Comp
entrez
25304
canonical
uniprot
P35444
canonical
ensembl
ENSRNOG00000048472
resolver
ensp
ENSRNOP00000067037
resolver
enst
ENSRNOT00000072536
resolver
genesymbol
Comp
resolver
uniprot
M0RBU0
resolver
uniprot_entry
COMP_RAT
resolver
uniprot_entry
M0RBU0_RAT
resolver
amino_acid_sequence
MSPTACVLVLALAALRATGQGQIPLGGDLAPQMLRELQETNAALQDVRELLRHRVKEITFLKNTVMECDACGMQPARTPGLSVRPVALCAPGSCFPGVVCTETATGARCGPCPPGYTGNGSHCTDVNECNAHPCFPRVRCINTSPGFHCEACPPGFSGPTHEGVGLTFAKTNKQVCTDINECETGQHNCVPNSVCVNTRGSFQCGPCQPGFVGDQRSGCQRRGQHFCPDGSPSPCHEKADCILERDGSRSCVCAVGWAGNGLLCGRDTDLDGFPDEKLRCSERQCRKDNCVTVPNSGQEDVDRDRIGDACDPDADGDGVPNEQDNCPLVRNPDQRNSDKDKWGDACDNCRSQKNDDQKDTDRDGQGDACDDDIDGDRIRNVADNCPRVPNFDQSDSDGDGVGDACDNCPQKDNPDQRDVDHDFVGDACDSDQDQDGDGHQDSRDNCPTVPNSAQQDSDHDGKGDACDDDDDNDGVPDSRDNCRLVPNPGQEDNDRDGVGDACQGDFDADKVIDKIDVCPENAEVTLTDFRAFQTVVLDPEGDAQIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTATDDDYAGFIFGYQDSSSFYVVMWKQMEQTYWQANPFRAVAEPGIQLKAVKSSTGPGEQLRNALWHTGDTASQVRLLWKDPRNVGWKDKTSYRWFLQHRPQVGYIRVRFYEGPELVADSNVVLDTAMRGGRLGVFCFSQENIIWANLRYRCNDTIPEDYERHRLRRA
uniprot
proteins
function
FUNCTION: Plays 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) (By similarity). 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 (PubMed:20019333). {ECO:0000250|UniProtKB:P49747, ECO:0000269|PubMed:20019333}.
uniprot
proteins
mass_dalton
82664
uniprot
proteins
post_translational_modification
PTM: Proteolytically cleaved by metalloproteases ADAMTS4 and ADAMTS1 with ADAMTS4 showing more potent activity. {ECO:0000250|UniProtKB:P49747}.
uniprot
proteins
protein_family
Thrombospondin family
uniprot
proteins
pubmed
1429587
uniprot
proteins
pubmed
20019333
uniprot
proteins
pubmed
8864111
uniprot
proteins
sequence_length
755
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P49747}.
uniprot
proteins