A0A0D9QZB3 · A0A0D9QZB3_CHLSB
- ProteinPhosphodiesterase
- GenePDE1B
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids536 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Cyclic nucleotide phosphodiesterase with a dual specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Has a preference for cGMP as a substrate.
Catalytic activity
- 3',5'-cyclic AMP + H2O = AMP + H+This reaction proceeds in the forward direction.
- 3',5'-cyclic GMP + H2O = GMP + H+This reaction proceeds in the forward direction.
Cofactor
Protein has several cofactor binding sites:
Note: Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 223 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 223-227 | AMP (UniProtKB | ChEBI) | ||||
Sequence: HNQIH | ||||||
Binding site | 227 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 263 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 264 | AMP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 264 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 264 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 370 | AMP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 370 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 421 | AMP (UniProtKB | ChEBI) | ||||
Sequence: Q |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | neuronal cell body | |
Molecular Function | calmodulin-activated 3',5'-cyclic-GMP phosphodiesterase activity | |
Molecular Function | calmodulin-activated dual specificity 3',5'-cyclic-GMP, 3',5'-cyclic-AMP phosphodiesterase activity | |
Molecular Function | metal ion binding | |
Biological Process | cellular response to granulocyte macrophage colony-stimulating factor stimulus | |
Biological Process | cellular response to macrophage colony-stimulating factor stimulus | |
Biological Process | dopamine catabolic process | |
Biological Process | locomotory behavior | |
Biological Process | monocyte differentiation | |
Biological Process | response to amphetamine | |
Biological Process | serotonin metabolic process | |
Biological Process | signal transduction | |
Biological Process | visual learning |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphodiesterase
- EC number
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Cercopithecidae > Cercopithecinae > Chlorocebus
Accessions
- Primary accessionA0A0D9QZB3
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Keywords
- PTM
Expression
Gene expression databases
Interaction
Structure
Family & Domains
Features
Showing features for region, coiled coil, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-20 | Disordered | ||||
Sequence: MELSPRSPPEMLEESDCPSP | ||||||
Coiled coil | 39-91 | |||||
Sequence: LRYMVKQLENGEVNIEELKKNLEYTASLLEAVYIDETRQILDTEDELQELRSD | ||||||
Domain | 146-503 | PDEase | ||||
Sequence: VGPTYSTAVLNCFKNLDLWCFDVFSLNRAADDHALRTIVFELLTRHNLISRFKIPTVFLMSFLDALETGYGKYKNPYHNQIHAADVTQTVHCFLLRTGMVHCLSEIEVLAIIFAAAIHDYEHTGTTNSFHIQTKSECAILYNDRSVLENHHISSVFRLMQDDELNIFINLTKDEFVELRALVIEMVLATDMSCHFQQVKTMKTALQQLERIDKPKALSLLLHAADISHPTKQWSVHSRWTKALMEEFFRQGDKEAELGLPFSPLCDRTSTLVAQSQIGFIDFIVEPTFSVLTDVAEKSVQPLADEDSKSKNQPSFQWRQPSLDVEVGDPNPDVVSFRSTWIKHIQENKQKWKERAASG | ||||||
Region | 447-473 | Disordered | ||||
Sequence: LADEDSKSKNQPSFQWRQPSLDVEVGD | ||||||
Compositional bias | 450-464 | Polar residues | ||||
Sequence: EDSKSKNQPSFQWRQ | ||||||
Region | 494-536 | Disordered | ||||
Sequence: QKWKERAASGITNQMSIDELSPCDEEAPPSPAEDEHNQNGNLD |
Sequence similarities
Belongs to the cyclic nucleotide phosphodiesterase family. PDE1 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length536
- Mass (Da)61,365
- Last updated2015-05-27 v1
- Checksum5B0F82829574B9C6
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 450-464 | Polar residues | ||||
Sequence: EDSKSKNQPSFQWRQ |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AQIB01022982 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |