UniProt functional annotation for Q05769

UniProt code: Q05769.

Organism: Mus musculus (Mouse).
Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus; Mus.
Function: Mediates the formation of prostaglandins from arachidonate. May have a role as a major mediator of inflammation and/or a role for prostanoid signaling in activity-dependent plasticity. Critical component of colonic mucosal wound repair.
Catalytic activity: Arachidonate + AH(2) + 2 O(2) = prostaglandin H(2) + A + H(2)O.
Cofactor: Binds 1 heme B (iron-protoporphyrin IX) group per subunit.
Enzyme regulation: Inhibited by the nonsteroidal anti-inflammatory drugs aspirin, naproxen, diclofenac, meclofenamic acid, indomethacin and their analogs.
Pathway: Lipid metabolism; prostaglandin biosynthesis.
Subunit: Homodimer.
Subcellular location: Microsome membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein.
Tissue specificity: Following colon injury, expressed in the wound bed mesenchyme during the first phase of repair, probably by colonic mesenchymal stem cells (at protein level).
Developmental stage: During colonic wound repair, highly up- regulated (more than 1600-fold) in the mesenchyme of the wound bed 2 days after injury as compared to uninjured mucosa. Further increase in expression is observed at day 4 following injury (close to 2200-fold). Down-regulated at day 6 (only 93-fold increase as compared to uninjured mucosa).
Induction: By cytokines and mitogens.
Ptm: S-nitrosylation by NOS2 (iNOS) activates enzyme activity. S- nitrosylation may take place on different Cys residues in addition to Cys-526 (By similarity).
Disruption phenotype: Mutant mice exhibit defects in colonic mucosal wound repair.
Miscellaneous: Acts both as a dioxygenase and as a peroxidase.
Miscellaneous: Target of nonsteroidal anti-inflammatory drugs, such as aspirin.
Similarity: Belongs to the prostaglandin G/H synthase family.
Similarity: Contains 1 EGF-like domain.

Annotations taken from UniProtKB at the EBI.