Member database | Pfam |
Pfam type | family |
Short name | Adcy_cons_dom |
Clan | Nucleot_cyclase |
Author | Yeats C;0000-0003-0080-6242 |
Sequence Ontology | 0100021 |
Description
Adenylate cyclase (AC) enzyme uses ATP as its substrate to produce Cyclic AMP (cAMP), a ubiquitous signalling molecule that mediates many cellular processes by activating cAMP- dependent kinases and also inducing protein-protein interactions. Mammalian adenylate cyclase has nine closely related membrane-bound isoforms (AC1-9) showing significant sequence homology and sharing the same overall structure: two hydrophobic transmembrane domains, and two cytoplasmic domains that are responsible for the catalytic activity. These isoforms differ in both their tissue specificity and their regulation
[3, 2]. This entry represents a region of unknown function found in many of these isoforms. It is part of the N-terminal cytoplasmic domain but its presence is not necessary for catalytic activity
[1].
References
1.Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha.GTPgammaS. Tesmer JJ, Sunahara RK, Gilman AG, Sprang SR. Science 278, 1907-16, (1997). View articlePMID: 9417641
2.Regulation and organization of adenylyl cyclases and cAMP. Cooper DM. Biochem. J. 375, 517-29, (2003). View articlePMID: 12940771
3.Regulation and role of adenylyl cyclase isoforms. Hanoune J, Defer N. Annu. Rev. Pharmacol. Toxicol. 41, 145-74, (2001). View articlePMID: 11264454