A0A4X2KN33 · A0A4X2KN33_VOMUR
- ProteinPhosphodiesterase
- GenePDE1B
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- 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 | 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 | 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
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Metatheria > Diprotodontia > Vombatidae > Vombatus
Accessions
- Primary accessionA0A4X2KN33
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Keywords
- PTM
Interaction
Structure
Family & Domains
Features
Showing features for coiled coil, domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 38-90 | |||||
Sequence: LRYMVKQLENGEVNIEELKKNLEYTASLLEAVYIDETRQILDTEDELQELRSD | ||||||
Domain | 145-504 | PDEase | ||||
Sequence: VGPTYSNAVINCLKTLDHWCFDVFALNRVADDHALRTIVFELLTRHNLISRFKLPTVFLMTFLDALEVGYGKYKNPYHNQIHAADVTQTVHCFLLRTGMVHCLSEIEVLAIIFAAAIHDYEHTGTTNSFHIQTKSECAILYNDRSVLENHHISSVFRMMQDDEMNIFINLTKDEFVELRSLVIEMVLATDMSCHFQQVKSMKTSLQQLERIDKSKALSLLLHAADISHPTKQWSVHSRWTKALMEEFFRQGDKEAELGLPFSPLCDRTSTLVAQSQIGFIDFIVEPTFSVLTDVAEKSVQPLVDEGSKAKTKPSSQWYQPSLDGSREPGDLNPDLVSFRTTWTKYIQENKQKWKERAASG | ||||||
Region | 447-477 | Disordered | ||||
Sequence: VDEGSKAKTKPSSQWYQPSLDGSREPGDLNP | ||||||
Region | 497-536 | Disordered | ||||
Sequence: WKERAASGITNQTSIDELSPCEEEAPSSPAEELNQNGNLD | ||||||
Compositional bias | 500-514 | Polar residues | ||||
Sequence: RAASGITNQTSIDEL |
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)61,240
- Last updated2019-09-18 v1
- Checksum33F07A76FEB10507
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A4X2KG02 | A0A4X2KG02_VOMUR | PDE1B | 517 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 500-514 | Polar residues | ||||
Sequence: RAASGITNQTSIDEL |
Keywords
- Technical term