A6XDB1 · A6XDB1_MOUSE
- ProteinPhosphodiesterase
- GenePde4d
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids504 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
Catalytic activity
- 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, 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 | 158 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 158-162 | AMP (UniProtKB | ChEBI) | ||||
Sequence: HNNIH | ||||||
Binding site | 162 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 198 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 199 | AMP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 199 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 199 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 316 | AMP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 316 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 367 | 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
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionA6XDB1
Proteomes
Organism-specific databases
PTM/Processing
Proteomic databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 39-60 | Disordered | ||||
Sequence: EVEIPSPTQKEKEKKKRPMSQI | ||||||
Compositional bias | 41-58 | Basic and acidic residues | ||||
Sequence: EIPSPTQKEKEKKKRPMS | ||||||
Domain | 82-411 | PDEase | ||||
Sequence: VKTEQEDVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIFQERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAADVVQSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPGVSNQFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENCDIFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMVETKKVTSSGVLLLDNYSDRIQVLQNMVHCADLSNPTKPLQLYRQWTDRIMEEFFRQGDRERERGMEISPMCDKHNASVEKSQVGFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQSTIPQS | ||||||
Region | 406-504 | Disordered | ||||
Sequence: STIPQSPSPAPDDQEEGRQGQTEKFQFELTLEEDCESDTEKDSGSQVEEDTSCSDSKTLCTQDSESTEIPLDEQVEEEAVAEEESQPETCVPDDCCPDT | ||||||
Compositional bias | 421-436 | Basic and acidic residues | ||||
Sequence: EGRQGQTEKFQFELTL | ||||||
Compositional bias | 454-473 | Polar residues | ||||
Sequence: EDTSCSDSKTLCTQDSESTE | ||||||
Compositional bias | 474-494 | Acidic residues | ||||
Sequence: IPLDEQVEEEAVAEEESQPET |
Sequence similarities
Belongs to the cyclic nucleotide phosphodiesterase family. PDE4 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length504
- Mass (Da)57,578
- Last updated2007-08-21 v1
- Checksum4AF93CD989A6A125
Computationally mapped potential isoform sequences
There are 9 potential isoforms mapped to this entry
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 41-58 | Basic and acidic residues | ||||
Sequence: EIPSPTQKEKEKKKRPMS | ||||||
Compositional bias | 421-436 | Basic and acidic residues | ||||
Sequence: EGRQGQTEKFQFELTL | ||||||
Compositional bias | 454-473 | Polar residues | ||||
Sequence: EDTSCSDSKTLCTQDSESTE | ||||||
Compositional bias | 474-494 | Acidic residues | ||||
Sequence: IPLDEQVEEEAVAEEESQPET |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DQ665896 EMBL· GenBank· DDBJ | ABG57277.1 EMBL· GenBank· DDBJ | mRNA |