| IED ID | IndEnz0002018818 |
| Enzyme Type ID | protease018818 |
| 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 | Rattus norvegicus (Rat) |
| 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 Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MQPEVPLGSGKLKPCSDMGDIQRAAKFRSSQSAHMLLLLLASITMLLCVRGAHGRPTEEDEELVLPSLERARGHDSTTLLRLDAFGQQLHLKLQPDSGFLAPGFTLQTVGRSPGSEAQHLDPTGDLAHCFYSGTVNGDPSSAAALSLCEGVRGAFYLQGEEFFIQPAPAVATERLVPAEPKEESIAPPRFHILRRRRRGSGGAKCGVMDEETLPTSNSGRESQNTPDQWPLRNPTPQGAGKPTGPGSIRKKRFVSSPRYVETMLVADQSMADFHGSGLKHYLLTLFSVAARFYKHPSIRNSISLVVVKILVIYEEQKGPEVTSNAALTLRNFCSWQKQHNSPSDRDPEHYDTAILFTRQDLCGSHTCDTLGMADVGTVCDPSRSCSVIEDDGLQAAFTTAHELGHVFNMPHDDAKHCASFNGVSGDSHLMASMLSSLDHSQPWSPCSAYMVTSFLDNGHGECLMDKPQNPIKLPSDLPGTLYDANRQCQFTFGEESTHCPDAASTCSTLWCTGTSGGLLVCQTKHFPWADGTSCGEGKWCVSGKCVNKTDMKHFATPVHGSWGPWGPWGDCSRTCGGGVQYTMRECDNPVPKNGGKYCEGKRVRYRSCNIEDCPDNNGKTFREEQCEAHNEFSKASFGNEPTVEWTPKYAGVSPKDRCKLTCEAKGIGYFFVLQPKVVDGTPCSPDSTSVCVQGQCVKAGCDRIIDSKKKFDKCGVCGGNGSTCKKISGTVTSTRPGYHDIVTIPAGATNIEVKHRNPRGSRNNGSFLAIRAADGTYILNGNFTLSTLEQDLTYKGTVLRYSGSSAALERIRSFSPLKEPLTIQVLMVGHALRPKIKYTYFMKKKTEPFNAIPTFSEWVIEEWGECSKTCGSGWQRRVVECRDINGHPASECAKEVKPASTRPCADLPCPRWQVGDWSPCSKTCGKGYKKRTLKCLSHDGGVLSNESCDPLKKPKHYIDFCILTQCS |
| Enzyme Length | 967 |
| Uniprot Accession Number | Q9WUQ1 |
| Absorption | |
| Active Site | ACT_SITE 402; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| 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 '1683-Glu-|-Leu-1684' 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}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Compositional bias (1); Disulfide bond (11); Domain (5); Glycosylation (5); Metal binding (12); Motif (1); Propeptide (1); Region (2); Sequence conflict (10); 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: Down-regulated in endothelial cells derived from cirrhotic liver. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.; 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..54; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10727282; 11108265; 11311987; 12379262; 15625312; 15777654; 16200461; 16630594; 17073862; 17583485; 18272597; 23025351; 23825416; |
| Motif | MOTIF 203..210; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 105,706 |
| Kinetics | |
| Metal Binding | METAL 205; /note=Zinc; in inhibited form; /evidence=ECO:0000250; METAL 261; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q9UHI8; METAL 261; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q9UHI8; METAL 344; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q9UHI8; METAL 344; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q9UHI8; METAL 351; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q9UHI8; METAL 401; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9UHI8; METAL 405; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9UHI8; METAL 411; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9UHI8; METAL 462; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q9UHI8; METAL 465; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q9UHI8; METAL 465; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q9UHI8 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.B11; |