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UniProt functional annotation for P21692 | ||
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| UniProt code: P21692. |
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| Organism: | |
Sus scrofa (Pig). |
| Taxonomy: | |
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. |
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| Function: | |
Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. |
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| Catalytic activity: | |
Reaction=Cleavage of the triple helix of collagen at about three- quarters of the length of the molecule from the N-terminus, at 775- Gly-|-Ile-776 in the alpha-1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue.; EC=3.4.24.7; |
| Cofactor: | |
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 4 Ca(2+) ions per subunit.; |
| Cofactor: | |
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; |
| Activity regulation: | |
Can be activated without removal of the activation peptide. |
| Subcellular location: | |
Secreted, extracellular space, extracellular matrix {ECO:0000250}. |
| 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: | |
Undergoes autolytic cleavage to produce a N-terminal fragment having reduced collagenolytic activity. |
| Ptm: | |
Tyrosine phosphorylated in platelets by PKDCC/VLK. {ECO:0000250|UniProtKB:P03956}. |
| Similarity: | |
Belongs to the peptidase M10A family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.