Q64395 · PDE1B_CRIGR
- ProteinDual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B
- GenePDE1B1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids535 (go to sequence)
- Protein existenceEvidence at transcript level
- 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
- a nucleoside 3',5'-cyclic phosphate + H2O = a nucleoside 5'-phosphate + H+This reaction proceeds in the forward direction.
- 3',5'-cyclic GMP + H2O = GMP + H+This reaction proceeds in the forward direction.
- 3',5'-cyclic AMP + H2O = AMP + 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.
Note: Binds 2 divalent metal cations per subunit. Site 2 has a preference for magnesium ions.
Activity regulation
Type I PDE are activated by the binding of calmodulin in the presence of Ca2+.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 222 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 226 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 262 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 263 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 263 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 369 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | neuronal cell body | |
Molecular Function | 3',5'-cyclic-AMP phosphodiesterase activity | |
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 | cyclic-nucleotide phosphodiesterase activity | |
Molecular Function | metal ion binding | |
Biological Process | signal transduction |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B
- EC number
- Short namesCam-PDE 1B
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Cricetidae > Cricetinae > Cricetulus
Accessions
- Primary accessionQ64395
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000198788 | 1-535 | Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B | |||
Sequence: MELSPRSPPEMLESDCPSPLELKSAPSKKMWIKLRSLLRYMVKQLENGEVNIEELKKNLEYTASLLEAVYIDETRQILDTEDELRELRSDAVPSEVRDWLASTFTQQTRAKGRRAEEKPKFRSIVHAVQAGIFVERMFRRTYTAVGPTYSTAVHNCLKNLDLWCFDVFSLNRAADDHALRTIVFELLTRHSLISRFKIPTVFLMSFLEALETGYGKYKNPYHNQIHAADVTQTVHCFLLRTGMVHCLSEIEVLAIIFAAAIHDYEHTGTTNSFHIQTKSECAILYNDRSVLENHHISSVFRMMQDDEMNIFINLTKDEFVELRALVIEMVLATDMSCHFQQVKSMKTALQQLERIDKSKALSLLLHAADISHPTKQWSVHSRWTKALMEEFFRQGDKEAELGLPFSPLCDRTSTLVAQSQIGFIDFIVEPTFSVLTDVAEKSVQPLADDDSKSKSQPSFQWRQPSLDVDVGDPNPDVISFRSTWTKYIQENKQKWKERAASGITNQMSIDELSPCEEEAPPSPAEDEHNQNGNLD | ||||||
Modified residue | 7 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 14 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 465 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 513 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-21 | Disordered | ||||
Sequence: MELSPRSPPEMLESDCPSPLE | ||||||
Region | 26-46 | Calmodulin-binding | ||||
Sequence: PSKKMWIKLRSLLRYMVKQLE | ||||||
Region | 117-140 | Calmodulin-binding | ||||
Sequence: EKPKFRSIVHAVQAGIFVERMFRR | ||||||
Domain | 145-502 | PDEase | ||||
Sequence: VGPTYSTAVHNCLKNLDLWCFDVFSLNRAADDHALRTIVFELLTRHSLISRFKIPTVFLMSFLEALETGYGKYKNPYHNQIHAADVTQTVHCFLLRTGMVHCLSEIEVLAIIFAAAIHDYEHTGTTNSFHIQTKSECAILYNDRSVLENHHISSVFRMMQDDEMNIFINLTKDEFVELRALVIEMVLATDMSCHFQQVKSMKTALQQLERIDKSKALSLLLHAADISHPTKQWSVHSRWTKALMEEFFRQGDKEAELGLPFSPLCDRTSTLVAQSQIGFIDFIVEPTFSVLTDVAEKSVQPLADDDSKSKSQPSFQWRQPSLDVDVGDPNPDVISFRSTWTKYIQENKQKWKERAASG | ||||||
Region | 445-474 | Disordered | ||||
Sequence: PLADDDSKSKSQPSFQWRQPSLDVDVGDPN | ||||||
Compositional bias | 449-463 | Polar residues | ||||
Sequence: DDSKSKSQPSFQWRQ | ||||||
Region | 495-535 | Disordered | ||||
Sequence: WKERAASGITNQMSIDELSPCEEEAPPSPAEDEHNQNGNLD |
Sequence similarities
Belongs to the cyclic nucleotide phosphodiesterase family. PDE1 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length535
- Mass (Da)61,254
- Last updated2022-05-25 v2
- Checksum02C1CB67989D1842
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 382 | in Ref. 2; AAB50017 | ||||
Sequence: R → H | ||||||
Compositional bias | 449-463 | Polar residues | ||||
Sequence: DDSKSKSQPSFQWRQ |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AMDS01070813 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AMDS01070814 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
U40585 EMBL· GenBank· DDBJ | AAB50017.1 EMBL· GenBank· DDBJ | mRNA |