| IED ID | IndEnz0002015681 |
| Enzyme Type ID | protease015681 |
| Protein Name |
Cartilage oligomeric matrix protein COMP Thrombospondin-5 TSP5 |
| Gene Name | COMP |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MVPDTACVLLLTLAALGASGQGQSPLGSDLGPQMLRELQETNAALQDVRELLRQQVREITFLKNTVMECDACGMQQSVRTGLPSVRPLLHCAPGFCFPGVACIQTESGARCGPCPAGFTGNGSHCTDVNECNAHPCFPRVRCINTSPGFRCEACPPGYSGPTHQGVGLAFAKANKQVCTDINECETGQHNCVPNSVCINTRGSFQCGPCQPGFVGDQASGCQRRAQRFCPDGSPSECHEHADCVLERDGSRSCVCAVGWAGNGILCGRDTDLDGFPDEKLRCPERQCRKDNCVTVPNSGQEDVDRDGIGDACDPDADGDGVPNEKDNCPLVRNPDQRNTDEDKWGDACDNCRSQKNDDQKDTDQDGRGDACDDDIDGDRIRNQADNCPRVPNSDQKDSDGDGIGDACDNCPQKSNPDQADVDHDFVGDACDSDQDQDGDGHQDSRDNCPTVPNSAQEDSDHDGQGDACDDDDDNDGVPDSRDNCRLVPNPGQEDADRDGVGDVCQDDFDADKVVDKIDVCPENAEVTLTDFRAFQTVVLDPEGDAQIDPNWVVLNQGREIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTVTDDDYAGFIFGYQDSSSFYVVMWKQMEQTYWQANPFRAVAEPGIQLKAVKSSTGPGEQLRNALWHTGDTESQVRLLWKDPRNVGWKDKKSYRWFLQHRPQVGYIRVRFYEGPELVADSNVVLDTTMRGGRLGVFCFSQENIIWANLRYRCNDTIPEDYETHQLRQA |
| Enzyme Length | 757 |
| Uniprot Accession Number | P49747 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme 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 (PubMed:16542502, PubMed:16051604). Could play a role in the pathogenesis of osteoarthritis (PubMed:16542502). 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) (PubMed:17993464). 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|UniProtKB:P35444, ECO:0000269|PubMed:16051604, ECO:0000269|PubMed:16542502, ECO:0000269|PubMed:17993464}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (1); Beta strand (34); Chain (1); Compositional bias (4); Disulfide bond (23); Domain (5); Erroneous gene model prediction (1); Glycosylation (2); Helix (12); Motif (1); Natural variant (81); Region (3); Repeat (8); Sequence conflict (3); Signal peptide (1); Turn (6) |
| Keywords | 3D-structure;Alternative splicing;Apoptosis;Calcium;Cell adhesion;Direct protein sequencing;Disease variant;Disulfide bond;Dwarfism;EGF-like domain;Extracellular matrix;Glycoprotein;Heparin-binding;Reference proteome;Repeat;Secreted;Signal |
| Interact With | P58397; P29972; O00244; A8MQ03; Q6FHY5; Q7Z417; P32242; Q96EQ0; P13608 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:32686688}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 3FBY; |
| Mapped Pubmed ID | 11501943; 11782471; 11891674; 12768438; 12792737; 12819015; 15266613; 15345499; 15472220; 15523498; 15694129; 15749701; 15880723; 16214313; 16340129; 16520029; 16802351; 17033713; 17195216; 17570134; 17579668; 17894003; 18193163; 18485748; 18855621; 19035482; 19125286; 19447929; 19605679; 19762713; 19877068; 19913121; 20033473; 20544356; 20628086; 20819661; 21029365; 21042783; 21221577; 21599986; 21616158; 21644213; 21834907; 21843649; 21872564; 21965141; 22068351; 22163547; 22241609; 22253028; 22264230; 22521401; 22573329; 22660798; 22764748; 23133613; 23507196; 23528838; 23562786; 23875975; 23915292; 23959964; 24187101; 24229584; 24330664; 24376648; 24595329; 24907621; 24917676; 25111190; 25380520; 25416956; 25430711; 25835418; 26269256; 26634947; 26848781; 27065333; 27217240; 27251407; 27385219; 27432013; 27455560; 27699484; 27930497; 28319091; 28685811; 28849199; 28889184; 28924040; 28951969; 29104872; 29164307; 29351749; 29369406; 29560517; 30100245; 30213581; 30217750; 30231922; 30464261; 30502262; 30502484; 30720083; 30995524; 30999932; 31177591; 31495329; 31665048; 31696983; 31944379; 32057837; 32497304; 32754278; 33068727; 33438071; 33472398; 33595934; 33748277; 33910854; 34117950; 34404836; 34680093; 8943283; 9685393; 9749943; |
| Motif | MOTIF 367..369; /note=Cell attachment site; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 82,860 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |