| UniProt functional annotation for P22288 | |||
| UniProt code: P22288. |
| Organism: | Rattus norvegicus (Rat). | |
| Taxonomy: | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus. | |
| Function: | May positively regulate nitric oxide synthesis in endothelial cells. May be involved in dopamine synthesis (By similarity). May modify pain sensitivity and persistence. {ECO:0000250|UniProtKB:P30793, ECO:0000269|PubMed:17057711}. | |
| Catalytic activity: | Reaction=GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+); Xref=Rhea:RHEA:17473, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:37565, ChEBI:CHEBI:58462; EC=3.5.4.16; Evidence={ECO:0000269|PubMed:2557335}; | |
| Activity regulation: | GTP shows a positive allosteric effect, and tetrahydrobiopterin inhibits the enzyme activity. Zinc is required for catalytic activity. Inhibited by Mg(2+). {ECO:0000269|PubMed:2557335}. | |
| Biophysicochemical properties: | Kinetic parameters: Vmax=2.7 umol/h/mg enzyme (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:2557335}; | |
| Pathway: | Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1. {ECO:0000305|PubMed:2557335}. | |
| Subunit: | Toroid-shaped homodecamer, composed of two pentamers of five dimers. Interacts with AHSA1 and GCHFR/GFRP. {ECO:0000269|PubMed:11818540}. | |
| Subcellular location: | Cytoplasm {ECO:0000250|UniProtKB:P30793}. Nucleus {ECO:0000250|UniProtKB:P30793}. | |
| Induction: | By cytokines such as insulin, interferon-gamma, and phytohemagglutinin in adrenal gland, macrophages, and T-cell respectively. | |
| Ptm: | Phosphorylated. {ECO:0000250|UniProtKB:P30793}. | |
| Similarity: | Belongs to the GTP cyclohydrolase I family. {ECO:0000305}. | |
Annotations taken from UniProtKB at the EBI.