UniProt functional annotation for P39900



	UniProt functional annotation for P39900

UniProt code: P39900.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3.

Catalytic activity: Reaction=Hydrolysis of soluble and insoluble elastin. Specific cleavages are also produced at 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in the B chain of insulin.; EC=3.4.24.65;

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.;

Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000305}.

Tissue specificity: Found in alveolar macrophages but not in peripheral blood monocytes.

Induction: By exposure to bacterial lipopolysaccharides (LPS). Inhibited by dexamethasone.

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.

Similarity: Belongs to the peptidase M10A family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3.


Catalytic activity:		Reaction=Hydrolysis of soluble and insoluble elastin. Specific cleavages are also produced at 14-Ala-\|-Leu-15 and 16-Tyr-\|-Leu-17 in the B chain of insulin.; EC=3.4.24.65;
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.;
Subcellular location:		Secreted, extracellular space, extracellular matrix {ECO:0000305}.
Tissue specificity:		Found in alveolar macrophages but not in peripheral blood monocytes.
Induction:		By exposure to bacterial lipopolysaccharides (LPS). Inhibited by dexamethasone.
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.
Similarity:		Belongs to the peptidase M10A family. {ECO:0000305}.