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UniProt functional annotation for Q02153 | ||
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| UniProt code: Q02153. |
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| Organism: | |
Homo sapiens (Human). |
| Taxonomy: | |
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. |
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| Function: | |
Mediates responses to nitric oxide (NO) by catalyzing the biosynthesis of the signaling molecule cGMP. {ECO:0000250|UniProtKB:P16068, ECO:0000269|PubMed:1352257}. |
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| Catalytic activity: | |
Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2; Evidence={ECO:0000269|PubMed:1352257}; |
| Cofactor: | |
Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P16068}; Note=Binds 1 or 2 heme groups per heterodimer. Heme is required for responding to nitric oxide, but not for catalytic activity. {ECO:0000250|UniProtKB:P16068}; |
| Activity regulation: | |
Activated by nitric oxide in the presence of magnesium or manganese ions. {ECO:0000269|PubMed:1352257}. |
| Subunit: | |
The active enzyme is formed by a heterodimer of an alpha and a beta subunit. Heterodimer with GUCY1A1 (PubMed:1352257, PubMed:23505436, PubMed:24669844). Can also form inactive homodimers in vitro (PubMed:23505436, PubMed:24669844). {ECO:0000269|PubMed:23505436, ECO:0000269|PubMed:24669844}. |
| Subcellular location: | |
Cytoplasm {ECO:0000250|UniProtKB:P16068}. |
| Tissue specificity: | |
Detected in brain cortex and cerebellum (at protein level). {ECO:0000269|PubMed:1352257}. |
| Miscellaneous: | |
There are two types of guanylate cyclases: soluble forms and membrane-associated receptor forms. |
| Similarity: | |
Belongs to the adenylyl cyclase class-4/guanylyl cyclase family. {ECO:0000255|PROSITE-ProRule:PRU00099}. |
Annotations taken from UniProtKB at the EBI.