ID:ATS12_HUMAN DESCRIPTION: RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 12; Short=ADAM-TS 12; Short=ADAM-TS12; Short=ADAMTS-12; EC=3.4.24.-; Flags: Precursor; FUNCTION: Metalloprotease that may play a role in the degradation of COMP. Cleaves also alpha-2 macroglobulin and aggregan. Has anti-tumorigenic properties. COFACTOR: Binds 1 zinc ion per subunit (By similarity). ENZYME REGULATION: Inhibited by alpha-2 macroglobulin. BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 7.5 and 9.5 with COMP for substrate; SUBUNIT: Interacts with COMP. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix (By similarity). TISSUE SPECIFICITY: Expressed in skeletal muscle and fat. Detected at significant levels in fetal lung. Widely expressed in gastric carcinomas and in cancer cells of diverse origin. INDUCTION: By IFN-alpha and by IL1B/interleukin-1 beta. Up- regulated in articular cartilage and synovium from arthritis patients. Up-regulared in chondrocytes. DOMAIN: The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix (By similarity). DOMAIN: The C-terminal four TSP1-like repeats are necessary and sufficient for binding COMP. DOMAIN: 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. PTM: The precursor is cleaved by a furin endopeptidase. PTM: Subjected to an intracellular maturation process yielding a 120 kDa N-terminal fragment containing the metalloproteinase, disintegrin, one TSP type-1 and the Cys-rich domains and a 83 kDa C-terminal fragment containing the spacer 2 and four TSP type-1 domains. SIMILARITY: Contains 1 disintegrin domain. SIMILARITY: Contains 1 peptidase M12B domain. SIMILARITY: Contains 1 PLAC domain. SIMILARITY: Contains 8 TSP type-1 domains.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P58397
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
US Server
Sequence and Links to Tools and Databases 
Common Gene Haplotype Alleles 
