Q9WUQ1.1
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UniProt Primary Accession #
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UniProt Secondary Accession #
UniProt Related Accession #
NCBI Official Full Name
A disintegrin and metalloproteinase with thrombospondin motifs 1
NCBI Official Synonym Full Names
ADAM metallopeptidase with thrombospondin type 1 motif, 1
NCBI Protein Information
A disintegrin and metalloproteinase with thrombospondin motifs 1; ADAM-TS1; ADAMTS-1; ADAM-TS 1; a disintegrin and metalloproteinase with thrombospondin motifs 1 (ADAMTS-1); a disintegrin-like and metallopeptidse (reprolysin type) with thrombospondin type 1 motif, 1; a disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 1; a disintegrin-like and metallopeptidase (reprolysin type) with thrombospondin type 1 motif, 1
UniProt Protein Name
A disintegrin and metalloproteinase with thrombospondin motifs 1
UniProt Synonym Gene Names
UniProt Entry Name
ATS1_RAT
NCBI Summary for ADAMTS1
disintegrin and metalloprotease that may be necessary for normal kidney morphology and function [RGD, Feb 2006]
UniProt Comments for ADAMTS1
Function: Cleaves aggrecan, a cartilage proteoglycan, 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.
Catalytic activity: Cleaves aggrecan at the 1683-Glu-|-Leu-1684 site, within the chondroitin sulfate attachment domain.
Cofactor: Binds 1 zinc ion per subunit
By similarity.
Subcellular location: Secreted › extracellular space › extracellular matrix
By similarity.
Induction: Down-regulated in endothelial cells derived from cirrhotic liver.
Domain: The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Post-translational modification: The precursor is cleaved by a furin endopeptidase
By similarity.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.
Sequence similarities: Contains 1 disintegrin domain.Contains 1 peptidase M12B domain.Contains 3 TSP type-1 domains.
Research Articles on ADAMTS1
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Pathways associated with ADAMTS1 recombinant protein
Organs/Tissues associated with ADAMTS1 recombinant protein
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