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MGP000643

UniProt Annotations

Entry Information
Gene Namecartilage oligomeric matrix protein
Protein EntryCOMP_HUMAN
UniProt IDP49747
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=2; Name=1; IsoId=P49747-1; Sequence=Displayed; Name=2; IsoId=P49747-2; Sequence=VSP_055758; Note=No experimental confirmation available.;
CofactorName=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 11-14 calcium ions per subunit.;
Developmental StagePresent during the earliest stages of limb maturation and is later found in regions where the joints develop. {ECO:0000269|PubMed:16542502}.
DiseaseMultiple epiphyseal dysplasia 1 (EDM1) [MIM:132400]: A generalized skeletal dysplasia associated with significant morbidity. Joint pain, joint deformity, waddling gait, and short stature are the main clinical signs and symptoms. Radiological examination of the skeleton shows delayed, irregular mineralization of the epiphyseal ossification centers and of the centers of the carpal and tarsal bones. Multiple epiphyseal dysplasia is broadly categorized into the more severe Fairbank and the milder Ribbing types. The Fairbank type is characterized by shortness of stature, short and stubby fingers, small epiphyses in several joints, including the knee, ankle, hand, and hip. The Ribbing type is confined predominantly to the hip joints and is characterized by hands that are normal and stature that is normal or near-normal. {ECO:0000269|PubMed:11565064, ECO:0000269|PubMed:21922596, ECO:0000269|PubMed:7670472, ECO:0000269|PubMed:9021009, ECO:0000269|PubMed:9184241, ECO:0000269|PubMed:9452026, ECO:0000269|PubMed:9463320, ECO:0000269|PubMed:9921895}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DiseasePseudoachondroplasia (PSACH) [MIM:177170]: A skeletal dysplasia usually manifesting in the second year of life and characterized by moderate to severe disproportionate short stature, deformity of the lower limbs, brachydactyly, ligamentous laxity, and degenerative joint disease. {ECO:0000269|PubMed:11746044, ECO:0000269|PubMed:11746045, ECO:0000269|PubMed:21922596, ECO:0000269|PubMed:7670471, ECO:0000269|PubMed:7670472, ECO:0000269|PubMed:9184241, ECO:0000269|PubMed:9452026, ECO:0000269|PubMed:9452063, ECO:0000269|PubMed:9463320}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DomainEach of the eight TSP type-3 repeats binds two calcium ions. The TSP C-terminal domain binds three calcium ions. {ECO:0000269|PubMed:17993464}.
DomainThe cell attachment motif mediates the attachment to chondrocytes. It mediates the induction of both the IAP family of survival proteins and the antiapoptotic response. {ECO:0000269|PubMed:17993464}.
DomainThe TSP C-terminal domain mediates interaction with FN1 and ACAN. {ECO:0000269|PubMed:17993464}.
FunctionMay play a role in the structural integrity of cartilage via its interaction with other extracellular matrix proteins such as the collagens and fibronectin. Can mediate the interaction of chondrocytes with the cartilage extracellular matrix through interaction with cell surface integrin receptors. Could play a role in the pathogenesis of osteoarthritis. Potent suppressor of apoptosis in both primary chondrocytes and transformed cells. Suppresses apoptosis by blocking the activation of caspase-3 and by inducing the IAP family of survival proteins (BIRC3, BIRC2, BIRC5 and XIAP). Essential for maintaining a vascular smooth muscle cells (VSMCs) contractile/differentiated phenotype under physiological and pathological stimuli. Maintains this phenotype of VSMCs by interacting with ITGA7 (By similarity). {ECO:0000250}.
InteractionP13608:ACAN (xeno); NbExp=2; IntAct=EBI-2531022, EBI-6259246; P58397:ADAMTS12; NbExp=3; IntAct=EBI-2531022, EBI-9028051;
Sequence CautionSequence=AAB86501.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
SimilarityBelongs to the thrombospondin family. {ECO:0000305}.
SimilarityContains 1 TSP C-terminal (TSPC) domain. {ECO:0000255|PROSITE-ProRule:PRU00635}.
SimilarityContains 4 EGF-like domains. {ECO:0000255|PROSITE- ProRule:PRU00076}.
SimilarityContains 8 TSP type-3 repeats. {ECO:0000255|PROSITE- ProRule:PRU00634}.
Subcellular LocationSecreted, extracellular space, extracellular matrix.
SubunitPentamer; disulfide-linked. Exists in a more compact conformation in the presence of calcium and shows a more extended conformation in the absence of calcium. Interacts with ITGB3, ITGA5 and FN1. Binding to FN1 requires the presence of divalent cations (Ca(2+), Mg(2+) or Mn(2+)). The greatest amount of binding is seen in the presence of Mn(2+). Interacts with MATN1, MATN3, MATN4 and ACAN. Binds heparin, heparan sulfate and chondroitin sulfate. EDTA dimishes significantly its binding to ACAN and abolishes its binding to MATN3, MATN4 and chondroitin sulfate. Interacts with collagen I, II and IX, and interaction with these collagens is dependent on the presence of zinc ions. Interacts with ADAMTS12. Interacts with ITGA7 (By similarity). {ECO:0000250}.
Tissue SpecificityAbundantly expressed in the chondrocyte extracellular matrix, and is also found in bone, tendon, ligament and synovium and blood vessels. Increased amounts are produced during late stages of osteoarthritis in the area adjacent to the main defect. {ECO:0000269|PubMed:16542502}.
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