| IED ID | IndEnz0002002412 |
| Enzyme Type ID | protease002412 |
| Protein Name |
A disintegrin and metalloproteinase with thrombospondin motifs 15 ADAM-TS 15 ADAM-TS15 ADAMTS-15 EC 3.4.24.- |
| Gene Name | Adamts15 |
| 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 | MLLLGISILALAWRPAGSSEPEWEVVVPIRRDPDINGRHYYRRGTEDSGDQGLIFQITAFQQDFYLHLTPDAQFLAPAFATEYLGVPLQRLTGSSLDLRRCFYSGYVNAEPDSFAAVSLCGGLRGAFGYRGAEYVISPLPNTSAPEAQRHSQGAHLLQRRGAPVGPSGDPTSRCGVASGWNPAILRALDPYKPRRTGAGESHNRRRSGRAKRFVSIPRYVETLVVADESMVKFHGADLEHYLLTLLATAARLYRHPSILNPINIVVVKVLLLGDRDTGPKVTGNAALTLRNFCAWQKKLNKVSDKHPEYWDTAILFTRQDLCGATTCDTLGMADVGTMCDPKRSCSVIEDDGLPSAFTTAHELGHVFNMPHDNVKVCEEVFGKLRANHMMSPTLIQIDRANPWSACSAAIITDFLDSGHGDCLLDQPSKPITLPEDLPGTSYSLSQQCELAFGVGSKPCPYMQYCTKLWCTGKAKGQMVCQTRHFPWADGTSCGEGKFCLKGACVERHNPNKYRVDGSWAKWEPYGSCSRTCGGGVQLARRQCSNPTPANGGKYCEGVRVKYRSCNLEPCPSSASGKSFREEQCEAFNGYNHSTNRLTLAVAWVPKYSGVSPRDKCKLICRANGTGYFYVLAPKVVDGTLCTPDSTSVCVQGKCIKAGCDGNLGSKKKFDKCGVCGGDNKSCKRVTGLFTKPMHGYNFVVAIPAGASSIDIRQRGYKGLIGDDNYLALKNSQGKYLLNGHFVVSAVERDLVVKGSVLRYSGTGTAVESLQASRPILEPLTVEVLSVGKMTPPRVRYSFYLPKEPREDKSTRPKDPRGSPVLRNSVLSLSNQVEQPDNRPPARWVAGSWGPCSVSCGSGLQKRAVDCRDSPGQQGASACDVDHRPLEKRACGEPCPTWELGNWSPCSKSCGRGFKRRPLKCVGHGGRLLARDQCDLRRKPQELDFCVLRPC |
| Enzyme Length | 950 |
| Uniprot Accession Number | P59384 |
| Absorption | |
| Active Site | ACT_SITE 362; /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: Metalloprotease which has proteolytic activity against the proteoglycan VCAN, cleaving it at the 'Glu-1401-|-1402-Ala' site (PubMed:24220035). Cleaves VCAN in the pericellular matrix surrounding myoblasts, facilitating myoblast contact and fusion which is required for skeletal muscle development and regeneration (PubMed:23233679). {ECO:0000269|PubMed:23233679, ECO:0000269|PubMed:24220035}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Compositional bias (1); Disulfide bond (11); Domain (5); Glycosylation (4); Metal binding (4); Motif (1); Mutagenesis (2); Propeptide (1); Region (3); Sequence conflict (3); Signal peptide (1); Site (1) |
| Keywords | Cleavage on pair of basic residues;Disulfide bond;Extracellular matrix;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:24220035}. Cell surface {ECO:0000269|PubMed:24220035}. |
| Modified Residue | |
| Post Translational Modification | PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000269|PubMed:24220035}.; PTM: Glycosylated (PubMed:24220035). 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 (By similarity). Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL (By similarity). Fucosylation mediates the efficient secretion of ADAMTS family members (By similarity). Can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs (By similarity). Also N-glycosylated (PubMed:24220035). These other glycosylations can also facilitate secretion (By similarity). {ECO:0000250|UniProtKB:Q76LX8, ECO:0000269|PubMed:24220035}. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 18554416; 19922873; 20637190; 21267068; 24194600; 25349050; 25510509; 27626380; 29337306; 31434798; 32094117; |
| Motif | MOTIF 172..179; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 103,938 |
| Kinetics | |
| Metal Binding | METAL 174; /note=Zinc; in inhibited form; /evidence=ECO:0000250; METAL 361; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9UNA0; METAL 365; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9UNA0; METAL 371; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9UNA0 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.B12; |