Adenylate cyclase type 1
Domain
The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain.
Function
Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. Mediates responses to increased cellular Ca(2+)/calmodulin levels (By similarity). May be involved in regulatory processes in the central nervous system. May play a role in memory and learning. Plays a role in the regulation of the circadian rhythm of daytime contrast sensitivity probably by modulating the rhythmic synthesis of cyclic AMP in the retina (By similarity).
Involvement in disease
Deafness, autosomal recessive, 44
DFNB44
A form of non-syndromic deafness characterized by prelingual profound hearing loss affecting all frequencies.
None
The disease is caused by variants affecting the gene represented in this entry.
Post-translational modifications
N-glycosylated.
Sequence Similarities
Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.
Tissue Specificity
Detected in zona glomerulosa and zona fasciculata in the adrenal gland (at protein level) (PubMed:11549699). Brain, retina and adrenal medulla.
Cellular localization
- Membrane
- Multi-pass membrane protein
- Cell membrane
- Multi-pass membrane protein
- Cytoplasm
- Membrane raft
- Expressed in the cytoplasm of supporting cells and hair cells of the cochlea vestibule, as well as to the cochlear hair cell nuclei and stereocilia.
Alternative names
Adenylate cyclase type 1, ATP pyrophosphate-lyase 1, Adenylate cyclase type I, Adenylyl cyclase 1, Ca(2+)/calmodulin-activated adenylyl cyclase, ADCY1