Q7KYS4 · Q7KYS4_HUMAN
- ProteinPhosphodiesterase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids606 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score2/5
Function
Catalytic activity
- 3',5'-cyclic AMP + H2O = AMP + 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.
Pathway
Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 282 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 282-286 | AMP (UniProtKB | ChEBI) | ||||
Sequence: HNSLH | ||||||
Binding site | 286 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 322 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 323 | AMP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 323 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 323 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 440 | AMP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 440 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 491 | AMP (UniProtKB | ChEBI) | ||||
Sequence: Q |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 3',5'-cyclic-AMP phosphodiesterase activity | |
Molecular Function | metal ion binding | |
Biological Process | cAMP catabolic process | |
Biological Process | signal transduction |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphodiesterase
- EC number
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ7KYS4
PTM/Processing
Proteomic databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 75-94 | Disordered | ||||
Sequence: AKQGPVGNPSSSNQLPPAED | ||||||
Compositional bias | 79-93 | Polar residues | ||||
Sequence: PVGNPSSSNQLPPAE | ||||||
Domain | 206-535 | PDEase | ||||
Sequence: VQTDQEEQLAKELEDTNKWGLDVFKVAELSGNQPLTAIIFSIFQERDLLKTFQIPADTLATYLLMLEGHYHANVAYHNSLHAADVAQSTHVLLATPALEAVFTDLEILAALFASAIHDVDHPGVSNQFLINTNSELALMYNDASVLENHHLAVGFKLLQAENCDIFQNLSAKQRLSLRRMVIDMVLATDMSKHMNLLADLKTMVETKKVTSLGVLLLDNYSDRIQVLQNLVHCADLSNPTKPLPLYRQWTDRIMAEFFQQGDRERESGLDISPMCDKHTASVEKSQVGFIDYIAHPLWETWADLVHPDAQDLLDTLEDNREWYQSKIPRS | ||||||
Region | 530-549 | Disordered | ||||
Sequence: SKIPRSPSDLTNPERDGPDR | ||||||
Compositional bias | 557-574 | Acidic residues | ||||
Sequence: EEAEEEDEEEEEEGEETA | ||||||
Region | 557-606 | Disordered | ||||
Sequence: EEAEEEDEEEEEEGEETALAKEALELPDTELLSPEAGPAPGDLPLDNQRT |
Sequence similarities
Belongs to the cyclic nucleotide phosphodiesterase family. PDE4 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length606
- Mass (Da)67,719
- Last updated2004-07-05 v1
- ChecksumAC14D9401F5CCDCE
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 79-93 | Polar residues | ||||
Sequence: PVGNPSSSNQLPPAE | ||||||
Compositional bias | 557-574 | Acidic residues | ||||
Sequence: EEAEEEDEEEEEEGEETA |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U88712 EMBL· GenBank· DDBJ | AAC51915.1 EMBL· GenBank· DDBJ | mRNA |