Q01061 · PDE1B_BOVIN
- ProteinDual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B
- GenePDE1B
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids534 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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+.
Kinetics
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
23 nmol/min/mg | with cGMP as substrate (in presence of calcium and calmodulin) | ||||
4.9 nmol/min/mg | with cAMP as substrate (in presence of calcium and calmodulin) |
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 221 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 225 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 261 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 262 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 262 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 368 | 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 | 3',5'-cyclic-GMP phosphodiesterase activity | |
Molecular Function | calmodulin binding | |
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 |
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
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionQ01061
Proteomes
Subcellular Location
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000198787 | 1-534 | Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B | |||
Sequence: MELSPRSPPEMLESDCPSPLELKSAPSKKMWIKLRSLLRYMVKQLENGEVNIEELKKNLEYTASLLEAVYIDETRQILDTEDELQELRSDAVPSEVRDWLASTFTQQTRAKGPSEEKPKFRSIVHAVQAGIFVERMFRRTYTSVGPTYSTAVLNCLKNVDLWCFDVFSLNRAADDHALRTIVFELLTRHNLISRFKIPTVFLMTFLDALETGYGKYKNPYHNQIHAADVTQTVHCFLLRTGMVHCLSEIEVLAIIFAAAIHDYEHTGTTNSFHIQTKSECAILYNDRSVLENHHISSVFRMMQDDEMNIFINLTKDEFVELRALVIEMVLATDMSCHFQQVKSMKTALQQLERIDKSKALSLLLHAADISHPTKQWSVHSRWTKALMEEFFRQGDKEAELGLPFSPLCDRTSTLVAQSQIGFIDFIVEPTFSVLTDVAEKSVQPTGDDDSKSKNQPSFQWRQPSLDVEVGDPNPDVVSFRSTWTKYIQENKQKWKERAASGITNQMSIDELSPCEEEAPASPAEDEHNQNGNLD | ||||||
Modified residue | 7 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 14 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 464 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 512 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
Expression
Tissue specificity
Expressed in central nervous system regions. Most abundant in basal ganglia. Also found in kidney papilla and adrenal medulla.
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-21 | Disordered | ||||
Sequence: MELSPRSPPEMLESDCPSPLE | ||||||
Region | 27-47 | Calmodulin-binding | ||||
Sequence: SKKMWIKLRSLLRYMVKQLEN | ||||||
Region | 116-139 | Calmodulin-binding | ||||
Sequence: EKPKFRSIVHAVQAGIFVERMFRR | ||||||
Domain | 144-501 | PDEase | ||||
Sequence: VGPTYSTAVLNCLKNVDLWCFDVFSLNRAADDHALRTIVFELLTRHNLISRFKIPTVFLMTFLDALETGYGKYKNPYHNQIHAADVTQTVHCFLLRTGMVHCLSEIEVLAIIFAAAIHDYEHTGTTNSFHIQTKSECAILYNDRSVLENHHISSVFRMMQDDEMNIFINLTKDEFVELRALVIEMVLATDMSCHFQQVKSMKTALQQLERIDKSKALSLLLHAADISHPTKQWSVHSRWTKALMEEFFRQGDKEAELGLPFSPLCDRTSTLVAQSQIGFIDFIVEPTFSVLTDVAEKSVQPTGDDDSKSKNQPSFQWRQPSLDVEVGDPNPDVVSFRSTWTKYIQENKQKWKERAASG | ||||||
Region | 442-473 | Disordered | ||||
Sequence: VQPTGDDDSKSKNQPSFQWRQPSLDVEVGDPN | ||||||
Compositional bias | 448-462 | Polar residues | ||||
Sequence: DDSKSKNQPSFQWRQ | ||||||
Region | 494-534 | Disordered | ||||
Sequence: WKERAASGITNQMSIDELSPCEEEAPASPAEDEHNQNGNLD |
Sequence similarities
Belongs to the cyclic nucleotide phosphodiesterase family. PDE1 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length534
- Mass (Da)61,006
- Last updated1994-06-01 v1
- ChecksumC86C3F48E0AE9B69
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 448-462 | Polar residues | ||||
Sequence: DDSKSKNQPSFQWRQ |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M94867 EMBL· GenBank· DDBJ | AAA74558.1 EMBL· GenBank· DDBJ | mRNA |