A0A0A0MSC1 · A0A0A0MSC1_HUMAN
- ProteinAdenylate cyclase type 3
- GeneADCY3
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1145 (go to sequence)
- Protein existenceEvidence at protein 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 | 324 | Mg2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 324 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 324-329 | ATP (UniProtKB | ChEBI) | ||||
Sequence: DIVGFT | ||||||
Binding site | 325 | Mg2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: I | ||||||
Binding site | 366-368 | ATP (UniProtKB | ChEBI) | ||||
Sequence: LGD | ||||||
Binding site | 368 | Mg2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 368 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 412 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 976 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 1063-1065 | ATP (UniProtKB | ChEBI) | ||||
Sequence: DIW | ||||||
Binding site | 1070-1074 | ATP (UniProtKB | ChEBI) | ||||
Sequence: NVASR | ||||||
Binding site | 1110 | 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 | 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 type 3
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA0A0A0MSC1
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 | 78-100 | Helical | ||||
Sequence: LLVLVVFAALFDCYVVVMCAVVF | ||||||
Transmembrane | 106-126 | Helical | ||||
Sequence: ASLAVAGIGLVLDIILFVLCK | ||||||
Transmembrane | 138-157 | Helical | ||||
Sequence: VLPYVLWLLITAQIFSYLGL | ||||||
Transmembrane | 169-185 | Helical | ||||
Sequence: VGWQVFFVFSFFITLPL | ||||||
Transmembrane | 190-210 | Helical | ||||
Sequence: IVIISVVSCVVHTLVLGVTVA | ||||||
Transmembrane | 230-247 | Helical | ||||
Sequence: VFLYLCAIAVGIMSYYMA | ||||||
Transmembrane | 633-653 | Helical | ||||
Sequence: GAAFSCSCVVLLCTALVEILI | ||||||
Transmembrane | 665-687 | Helical | ||||
Sequence: MVGEILLLILTICSLAAIFPRAF | ||||||
Transmembrane | 708-733 | Helical | ||||
Sequence: WAMLAIFILVMANVVDMLSCLQYYTG | ||||||
Transmembrane | 753-770 | Helical | ||||
Sequence: YYNYVAVLSLIATIMLVQ | ||||||
Transmembrane | 777-795 | Helical | ||||
Sequence: LTLMLLVAGAVATINLYAW | ||||||
Transmembrane | 841-858 | Helical | ||||
Sequence: YSMTVMVFLMMLSFYYFS |
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,057 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue (large scale data) | 524 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 525 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 580 | PRIDE | Phosphoserine | ||||
Sequence: S |
Proteomic databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 319-446 | Guanylate cyclase | ||||
Sequence: SILFADIVGFTQLSSACSAQELVKLLNELFARFDKLAAKYHQLRIKILGDCYYCICGLPDYREDHAVCSILMGLAMVEAISYVREKTKTGVDMRVGVHTGTVLGGVLGQKRWQYDVWSTDVTVANKME | ||||||
Compositional bias | 504-544 | Polar residues | ||||
Sequence: TQNGLNGSALPNGAPASSKSSSPALIETKEPNGSAHSSGST | ||||||
Region | 504-566 | Disordered | ||||
Sequence: TQNGLNGSALPNGAPASSKSSSPALIETKEPNGSAHSSGSTSEKPEEQDAQADNPSFPNPRRR | ||||||
Domain | 924-1076 | Guanylate cyclase | ||||
Sequence: GVMFASLPNFADFYTEESINNGGIECLRFLNEIISDFDSLLDNPKFRVITKIKTIGSTYMAASGVTPDVNTNGFASSNKEDKSERERWQHLADLADFALAMKDTLTNINNQSFNNFMLRIGMNKGGVLAGVIGARKPHYDIWGNTVNVASRME |
Sequence similarities
Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,145
- Mass (Da)129,047
- Last updated2015-01-07 v1
- ChecksumB0B4EDD6F20AE7F6
Computationally mapped potential isoform sequences
There are 7 potential isoforms mapped to this entry
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 504-544 | Polar residues | ||||
Sequence: TQNGLNGSALPNGAPASSKSSSPALIETKEPNGSAHSSGST |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC012073 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |