A0A3Q1MCV4 · A0A3Q1MCV4_BOVIN
- ProteinPhosphodiesterase
- GenePDE1C
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids648 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
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
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 | 219 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 219-223 | AMP (UniProtKB | ChEBI) | ||||
Sequence: HNLMH | ||||||
Binding site | 223 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 259 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 260 | AMP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 260 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 260 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 367 | AMP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 367 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 418 | AMP (UniProtKB | ChEBI) | ||||
Sequence: Q |
GO annotations
Aspect | Term | |
---|---|---|
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 |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphodiesterase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionA0A3Q1MCV4
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 60 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
Expression
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 142-519 | PDEase | ||||
Sequence: VGLSYPPAVIEALKDVDKWSFDVFSLNEASGDHALKFIFYELLTRYDLISRFKIPISALVSFVEALEVGYSKHKNPYHNLMHAADVTQTVHYLLYKTGVANWLTELEIFAIIFSAAIHDYEHTGTTNNFHIQTRSDPAILYNDRSVLENHHLSAAYRLLQEDEEMNILINLSKDDWREFRTLVIEMVMATDMSCHFQQIKAMKTALQQPEAIEKPKALSLMLHTADISHPAKAWELHHRWTMSLLEEFFRQGDREAELGLPFSPLCDRKSTMVAQSQVGFIDFIVEPTFTVLTDMTEKIVSPLIDEPSQTGGTGQRRSSLNNISSTDAKRSGVKSSGSEGSAPINNPVIPVDYKSFKATWTEVVHINRERWRAKVPKE | ||||||
Region | 444-490 | Disordered | ||||
Sequence: LIDEPSQTGGTGQRRSSLNNISSTDAKRSGVKSSGSEGSAPINNPVI | ||||||
Compositional bias | 447-484 | Polar residues | ||||
Sequence: EPSQTGGTGQRRSSLNNISSTDAKRSGVKSSGSEGSAP | ||||||
Compositional bias | 514-561 | Basic and acidic residues | ||||
Sequence: AKVPKEEKAKKEAEEKARLAAEEKQKEMEAKSQAEESASGKAEKKTSG | ||||||
Region | 514-648 | Disordered | ||||
Sequence: AKVPKEEKAKKEAEEKARLAAEEKQKEMEAKSQAEESASGKAEKKTSGEAKNQVNGTRTNKSNNPHGKNSKTEKSSGEKQQNGDLKDGKNKTGKKDQSDVGNDSKKTDGTKKHSQGSPAPSTSSMSRLTLPGDYG | ||||||
Compositional bias | 562-579 | Polar residues | ||||
Sequence: EAKNQVNGTRTNKSNNPH | ||||||
Compositional bias | 580-625 | Basic and acidic residues | ||||
Sequence: GKNSKTEKSSGEKQQNGDLKDGKNKTGKKDQSDVGNDSKKTDGTKK | ||||||
Compositional bias | 626-642 | Polar residues | ||||
Sequence: HSQGSPAPSTSSMSRLT |
Sequence similarities
Belongs to the cyclic nucleotide phosphodiesterase family. PDE1 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length648
- Mass (Da)73,300
- Last updated2024-05-29 v2
- Checksum4FC114AC1ED39719
Computationally mapped potential isoform sequences
There are 9 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A3Q1N4S8 | A0A3Q1N4S8_BOVIN | PDE1C | 769 | ||
A0A3Q1LI50 | A0A3Q1LI50_BOVIN | PDE1C | 717 | ||
A0A3Q1LN38 | A0A3Q1LN38_BOVIN | PDE1C | 638 | ||
F1MCY0 | F1MCY0_BOVIN | PDE1C | 676 | ||
A0A3Q1LQL5 | A0A3Q1LQL5_BOVIN | PDE1C | 734 | ||
A0A3Q1M1A4 | A0A3Q1M1A4_BOVIN | PDE1C | 619 | ||
A0A3Q1LV25 | A0A3Q1LV25_BOVIN | PDE1C | 634 | ||
A0A3Q1M871 | A0A3Q1M871_BOVIN | PDE1C | 820 | ||
A0A3Q1LWK6 | A0A3Q1LWK6_BOVIN | PDE1C | 634 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 447-484 | Polar residues | ||||
Sequence: EPSQTGGTGQRRSSLNNISSTDAKRSGVKSSGSEGSAP | ||||||
Compositional bias | 514-561 | Basic and acidic residues | ||||
Sequence: AKVPKEEKAKKEAEEKARLAAEEKQKEMEAKSQAEESASGKAEKKTSG | ||||||
Compositional bias | 562-579 | Polar residues | ||||
Sequence: EAKNQVNGTRTNKSNNPH | ||||||
Compositional bias | 580-625 | Basic and acidic residues | ||||
Sequence: GKNSKTEKSSGEKQQNGDLKDGKNKTGKKDQSDVGNDSKKTDGTKK | ||||||
Compositional bias | 626-642 | Polar residues | ||||
Sequence: HSQGSPAPSTSSMSRLT |
Keywords
- Technical term