D1MIA2 · D1MIA2_DANRE
- Proteinadenylate cyclase
- Geneadcy1a
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1114 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling.
Catalytic activity
- ATP = 3',5'-cyclic AMP + diphosphate
Cofactor
Protein has several cofactor binding sites:
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 301 | Mg2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 301 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 301-306 | ATP (UniProtKB | ChEBI) | ||||
Sequence: DIVGFT | ||||||
Binding site | 302 | Mg2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: I | ||||||
Binding site | 343-345 | ATP (UniProtKB | ChEBI) | ||||
Sequence: LGD | ||||||
Binding site | 345 | Mg2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 345 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 389 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 913 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 990-992 | ATP (UniProtKB | ChEBI) | ||||
Sequence: DIW | ||||||
Binding site | 997-1001 | ATP (UniProtKB | ChEBI) | ||||
Sequence: NVASR | ||||||
Binding site | 1036 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | adenylate cyclase activity | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Biological Process | adenylate cyclase-activating G protein-coupled receptor signaling pathway | |
Biological Process | cAMP biosynthetic process | |
Biological Process | intracellular signal transduction |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameadenylate cyclase
- EC number
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio
Accessions
- Primary accessionD1MIA2
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 52-74 | Helical | ||||
Sequence: ATLKALAILILAASALALVELLS | ||||||
Transmembrane | 86-104 | Helical | ||||
Sequence: HPVHCVIFTSLFIVTNVKY | ||||||
Transmembrane | 116-135 | Helical | ||||
Sequence: LALLFSFTFALLCCPFPLAL | ||||||
Transmembrane | 155-170 | Helical | ||||
Sequence: GVWQLMLVTFVAYSLL | ||||||
Transmembrane | 177-197 | Helical | ||||
Sequence: AVLFGVLVAASHFIVTATSVT | ||||||
Transmembrane | 203-224 | Helical | ||||
Sequence: VWTPLVANAVLLVGVNLSGVFV | ||||||
Transmembrane | 601-623 | Helical | ||||
Sequence: AFISAVVISLVLTSFFAVVYFLI | ||||||
Transmembrane | 629-650 | Helical | ||||
Sequence: LVVILLVLCLCFHMASVMYLHV | ||||||
Transmembrane | 671-692 | Helical | ||||
Sequence: FLVLLMYSVTQGCVVTCVPWSL | ||||||
Transmembrane | 718-738 | Helical | ||||
Sequence: YTPYVFLSCVMASLSVALYLR | ||||||
Transmembrane | 745-764 | Helical | ||||
Sequence: ILLLLLLNILHTVVMETSGY |
Keywords
- Cellular component
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 296-423 | Guanylate cyclase | ||||
Sequence: SILFADIVGFTSLASQCTAQELVKLLNELFGKFDELATENHCRRIKILGDCYYCVSGLTQPKADHAHCCVEMGLDMIDTITSVAEATEVDLNMRVGLHTGRVLCGVLGLRKWQYDVWSNDVTLANMME | ||||||
Domain | 861-1003 | Guanylate cyclase | ||||
Sequence: GVLFASIPNFNDFYIELDGNNMGVECLRLLNEIIADFDALMDKECYRDIEKIKTIGSTYMAAVGLVPTEGSKVKKSISAHLCTVADYAIEMFDVLDAINYQSYNDFVLRVGINVGPVVAGVIGARRPQYDIWGNTVNVASRMD |
Sequence similarities
Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,114
- Mass (Da)124,626
- Last updated2010-01-19 v1
- Checksum2539D429A23FC0C8
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
GU169394 EMBL· GenBank· DDBJ | ACZ48694.1 EMBL· GenBank· DDBJ | mRNA |