Q9BZV3 · IMPG2_HUMAN

  • Protein
    Interphotoreceptor matrix proteoglycan 2
  • Gene
    IMPG2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

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.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcell projection
Cellular Componentextracellular matrix
Cellular Componentextracellular region
Cellular Componentinterphotoreceptor matrix
Cellular Componentmembrane
Cellular Componentreceptor complex
Molecular Functionextracellular matrix structural constituent
Molecular Functionheparin binding
Molecular Functionhyaluronic acid binding
Biological Processextracellular matrix organization
Biological Processprotein localization
Biological Processretina morphogenesis in camera-type eye
Biological Processvisual perception

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Interphotoreceptor matrix proteoglycan 2
  • Alternative names
    • Interphotoreceptor matrix proteoglycan of 200 kDa (IPM 200)
    • Sialoprotein associated with cones and rods proteoglycan (Spacrcan)

Gene names

    • Name
      IMPG2
    • Synonyms
      IPM200

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q9BZV3
  • Secondary accessions
    • A8MWT5
    • Q9UKD4
    • Q9UKK5

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain23-1099Extracellular
Transmembrane1100-1120Helical
Topological domain1121-1241Cytoplasmic

Keywords

Disease & Variants

Involvement in disease

Retinitis pigmentosa 56 (RP56)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    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.
  • See also
    MIM:613581
Natural variants in RP56
Variant IDPosition(s)ChangeDescription
VAR_082176127-1241missingin RP56
VAR_082177171-1241missingin RP56
VAR_082178212-1241missingin RP56
VAR_082181296-302missingin RP56
VAR_082184560-1241missingin RP56
VAR_082186906-1241missingin RP56
VAR_082187964-1241missingin RP56
VAR_0821911088-1241missingin RP56

Macular dystrophy, vitelliform, 5 (VMD5)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    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.
  • See also
    MIM:616152
Natural variants in VMD5
Variant IDPosition(s)ChangeDescription
VAR_064336124F>Lin VMD5; dbSNP:rs201893545
VAR_082179226-1241missingin VMD5
VAR_082183522-1241missingin VMD5
VAR_082185856-1241missingin VMD5
VAR_0726711077C>Fin VMD5; dbSNP:rs713993049

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_064336124in VMD5; dbSNP:rs201893545
Natural variantVAR_082176127-1241in RP56
Natural variantVAR_082177171-1241in RP56
Natural variantVAR_082178212-1241in RP56
Natural variantVAR_082179226-1241in VMD5
Natural variantVAR_082180243found in a patient with vitelliform macular dystrophy; uncertain significance; dbSNP:rs1706811719
Natural variantVAR_082181296-302in RP56
Natural variantVAR_039144344in dbSNP:rs34375459
Natural variantVAR_082182379found in a patient with retinitis pigmentosa; uncertain significance
Natural variantVAR_082183522-1241in VMD5
Natural variantVAR_082184560-1241in RP56
Natural variantVAR_039145674in dbSNP:rs571391
Natural variantVAR_082185856-1241in VMD5
Natural variantVAR_082186906-1241in RP56
Natural variantVAR_082187964-1241in RP56
Natural variantVAR_0821881008found in a patient with vitelliform macular dystrophy; uncertain significance
Natural variantVAR_0391461013in dbSNP:rs116450347
Natural variantVAR_0821891016found in a patient with VMD5; uncertain significance
Natural variantVAR_0821901042found in a patient with vitelliform macular dystophy; uncertain significance; dbSNP:rs990633116
Natural variantVAR_0726711077in VMD5; dbSNP:rs713993049
Natural variantVAR_0821911088-1241in RP56

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 1,584 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for signal, chain, glycosylation, disulfide bond.

TypeIDPosition(s)Description
Signal1-22
ChainPRO_000032014923-1241Interphotoreceptor matrix proteoglycan 2
Glycosylation154N-linked (GlcNAc...) asparagine
Glycosylation190O-linked (GalNAc...) threonine
Glycosylation192O-linked (GalNAc...) threonine
Glycosylation301N-linked (GlcNAc...) asparagine
Glycosylation320N-linked (GlcNAc...) asparagine
Glycosylation370N-linked (GlcNAc...) asparagine
Glycosylation544O-linked (GalNAc...) threonine
Glycosylation556O-linked (GalNAc...) threonine
Glycosylation942N-linked (GlcNAc...) asparagine
Glycosylation956N-linked (GlcNAc...) asparagine
Disulfide bond1014↔1025
Disulfide bond1019↔1036
Disulfide bond1038↔1050
Disulfide bond1054↔1067
Disulfide bond1061↔1077
Disulfide bond1079↔1092

Post-translational modification

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

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in the retina (at protein level) (PubMed:10702256, PubMed:29777959).
Expressed by photoreceptors of the interphotoreceptor matrix (IPM) surrounding both rods and cones (at protein level) (PubMed:10542133, PubMed:29777959).
IPM occupies the subretinal space between the apices of the retinal pigment epithelium and the neural retina (PubMed:10542133).
Expressed in the pineal gland (at protein level) (PubMed:10702256).

Developmental stage

Expressed in the retina 17 weeks post-conception (at protein level) (PubMed:29777959).
Expressed in the outer neuroblastic zone and retinal pigment epithelium (at protein level) (PubMed:29777959).

Gene expression databases

Organism-specific databases

Interaction

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias180-198Polar residues
Region180-223Disordered
Domain239-353SEA 1
Region259-267Hyaluronan-binding motif involved in chondroitin sulfate A-binding
Compositional bias660-678Basic and acidic residues
Region660-684Disordered
Domain897-1010SEA 2
Domain1010-1051EGF-like 1
Domain1052-1093EGF-like 2
Region1080-1088Hyaluronan-binding motif involved in chondroitin sulfate C-binding
Region1125-1133Hyaluronan-binding motif involved in chondroitin sulfate A- and C-binding
Region1136-1145Hyaluronan-binding motif involved in chondroitin sulfate C-binding
Region1210-1218Hyaluronan-binding motif involved in chondroitin sulfate A- and C-binding motif

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    1,241
  • Mass (Da)
    138,621
  • Last updated
    2010-05-18 v3
  • Checksum
    E72D7BFB84824078
MIMFPLFGKISLGILIFVLIEGDFPSLTAQTYLSIEEIQEPKSAVSFLLPEESTDLSLATKKKQPLDRRETERQWLIRRRRSILFPNGVKICPDESVAEAVANHVKYFKVRVCQEAVWEAFRTFWDRLPGREEYHYWMNLCEDGVTSIFEMGTNFSESVEHRSLIMKKLTYAKETVSSSELSSPVPVGDTSTLGDTTLSVPHPEVDAYEGASESSLERPEESISNEIENVIEEATKPAGEQIAEFSIHLLGKQYREELQDSSSFHHQHLEEEFISEVENAFTGLPGYKEIRVLEFRSPKENDSGVDVYYAVTFNGEAISNTTWDLISLHSNKVENHGLVELDDKPTVVYTISNFRDYIAETLQQNFLLGNSSLNPDPDSLQLINVRGVLRHQTEDLVWNTQSSSLQATPSSILDNTFQAAWPSADESITSSIPPLDFSSGPPSATGRELWSESPLGDLVSTHKLAFPSKMGLSSSPEVLEVSSLTLHSVTPAVLQTGLPVASEERTSGSHLVEDGLANVEESEDFLSIDSLPSSSFTQPVPKETIPSMEDSDVSLTSSPYLTSSIPFGLDSLTSKVKDQLKVSPFLPDASMEKELIFDGGLGSGSGQKVDLITWPWSETSSEKSAEPLSKPWLEDDDSLLPAEIEDKKLVLVDKMDSTDQISKHSKYEHDDRSTHFPEEEPLSGPAVPIFADTAAESASLTLPKHISEVPGVDDYSVTKAPLILTSVAISASTDKSDQADAILREDMEQITESSNYEWFDSEVSMVKPDMQTLWTILPESERVWTRTSSLEKLSRDILASTPQSADRLWLSVTQSTKLPPTTISTLLEDEVIMGVQDISLELDRIGTDYYQPEQVQEQNGKVGSYVEMSTSVHSTEMVSVAWPTEGGDDLSYTQTSGALVVFFSLRVTNMMFSEDLFNKNSLEYKALEQRFLELLVPYLQSNLTGFQNLEILNFRNGSIVVNSRMKFANSVPPNVNNAVYMILEDFCTTAYNTMNLAIDKYSLDVESGDEANPCKFQACNEFSECLVNPWSGEAKCRCFPGYLSVEERPCQSLCDLQPDFCLNDGKCDIMPGHGAICRCRVGENWWYRGKHCEEFVSEPVIIGITIASVVGLLVIFSAIIYFFIRTLQAHHDRSERESPFSGSSRQPDSLSSIENAVKYNPVYESHRAGCEKYEGPYPQHPFYSSASGDVIGGLSREEIRQMYESSELSREEIQERMRVLELYANDPEFAAFVREQQVEEV

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict5in Ref. 2; AAF13154
Sequence conflict77in Ref. 2; AAF13154
Compositional bias180-198Polar residues
Compositional bias660-678Basic and acidic residues
Sequence conflict668in Ref. 2; AAF13154
Sequence conflict715in Ref. 1; AAF06999
Sequence conflict1012in Ref. 1; AAG49889

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF173155
EMBL· GenBank· DDBJ
AAF06999.1
EMBL· GenBank· DDBJ
mRNA
AF271379
EMBL· GenBank· DDBJ
AAG49889.1
EMBL· GenBank· DDBJ
Genomic DNA
AF271363
EMBL· GenBank· DDBJ
AAG49889.1
EMBL· GenBank· DDBJ
Genomic DNA
AF271364
EMBL· GenBank· DDBJ
AAG49889.1
EMBL· GenBank· DDBJ
Genomic DNA
AF271365
EMBL· GenBank· DDBJ
AAG49889.1
EMBL· GenBank· DDBJ
Genomic DNA
AF271366
EMBL· GenBank· DDBJ
AAG49889.1
EMBL· GenBank· DDBJ
Genomic DNA
AF271367
EMBL· GenBank· DDBJ
AAG49889.1
EMBL· GenBank· DDBJ
Genomic DNA
AF271368
EMBL· GenBank· DDBJ
AAG49889.1
EMBL· GenBank· DDBJ
Genomic DNA
AF271369
EMBL· GenBank· DDBJ
AAG49889.1
EMBL· GenBank· DDBJ
Genomic DNA
AF271370
EMBL· GenBank· DDBJ
AAG49889.1
EMBL· GenBank· DDBJ
Genomic DNA
AF271371
EMBL· GenBank· DDBJ
AAG49889.1
EMBL· GenBank· DDBJ
Genomic DNA
AF271372
EMBL· GenBank· DDBJ
AAG49889.1
EMBL· GenBank· DDBJ
Genomic DNA
AF271373
EMBL· GenBank· DDBJ
AAG49889.1
EMBL· GenBank· DDBJ
Genomic DNA
AF271374
EMBL· GenBank· DDBJ
AAG49889.1
EMBL· GenBank· DDBJ
Genomic DNA
AF271375
EMBL· GenBank· DDBJ
AAG49889.1
EMBL· GenBank· DDBJ
Genomic DNA
AF271376
EMBL· GenBank· DDBJ
AAG49889.1
EMBL· GenBank· DDBJ
Genomic DNA
AF271377
EMBL· GenBank· DDBJ
AAG49889.1
EMBL· GenBank· DDBJ
Genomic DNA
AF271378
EMBL· GenBank· DDBJ
AAG49889.1
EMBL· GenBank· DDBJ
Genomic DNA
AF157624
EMBL· GenBank· DDBJ
AAF13154.1
EMBL· GenBank· DDBJ
mRNA
AC068764
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

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