG17485.
    HOGENOMiHOG000113064.
    HOVERGENiHBG108006.
    InParanoidiQ9BZV3.
    OMAiWPWSETS.
    OrthoDBiEOG7TXKFR.
    PhylomeDBiQ9BZV3.
    TreeFamiTF331340.

    Family and domain databases

    Gene3Di3.30.70.960. 2 hits.
    InterProiIPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR000082. SEA_dom.
    [Graphical view]
    PfamiPF01390. SEA. 2 hits.
    [Graphical view]
    SMARTiSM00200. SEA. 2 hits.
    [Graphical view]
    SUPFAMiSSF82671. SSF82671. 2 hits.
    PROSITEiPS01186. EGF_2. 1 hit.
    PS50026. EGF_3. 2 hits.
    PS50024. SEA. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9BZV3-1 [UniParc]FASTAAdd to Basket

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    MIMFPLFGKI SLGILIFVLI EGDFPSLTAQ TYLSIEEIQE PKSAVSFLLP     50
    EESTDLSLAT KKKQPLDRRE TERQWLIRRR RSILFPNGVK ICPDESVAEA 100
    VANHVKYFKV RVCQEAVWEA FRTFWDRLPG REEYHYWMNL CEDGVTSIFE 150
    MGTNFSESVE HRSLIMKKLT YAKETVSSSE LSSPVPVGDT STLGDTTLSV 200
    PHPEVDAYEG ASESSLERPE ESISNEIENV IEEATKPAGE QIAEFSIHLL 250
    GKQYREELQD SSSFHHQHLE EEFISEVENA FTGLPGYKEI RVLEFRSPKE 300
    NDSGVDVYYA VTFNGEAISN TTWDLISLHS NKVENHGLVE LDDKPTVVYT 350
    ISNFRDYIAE TLQQNFLLGN SSLNPDPDSL QLINVRGVLR HQTEDLVWNT 400
    QSSSLQATPS SILDNTFQAA WPSADESITS SIPPLDFSSG PPSATGRELW 450
    SESPLGDLVS THKLAFPSKM GLSSSPEVLE VSSLTLHSVT PAVLQTGLPV 500
    ASEERTSGSH LVEDGLANVE ESEDFLSIDS LPSSSFTQPV PKETIPSMED 550
    SDVSLTSSPY LTSSIPFGLD SLTSKVKDQL KVSPFLPDAS MEKELIFDGG 600
    LGSGSGQKVD LITWPWSETS SEKSAEPLSK PWLEDDDSLL PAEIEDKKLV 650
    LVDKMDSTDQ ISKHSKYEHD DRSTHFPEEE PLSGPAVPIF ADTAAESASL 700
    TLPKHISEVP GVDDYSVTKA PLILTSVAIS ASTDKSDQAD AILREDMEQI 750
    TESSNYEWFD SEVSMVKPDM QTLWTILPES ERVWTRTSSL EKLSRDILAS 800
    TPQSADRLWL SVTQSTKLPP TTISTLLEDE VIMGVQDISL ELDRIGTDYY 850
    QPEQVQEQNG KVGSYVEMST SVHSTEMVSV AWPTEGGDDL SYTQTSGALV 900
    VFFSLRVTNM MFSEDLFNKN SLEYKALEQR FLELLVPYLQ SNLTGFQNLE 950
    ILNFRNGSIV VNSRMKFANS VPPNVNNAVY MILEDFCTTA YNTMNLAIDK 1000
    YSLDVESGDE ANPCKFQACN EFSECLVNPW SGEAKCRCFP GYLSVEERPC 1050
    QSLCDLQPDF CLNDGKCDIM PGHGAICRCR VGENWWYRGK HCEEFVSEPV 1100
    IIGITIASVV GLLVIFSAII YFFIRTLQAH HDRSERESPF SGSSRQPDSL 1150
    SSIENAVKYN PVYESHRAGC EKYEGPYPQH PFYSSASGDV IGGLSREEIR 1200
    QMYESSELSR EEIQERMRVL ELYANDPEFA AFVREQQVEE V 1241
    Length:1,241
    Mass (Da):138,621
    Last modified:May 18, 2010 - v3
    Checksum:iE72D7BFB84824078
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51P → L in AAF13154. (PubMed:10702256)Curated
    Sequence conflicti77 – 771I → T in AAF13154. (PubMed:10702256)Curated
    Sequence conflicti668 – 6681E → V in AAF13154. (PubMed:10702256)Curated
    Sequence conflicti715 – 7151Y → C in AAF06999. (PubMed:10542133)Curated
    Sequence conflicti1012 – 10121N → T in AAG49889. (PubMed:10542133)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti124 – 1241F → L in MACLP-IMPG2. 1 Publication
    VAR_064336
    Natural varianti344 – 3441K → N.
    Corresponds to variant rs34375459 [ dbSNP | Ensembl ].
    VAR_039144
    Natural varianti674 – 6741T → I.3 Publications
    Corresponds to variant rs571391 [ dbSNP | Ensembl ].
    VAR_039145
    Natural varianti1013 – 10131P → L.1 Publication
    Corresponds to variant rs116450347 [ dbSNP | Ensembl ].
    VAR_039146

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF173155 mRNA. Translation: AAF06999.1.
    AF271379
    , AF271363, AF271364, AF271365, AF271366, AF271367, AF271368, AF271369, AF271370, AF271371, AF271372, AF271373, AF271374, AF271375, AF271376, AF271377, AF271378 Genomic DNA. Translation: AAG49889.1.
    AF157624 mRNA. Translation: AAF13154.1.
    AC068764 Genomic DNA. No translation available.
    CCDSiCCDS2940.1.
    RefSeqiNP_057331.2. NM_016247.3.
    UniGeneiHs.209249.

    Genome annotation databases

    EnsembliENST00000193391; ENSP00000193391; ENSG00000081148.
    GeneIDi50939.
    KEGGihsa:50939.
    UCSCiuc003duq.2. human.

    Polymorphism databases

    DMDMi296439325.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF173155 mRNA. Translation: AAF06999.1 .
    AF271379
    , AF271363 , AF271364 , AF271365 , AF271366 , AF271367 , AF271368 , AF271369 , AF271370 , AF271371 , AF271372 , AF271373 , AF271374 , AF271375 , AF271376 , AF271377 , AF271378 Genomic DNA. Translation: AAG49889.1 .
    AF157624 mRNA. Translation: AAF13154.1 .
    AC068764 Genomic DNA. No translation available.
    CCDSi CCDS2940.1.
    RefSeqi NP_057331.2. NM_016247.3.
    UniGenei Hs.209249.

    3D structure databases

    ProteinModelPortali Q9BZV3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000193391.

    PTM databases

    PhosphoSitei Q9BZV3.

    Polymorphism databases

    DMDMi 296439325.

    Proteomic databases

    PaxDbi Q9BZV3.
    PRIDEi Q9BZV3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000193391 ; ENSP00000193391 ; ENSG00000081148 .
    GeneIDi 50939.
    KEGGi hsa:50939.
    UCSCi uc003duq.2. human.

    Organism-specific databases

    CTDi 50939.
    GeneCardsi GC03M100944.
    GeneReviewsi IMPG2.
    H-InvDB HIX0030730.
    HGNCi HGNC:18362. IMPG2.
    MIMi 607056. gene.
    613581. phenotype.
    neXtProti NX_Q9BZV3.
    Orphaneti 791. Retinitis pigmentosa.
    PharmGKBi PA29866.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG17485.
    HOGENOMi HOG000113064.
    HOVERGENi HBG108006.
    InParanoidi Q9BZV3.
    OMAi WPWSETS.
    OrthoDBi EOG7TXKFR.
    PhylomeDBi Q9BZV3.
    TreeFami TF331340.

    Miscellaneous databases

    GenomeRNAii 50939.
    NextBioi 53387.
    PROi Q9BZV3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BZV3.
    Bgeei Q9BZV3.
    CleanExi HS_IMPG2.
    Genevestigatori Q9BZV3.

    Family and domain databases

    Gene3Di 3.30.70.960. 2 hits.
    InterProi IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR000082. SEA_dom.
    [Graphical view ]
    Pfami PF01390. SEA. 2 hits.
    [Graphical view ]
    SMARTi SM00200. SEA. 2 hits.
    [Graphical view ]
    SUPFAMi SSF82671. SSF82671. 2 hits.
    PROSITEi PS01186. EGF_2. 1 hit.
    PS50026. EGF_3. 2 hits.
    PS50024. SEA. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular characterization and genomic mapping of human IPM 200, a second member of a novel family of proteoglycans."
      Kuehn M.H., Hageman G.S.
      Mol. Cell Biol. Res. Commun. 2:103-110(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, VARIANT ILE-674.
    2. "SPACRCAN, a novel human interphotoreceptor matrix hyaluronan-binding proteoglycan synthesized by photoreceptors and pinealocytes."
      Acharya S., Foletta V.C., Lee J.W., Rayborn M.E., Rodriguez I.R., Young W.S. III, Hollyfield J.G.
      J. Biol. Chem. 275:6945-6955(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 82-86; 123-127 AND 582-593, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, FUNCTION, GLYCOSYLATION, VARIANT ILE-674.
    3. "The DNA sequence, annotation and analysis of human chromosome 3."
      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.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Organization of the human IMPG2 gene and its evaluation as a candidate gene in age-related macular degeneration and other retinal degenerative disorders."
      Kuehn M.H., Stone E.M., Hageman G.S.
      Invest. Ophthalmol. Vis. Sci. 42:3123-3129(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ILE-674 AND LEU-1013.
    5. Cited for: VARIANT MACLP-IMPG2 LEU-124, INVOLVEMENT IN RP56.

    Entry informationi

    Entry nameiIMPG2_HUMAN
    AccessioniPrimary (citable) accession number: Q9BZV3
    Secondary accession number(s): A8MWT5, Q9UKD4, Q9UKK5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 85 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3