A0A2I2UT70 · A0A2I2UT70_FELCA
- ProteinPhosphodiesterase
- GenePDE1B
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids535 (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 | 222 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 222-226 | AMP (UniProtKB | ChEBI) | ||||
Sequence: HNQIH | ||||||
Binding site | 226 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 262 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 263 | AMP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 263 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 263 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 369 | AMP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 369 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 420 | 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 | cAMP-mediated signaling | |
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 | visual learning |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphodiesterase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Carnivora > Feliformia > Felidae > Felinae > Felis
Accessions
- Primary accessionA0A2I2UT70
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Expression
Gene expression databases
Interaction
Structure
Family & Domains
Features
Showing features for region, coiled coil, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-21 | Disordered | ||||
Sequence: MELSPRSPPEMLESDCPSPLE | ||||||
Coiled coil | 38-90 | |||||
Sequence: LRYMVKQLENGEVNIEELKKNLEYTASLLEAVYIDETRQILDTEDELQELRSD | ||||||
Domain | 145-502 | PDEase | ||||
Sequence: VGPTYSTVVLNCLKNLDLWCFDVFSLNRAADDHALRTIVFELLTRHNLISRFKIPTVFLMTFLDALETGYGKYKNPYHNQIHAADVTQTVHCFLLRTGMVHCLSEIEVLAIVFAAAIHDYEHTGTTNSFHIQTKSECAILYNDRSVLENHHISSVFRMMQDDEMNIFINLTKDEFVELRALVIEMVLATDMSCHFQQVKCMKTALQQLERIDKSKALSLLLHAADISHPTKQWSVHSRWTKALMEEFFRQGDKEAELGLPFSPLCDRTSTLVAQSQIGFIDFIVEPTFSVLTDVAEKSVQPLVDDDSKSKNQPSFQWRQPSLDVEVGDPNPDVVSFRSTWTKYIQENKQKWKERAASG | ||||||
Region | 445-474 | Disordered | ||||
Sequence: PLVDDDSKSKNQPSFQWRQPSLDVEVGDPN | ||||||
Compositional bias | 449-463 | Polar residues | ||||
Sequence: DDSKSKNQPSFQWRQ | ||||||
Region | 495-535 | Disordered | ||||
Sequence: WKERAASGITNQMSIDELSPCEEDTLPSPAEDEHNQNGNLD | ||||||
Compositional bias | 498-512 | Polar residues | ||||
Sequence: RAASGITNQMSIDEL |
Sequence similarities
Belongs to the cyclic nucleotide phosphodiesterase family. PDE1 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length535
- Mass (Da)61,332
- Last updated2018-02-28 v1
- ChecksumD15445B84F4B952A
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
M3WCT1 | M3WCT1_FELCA | PDE1B | 516 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 449-463 | Polar residues | ||||
Sequence: DDSKSKNQPSFQWRQ | ||||||
Compositional bias | 498-512 | Polar residues | ||||
Sequence: RAASGITNQMSIDEL |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AANG04001751 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |