Detail Information for IndEnz0002002414
IED ID IndEnz0002002414
Enzyme Type ID protease002414
Protein Name A disintegrin and metalloproteinase with thrombospondin motifs 5
ADAM-TS 5
ADAM-TS5
ADAMTS-5
EC 3.4.24.-
ADMP-2
Aggrecanase-2
Implantin
Gene Name Adamts5
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 MRLEWAPLLLLLLLLSASCLSLAADSPAAAPAQDKTRQPQAAAAAAEPDQPQGEETRERGHLQPLAGQRRSGGLVQNIDQLYSGGGKVGYLVYAGGRRFLLDLERDDTVGAAGSIVTAGGGLSASSGHRGHCFYRGTVDGSPRSLAVFDLCGGLDGFFAVKHARYTLKPLLRGSWAEYERIYGDGSSRILHVYNREGFSFEALPPRASCETPASPSGPQESPSVHSRSRRRSALAPQLLDHSAFSPSGNAGPQTWWRRRRRSISRARQVELLLVADSSMARMYGRGLQHYLLTLASIANRLYSHASIENHIRLAVVKVVVLTDKDTSLEVSKNAATTLKNFCKWQHQHNQLGDDHEEHYDAAILFTREDLCGHHSCDTLGMADVGTICSPERSCAVIEDDGLHAAFTVAHEIGHLLGLSHDDSKFCEENFGTTEDKRLMSSILTSIDASKPWSKCTSATITEFLDDGHGNCLLDLPRKQILGPEELPGQTYDATQQCNLTFGPEYSVCPGMDVCARLWCAVVRQGQMVCLTKKLPAVEGTPCGKGRVCLQGKCVDKTKKKYYSTSSHGNWGSWGPWGQCSRSCGGGVQFAYRHCNNPAPRNSGRYCTGKRAIYRSCSVTPCPPNGKSFRHEQCEAKNGYQSDAKGVKTFVEWVPKYAGVLPADVCKLTCRAKGTGYYVVFSPKVTDGTECRPYSNSVCVRGRCVRTGCDGIIGSKLQYDKCGVCGGDNSSCTKIIGTFNKKSKGYTDVVRIPEGATHIKVRQFKAKDQTRFTAYLALKKKTGEYLINGKYMISTSETIIDINGTVMNYSGWSHRDDFLHGMGYSATKEILIVQILATDPTKALDVRYSFFVPKKTTQKVNSVISHGSNKVGPHSTQLQWVTGPWLACSRTCDTGWHTRTVQCQDGNRKLAKGCLLSQRPSAFKQCLLKKC
Enzyme Length 930
Uniprot Accession Number Q9R001
Absorption
Active Site ACT_SITE 411; /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: Metalloproteinase that plays an important role in connective tissue organization, development, inflammation and cell migration. Extracellular matrix (ECM) degrading enzyme that shows proteolytic activity toward the hyalectan group of chondroitin sulfate proteoglycans (CSPGs) including ACAN, VCAN, BCAN and NCAN. 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 (PubMed:23233679). Participates in the development of brown adipose tissue and browning of white adipose tissue (PubMed:28702327). Plays an important role for T-lymphocyte migration from draining lymph nodes following viral infection (PubMed:27855162). {ECO:0000269|PubMed:15800625, ECO:0000269|PubMed:23233679, ECO:0000269|PubMed:27855162, ECO:0000269|PubMed:28702327}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Disulfide bond (11); Domain (4); Glycosylation (7); Metal binding (4); Motif (1); Propeptide (1); Region (3); Sequence conflict (4); Signal peptide (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:0000250|UniProtKB:Q9UNA0}.
Modified Residue
Post Translational Modification PTM: The precursor is cleaved by furin and PCSK7 outside of the cell. {ECO:0000250|UniProtKB:Q9UNA0}.; 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..21; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10438522; 11217851; 11831030; 12466851; 12466854; 12466855; 14681479; 15659705; 15800624; 16141072; 16452166; 16537572; 17243865; 17255106; 17938173; 17968948; 18267097; 18799682; 19250981; 19334288; 19386638; 19565481; 19684582; 19922873; 20036347; 20466812; 20495570; 20637190; 21041365; 21148564; 21337391; 21539915; 21566131; 21749862; 21800360; 21828051; 21928430; 22183742; 22493487; 22824241; 23082219; 23154421; 23354118; 23436205; 23531444; 23684986; 23754494; 23843306; 23963448; 23982761; 24006456; 24220035; 24427155; 24753090; 25101296; 25349050; 25615642; 25733872; 25770910; 25840345; 26100917; 26657033; 26668318; 27254774; 27732085; 28570296; 29030347; 29293679; 29337306; 29567669; 29622560; 29688375; 29720262; 29743679; 29791855; 30579834; 30958594; 31366218; 31434798; 31608494; 31676809; 32156081; 32648916; 32909945; 33561540; 33934089; 34806902;
Motif MOTIF 207..214; /note=Cysteine switch; /evidence=ECO:0000250
Gene Encoded By
Mass 101,844
Kinetics
Metal Binding METAL 209; /note=Zinc; in inhibited form; /evidence=ECO:0000250; METAL 410; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9UNA0; METAL 414; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9UNA0; METAL 420; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9UNA0
Rhea ID
Cross Reference Brenda 3.4.24.B12;