Detail Information for IndEnz0002018818
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;