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adenyl cyclase-1 (ADCY1, Ca+2/calmodulin-activated adenyl cyclase)
Function:
- calmodulin-sensitive adenylyl cyclase
- may be involved in regulatory processes in the central nervous system
- may play a role in memory acquisition & learning
- activated by Ca+2/calmodulin
- Gs-alpha[GTP] is only mildly stimulatory [2]
- inhibited by G-beta/gamma
ATP 3',5'-cyclic AMP + diphosphate
Cofactor: binds 2 Mg+2 per subunit (putative)
Structure:
- belongs to the adenylyl cyclase class-4/guanylyl cyclase family
- contains 2 guanylate cyclase domains
Compartment: membrane
Expression:
- brain, retina & adrenal medulla
- richest sources are the dentate gyrus & hippocampus
General
adenyl cyclase, adenylyl cyclase or adenylate cyclase
glycoprotein
Properties
SIZE: entity length = 1119 aa
MW = 123 kD
COMPARTMENT: plasma membrane*
CELL: most cell types*
ORGANISM: eukaryote*
MOTIF: cytoplasmic domain {1-63}
transmembrane domain {64-84}
exoplasmic loop {85-87}
transmembrane domain {88-108}
cytoplasmic loop {109-124}
transmembrane domain {125-145}
exoplasmic loop {146-157}
transmembrane domain {158-178}
cytoplasmic loop {179-182}
transmembrane domain {183-203}
exoplasmic loop {204-213}
transmembrane domain {214-234}
cytoplasmic loop {235-610}
MOTIF: Mg+2-binding site
SITE: 308-308
Mg+2-binding site
SITE: 309-309
Mg+2-binding site
SITE: 352-352
calmodulin interaction {493-520}
transmembrane domain {611-631}
exoplasmic loop {632-634}
transmembrane domain {635-655}
cytoplasmic loop {656-673}
transmembrane domain {674-694}
exoplasmic loop {695-724}
MOTIF: N-glycosylation site {N704}
transmembrane domain {725-745}
cytoplasmic loop {746-752}
transmembrane domain {753-773}
exoplasmic loop {774-774}
transmembrane domain {775-794}
cytoplasmic domain {795-1119}
MOTIF: calmodulin interaction {1024-1047}
STATE: Inactive
Database Correlations
OMIM 103072
UniProt Q08828
Pfam PF00211
Entrez Gene 107
Kegg hsa:107
ENZYME 4.6.1.1
References
- Bakalyar & Reed Science 250:1403 1990
- Cooper et al
Adenylyl cyclases and the interaction between calcium and
cAMP signalling.
Nature 374:421 1995
PMID: 7700350
- UniProt :accession Q08828