| IED ID | IndEnz0002013706 |
| Enzyme Type ID | protease013706 |
| Protein Name |
A disintegrin and metalloproteinase with thrombospondin motifs 1 ADAM-TS 1 ADAM-TS1 ADAMTS-1 EC 3.4.24.- |
| Gene Name | Adamts1 |
| Organism | Mus musculus (Mouse) |
| 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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MQPKVPLGSRKQKPCSDMGDVQRAARSRGSLSAHMLLLLLASITMLLCARGAHGRPTEEDEELVLPSLERAPGHDSTTTRLRLDAFGQQLHLKLQPDSGFLAPGFTLQTVGRSPGSEAQHLDPTGDLAHCFYSGTVNGDPGSAAALSLCEGVRGAFYLQGEEFFIQPAPGVATERLAPAVPEEESSARPQFHILRRRRRGSGGAKCGVMDDETLPTSDSRPESQNTRNQWPVRDPTPQDAGKPSGPGSIRKKRFVSSPRYVETMLVADQSMADFHGSGLKHYLLTLFSVAARFYKHPSIRNSISLVVVKILVIYEEQKGPEVTSNAALTLRNFCSWQKQHNSPSDRDPEHYDTAILFTRQDLCGSHTCDTLGMADVGTVCDPSRSCSVIEDDGLQAAFTTAHELGHVFNMPHDDAKHCASLNGVSGDSHLMASMLSSLDHSQPWSPCSAYMVTSFLDNGHGECLMDKPQNPIKLPSDLPGTLYDANRQCQFTFGEESKHCPDAASTCTTLWCTGTSGGLLVCQTKHFPWADGTSCGEGKWCVSGKCVNKTDMKHFATPVHGSWGPWGPWGDCSRTCGGGVQYTMRECDNPVPKNGGKYCEGKRVRYRSCNIEDCPDNNGKTFREEQCEAHNEFSKASFGNEPTVEWTPKYAGVSPKDRCKLTCEAKGIGYFFVLQPKVVDGTPCSPDSTSVCVQGQCVKAGCDRIIDSKKKFDKCGVCGGNGSTCKKMSGIVTSTRPGYHDIVTIPAGATNIEVKHRNQRGSRNNGSFLAIRAADGTYILNGNFTLSTLEQDLTYKGTVLRYSGSSAALERIRSFSPLKEPLTIQVLMVGHALRPKIKFTYFMKKKTESFNAIPTFSEWVIEEWGECSKTCGSGWQRRVVQCRDINGHPASECAKEVKPASTRPCADLPCPHWQVGDWSPCSKTCGKGYKKRTLKCVSHDGGVLSNESCDPLKKPKHYIDFCTLTQCS |
| Enzyme Length | 968 |
| Uniprot Accession Number | P97857 |
| Absorption | |
| Active Site | ACT_SITE 403; /evidence=ECO:0000269|PubMed:10373500 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Cleaves aggrecan, a cartilage proteoglycan, at the '1691-Glu-|-Leu-1692' site (within the chondroitin sulfate attachment domain), and may be involved in its turnover. Has angiogenic inhibitor activity (By similarity). Active metalloprotease, which may be associated with various inflammatory processes as well as development of cancer cachexia. May play a critical role in follicular rupture (By similarity). {ECO:0000250, ECO:0000269|PubMed:10781075, ECO:0000269|PubMed:10930576}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Compositional bias (1); Disulfide bond (11); Domain (5); Erroneous initiation (1); Frameshift (1); Glycosylation (5); Metal binding (12); Motif (1); Mutagenesis (1); Propeptide (1); Region (3); Sequence conflict (6); Signal peptide (1) |
| Keywords | Calcium;Cleavage on pair of basic residues;Disulfide bond;Extracellular matrix;Glycoprotein;Heparin-binding;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | INDUCTION: Induced in vitro in colon adenocarcinoma cells by interleukin-1, or in vivo in kidney and heart by lipopolysaccharide. Also induced by LH stimulation in granulosa cells of preovulatory follicles. {ECO:0000269|PubMed:10781075}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. |
| Modified Residue | |
| Post Translational Modification | PTM: The precursor is cleaved by a furin endopeptidase.; PTM: Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity). {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..48; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10438512; 10464288; 10811839; 10811842; 10847486; 11831030; 11970905; 12049787; 12466854; 12466855; 12907688; 14668204; 14681479; 15194513; 15256533; 15615810; 15659705; 15843381; 15880348; 15907280; 16061471; 16141072; 16216914; 16537572; 16691565; 17082774; 17097630; 18267097; 18322241; 18353623; 18554416; 19608765; 19922873; 20101710; 20103648; 20592310; 20598569; 20637190; 20665671; 20795945; 21148564; 21267068; 21411713; 21584905; 21826695; 21862448; 22001177; 22002813; 22183742; 22383695; 22913326; 23071766; 23095891; 23261447; 23354118; 23444028; 23562508; 23843306; 24498290; 24990151; 25615642; 25633245; 25770910; 26208718; 26217013; 26563155; 27120788; 27143554; 27447109; 28067899; 28302382; 28569793; 28939843; 29337306; 29567669; 29743679; 29791855; 29891551; 30166561; 30579834; 31434798; 31974739; 32648916; 32909945; 34175316; 9593739; |
| Motif | MOTIF 204..211; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 105,801 |
| Kinetics | |
| Metal Binding | METAL 206; /note=Zinc; in inhibited form; /evidence=ECO:0000250; METAL 262; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q9UHI8; METAL 262; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q9UHI8; METAL 345; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q9UHI8; METAL 345; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q9UHI8; METAL 352; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q9UHI8; METAL 402; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9UHI8; METAL 406; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9UHI8; METAL 412; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9UHI8; METAL 463; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q9UHI8; METAL 466; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q9UHI8; METAL 466; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q9UHI8 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.B11; |