| IED ID | IndEnz0002005134 |
| Enzyme Type ID | protease005134 |
| Protein Name |
A disintegrin and metalloproteinase with thrombospondin motifs 5 ADAM-TS 5 ADAM-TS5 ADAMTS-5 EC 3.4.24.- A disintegrin and metalloproteinase with thrombospondin motifs 11 ADAM-TS 11 ADAMTS-11 ADMP-2 Aggrecanase-2 |
| Gene Name | ADAMTS5 ADAMTS11 ADMP2 |
| 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 | MLLGWASLLLCAFRLPLAAVGPAATPAQDKAGQPPTAAAAAQPRRRQGEEVQERAEPPGHPHPLAQRRRSKGLVQNIDQLYSGGGKVGYLVYAGGRRFLLDLERDGSVGIAGFVPAGGGTSAPWRHRSHCFYRGTVDGSPRSLAVFDLCGGLDGFFAVKHARYTLKPLLRGPWAEEEKGRVYGDGSARILHVYTREGFSFEALPPRASCETPASTPEAHEHAPAHSNPSGRAALASQLLDQSALSPAGGSGPQTWWRRRRRSISRARQVELLLVADASMARLYGRGLQHYLLTLASIANRLYSHASIENHIRLAVVKVVVLGDKDKSLEVSKNAATTLKNFCKWQHQHNQLGDDHEEHYDAAILFTREDLCGHHSCDTLGMADVGTICSPERSCAVIEDDGLHAAFTVAHEIGHLLGLSHDDSKFCEETFGSTEDKRLMSSILTSIDASKPWSKCTSATITEFLDDGHGNCLLDLPRKQILGPEELPGQTYDATQQCNLTFGPEYSVCPGMDVCARLWCAVVRQGQMVCLTKKLPAVEGTPCGKGRICLQGKCVDKTKKKYYSTSSHGNWGSWGSWGQCSRSCGGGVQFAYRHCNNPAPRNNGRYCTGKRAIYRSCSLMPCPPNGKSFRHEQCEAKNGYQSDAKGVKTFVEWVPKYAGVLPADVCKLTCRAKGTGYYVVFSPKVTDGTECRLYSNSVCVRGKCVRTGCDGIIGSKLQYDKCGVCGGDNSSCTKIVGTFNKKSKGYTDVVRIPEGATHIKVRQFKAKDQTRFTAYLALKKKNGEYLINGKYMISTSETIIDINGTVMNYSGWSHRDDFLHGMGYSATKEILIVQILATDPTKPLDVRYSFFVPKKSTPKVNSVTSHGSNKVGSHTSQPQWVTGPWLACSRTCDTGWHTRTVQCQDGNRKLAKGCPLSQRPSAFKQCLLKKC |
| Enzyme Length | 930 |
| Uniprot Accession Number | Q9UNA0 |
| Absorption | |
| Active Site | ACT_SITE 411; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:18042673" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Metalloproteinase that plays an important role in connective tissue organization, development, inflammation and cell migration. Extracellular matrix (ECM) degrading enzyme that show proteolytic activity toward the hyalectan group of chondroitin sulfate proteoglycans (CSPGs) including ACAN, VCAN, BCAN and NCAN (PubMed:16133547, PubMed:18992360). Cleavage within the hyalectans occurs at Glu-Xaa recognition motifs. Plays a role in embryonic development, including limb and cardiac morphogenesis, and skeletal muscle development through its VCAN remodeling properties. Cleaves VCAN in the pericellular matrix surrounding myoblasts, facilitating myoblast contact and fusion which is required for skeletal muscle development and regeneration (By similarity). Participates in development of brown adipose tissue and browning of white adipose tissue (By similarity). Plays an important role for T-lymphocyte migration from draining lymph nodes following viral infection. {ECO:0000250|UniProtKB:Q9R001, ECO:0000269|PubMed:16133547, ECO:0000269|PubMed:18992360}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (15); Chain (1); Compositional bias (1); Disulfide bond (11); Domain (4); Glycosylation (7); Helix (13); Metal binding (4); Motif (1); Mutagenesis (1); Natural variant (3); Propeptide (1); Region (3); Signal peptide (1); Site (1); Turn (3) |
| Keywords | 3D-structure;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 | P13608 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:18992360}. |
| Modified Residue | |
| Post Translational Modification | PTM: The precursor is cleaved by furin and PCSK7 outside of the cell. {ECO:0000269|PubMed:18992360}.; 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..16; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (7) |
| Cross Reference PDB | 2RJQ; 3B8Z; 3HY7; 3HY9; 3HYG; 3LJT; 6YJM; |
| Mapped Pubmed ID | 10986281; 11067851; 11801682; 11831030; 11956193; 12054629; 12392761; 12514189; 14715656; 15296936; 15599946; 16003758; 16464858; 16507336; 17067994; 17211519; 17265492; 17265493; 17430884; 17978660; 17991750; 18156631; 18240210; 18478108; 18671934; 18720094; 19586907; 19643179; 19684582; 19796186; 19834535; 20237151; 20494980; 20568084; 20711500; 21345877; 21370305; 21437951; 21828051; 22406378; 22493487; 22562232; 22588082; 22707719; 22735305; 22796434; 22961118; 23064555; 23082219; 23131589; 23154421; 23491141; 23859810; 23889335; 23963448; 24312401; 24415654; 24732836; 24786121; 25122765; 25477257; 25519309; 25544610; 25848214; 26303525; 26612259; 26668318; 26707794; 26738863; 26888488; 27067395; 27084377; 27159841; 27706574; 28081267; 28085114; 28099917; 28110479; 28341660; 28546218; 28583914; 28728848; 29137610; 29143120; 29162281; 29248417; 29622560; 29737873; 30016600; 30105548; 30369484; 30652828; 30730845; 31484722; 31526197; 31637891; 31734268; 31734379; 31929842; 32415504; 32700984; 32917786; 33128918; 33441904; 33444494; 33522433; 33719441; 33934089; 34140036; 34806902; |
| Motif | MOTIF 207..214; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 101,718 |
| Kinetics | |
| Metal Binding | METAL 209; /note=Zinc; in inhibited form; /evidence=ECO:0000250; METAL 410; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:18042673; METAL 414; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:18042673; METAL 420; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:18042673 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.B12; |