NP_777056.1
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NCBI GenBank Nucleotide #
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UniProt Primary Accession #
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UniProt Related Accession #
NCBI Official Full Name
A disintegrin and metalloproteinase with thrombospondin motifs 2
NCBI Official Synonym Full Names
ADAM metallopeptidase with thrombospondin type 1 motif, 2<
NCBI Protein Information
A disintegrin and metalloproteinase with thrombospondin motifs 2; pNPI; PC I-NP; ADAM-TS2; ADAMTS-2; ADAM-TS 2; procollagen I N-proteinase; procollagen N-endopeptidase; procollagen I/II amino propeptide-processing enzyme; a disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 2
UniProt Protein Name
A disintegrin and metalloproteinase with thrombospondin motifs 2
UniProt Synonym Protein Names
Procollagen I N-proteinase; PC I-NP; Procollagen I/II amino propeptide-processing enzyme; Procollagen N-endopeptidase
UniProt Synonym Gene Names
UniProt Entry Name
ATS2_BOVIN
UniProt Comments for ADAMTS2
Function: Cleaves the propeptides of type I and II collagen prior to fibril assembly. Does not act on type III collagen. May also play a role in development that is independent of its role in collagen biosynthesis.
Catalytic activity: Cleaves the N-propeptide of collagen chain alpha-1(I) at Pro-|-Gln and of alpha-1(II) and alpha-2(I) at Ala-|-Gln.
Cofactor: Binds 1 zinc ion per subunit
By similarity.
Subunit structure: May belong to a multimeric complex. Binds specifically to collagen type XIV.
Subcellular location: Secreted › extracellular space › extracellular matrix
By similarity.
Tissue specificity: Enzymatic activity is detected at high level in all type I collagen-rich tissues such as skin, bones, tendons and aorta and at low level in brain and thymus. The mRNA levels were disproportionately high in heart, liver, retina and muscle.
Domain: The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.
Post-translational modification: The N-terminus is blocked.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.
Involvement in disease: Defects in ADAMTS2 are the cause of dermatosparaxis, a recessively inherited disorder characterized by severe skin fragility and biochemically by the presence in skin of procollagen incompletely processed at the N-terminus.
Sequence similarities: Contains 1 disintegrin domain.Contains 1 peptidase M12B domain.Contains 1 PLAC domain.Contains 4 TSP type-1 domains.
Caution: Has sometimes been referred to as ADAMTS3.
Research Articles on ADAMTS2
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Pathways associated with ADAMTS2 recombinant protein
Diseases associated with ADAMTS2 recombinant protein
Organs/Tissues associated with ADAMTS2 recombinant protein
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