A0A8I6A5M3 · A0A8I6A5M3_RAT
- ProteinPhosphodiesterase
- GenePde1a
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids526 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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
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 | 203 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 203-207 | AMP (UniProtKB | ChEBI) | ||||
Sequence: HNLVH | ||||||
Binding site | 207 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 243 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 244 | AMP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 244 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 244 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 350 | AMP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 350 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 401 | AMP (UniProtKB | ChEBI) | ||||
Sequence: Q |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | neuronal cell body | |
Cellular Component | sperm flagellum | |
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 | |
Biological Process | cGMP catabolic process | |
Biological Process | regulation of smooth muscle cell apoptotic process | |
Biological Process | regulation of smooth muscle cell proliferation |
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 > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionA0A8I6A5M3
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 126-506 | PDEase | ||||
Sequence: VGLTYPAAVIVTLKEVDKWSFDVFALNEASGEHSLKFMIYELFTRYDLINRFKIPVSCLIAFAEALEVGYSKHKNPYHNLVHAADVTQTVHYIMLHTGIMHWLTELEILAMVFAAAVHDYEHTGTTNNFHIQTRSDVAILYNDRSVLENHHVSAAYRLMQEEEMNILVNLSKDDWRDLRNLVIEMVLATDMSGHFQQIKNIRSSLQQPEGIDRAKTMSLILHAADISHPAKTWKLHYRWTMALMEEFFLQGDKEAELGLPFSPLCDRKSTMVAQSQIGFIDFIVEPTFSLLTDSTEKIVIPLIEEASKPESSNYGASSSSTMIGFHVADALRRSNTKGCMSDGTYAPDYSLSAVDLKSFKNNLVDIIQQNKERWKELAAQG |
Sequence similarities
Belongs to the cyclic nucleotide phosphodiesterase family. PDE1 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length526
- Mass (Da)60,350
- Last updated2022-05-25 v1
- Checksum22A5BEFB4090D4CB
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6A416 | A0A8I6A416_RAT | Pde1a | 542 | ||
A0A0G2K2K1 | A0A0G2K2K1_RAT | Pde1a | 515 | ||
A0A0G2JZX9 | A0A0G2JZX9_RAT | Pde1a | 465 | ||
A0A8I6GJQ6 | A0A8I6GJQ6_RAT | Pde1a | 508 | ||
A0A8I5Y879 | A0A8I5Y879_RAT | Pde1a | 508 | ||
A0A8I5Y792 | A0A8I5Y792_RAT | Pde1a | 515 |
Keywords
- Technical term