Q8CG03 · PDE5A_MOUSE
- ProteincGMP-specific 3',5'-cyclic phosphodiesterase
- GenePde5a
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids865 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-GMP. Specifically regulates nitric-oxide-generated cGMP.
Catalytic activity
- 3',5'-cyclic GMP + H2O = GMP + H+This reaction proceeds in the forward direction.
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 Zn2+ ion per subunit. Binds 2 divalent metal cations per subunit: site 1 preferentially binds zinc, while site 2 has a preference for magnesium. Tightly binds zinc.
Note: Binds 1 Mg2+ ions per subunit. Binds 2 divalent metal cations per subunit: site 1 preferentially binds zinc, while site 2 has a preference for magnesium. Binds magnesium less tightly than zinc.
Pathway
Purine metabolism; 3',5'-cyclic GMP degradation; GMP from 3',5'-cyclic GMP: step 1/1.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 603 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 607 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 643 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 644 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 644 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 754 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 807 | 3',5'-cyclic GMP (UniProtKB | ChEBI) | ||||
Sequence: Q |
GO annotations
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namecGMP-specific 3',5'-cyclic phosphodiesterase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ8CG03
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000198824 | 1-865 | cGMP-specific 3',5'-cyclic phosphodiesterase | |||
Sequence: MERAGPNSVRSQQQRDPDWVEAWLDDHRDFTFSYFIRKATRDMVNAWFSERVHNIPVCKEGIRAHTESCSCSLQQSPHADNTTPGAPARKISASEFDRPLRPIVVKDSEGTVSFLSDSGKKEQMPLTPPRFDSDEGDQCSRLLELVKDISSHLDVTALCHKIFLHIHGLISADRYSLFLVCEDSSKDKFLISRLFDVAEGSTLEEASNNCIRLEWNKGIVGHVAAFGEPLNIKDAYEDPRFNAEVDQITGYKTQSILCMPIKNHREEVVGVAQAINKKSGNGGTFTEKDEKDFAAYLAFCGIVLHNAQLYETSLLENKRNQVLLDLASLIFEEQQSLEVILKKIAATIISFMQVQKCTIFIVDEDCPDSFSRVFHMECEEVGKPSDPLTREQDANKINYMYAQYVKNTMEPLNIPDVTKDKRFPWTNENMGHVNTPCIGSLLCTPIKNGKKNKVIGVCQLVNKMEENTGKIKAFNQNDEQFLEAFVIFCGLGIQNTQMYEAVERAMAKQMVTLEVLSYHASAAEEETRELQALSAAVVPSAQTLKITDFSFSDFELSDLETALCTIRMFTDLNLVQNFQMKHEVLCRWILSVKKNYRKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLETLALLIAALSHDLDHRGVNNSYIQRSEHPLAQLYCHSIMEHHHFDQCLMILNSPGNQILSGLSIDEYKTTLKIIKQAILATDLALYIKRRGEFFELIRKNQFSFEDPLQKELFLAMLMTACDLSAITKPWPIQQRIAELVAAEFFDQGDRERKELNMEPADLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCLPLLDGCRKNRQKWQALAEQQEKMLLNGESSQGKRD | ||||||
Modified residue | 92 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylation is regulated by binding of cGMP to the two allosteric sites. Phosphorylation by PRKG1 leads to its activation.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 154-304 | GAF 1 | ||||
Sequence: DVTALCHKIFLHIHGLISADRYSLFLVCEDSSKDKFLISRLFDVAEGSTLEEASNNCIRLEWNKGIVGHVAAFGEPLNIKDAYEDPRFNAEVDQITGYKTQSILCMPIKNHREEVVGVAQAINKKSGNGGTFTEKDEKDFAAYLAFCGIVL | ||||||
Domain | 336-493 | GAF 2 | ||||
Sequence: SLEVILKKIAATIISFMQVQKCTIFIVDEDCPDSFSRVFHMECEEVGKPSDPLTREQDANKINYMYAQYVKNTMEPLNIPDVTKDKRFPWTNENMGHVNTPCIGSLLCTPIKNGKKNKVIGVCQLVNKMEENTGKIKAFNQNDEQFLEAFVIFCGLGI | ||||||
Domain | 526-850 | PDEase | ||||
Sequence: ETRELQALSAAVVPSAQTLKITDFSFSDFELSDLETALCTIRMFTDLNLVQNFQMKHEVLCRWILSVKKNYRKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLETLALLIAALSHDLDHRGVNNSYIQRSEHPLAQLYCHSIMEHHHFDQCLMILNSPGNQILSGLSIDEYKTTLKIIKQAILATDLALYIKRRGEFFELIRKNQFSFEDPLQKELFLAMLMTACDLSAITKPWPIQQRIAELVAAEFFDQGDRERKELNMEPADLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCLPLLDGCRKNRQKWQALAEQQ |
Domain
Composed of a C-terminal catalytic domain containing two putative divalent metal sites and an N-terminal regulatory domain which contains two homologous allosteric cGMP-binding regions, A and B.
Sequence similarities
Belongs to the cyclic nucleotide phosphodiesterase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length865
- Mass (Da)98,407
- Last updated2011-07-27 v2
- ChecksumBADD21CC6B62045E
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0G2JF67 | A0A0G2JF67_MOUSE | Pde5a | 833 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 176 | in Ref. 1; AAN17330 | ||||
Sequence: S → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF541937 EMBL· GenBank· DDBJ | AAN17330.1 EMBL· GenBank· DDBJ | mRNA | ||
CH466532 EMBL· GenBank· DDBJ | EDL12317.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC119137 EMBL· GenBank· DDBJ | AAI19138.1 EMBL· GenBank· DDBJ | mRNA | ||
BC120486 EMBL· GenBank· DDBJ | AAI20487.1 EMBL· GenBank· DDBJ | mRNA |