Reviewed,
UniProtKB/Swiss-Prot Q1KKS3 (PDE11_FUGRU)
Last modified
June 16, 2009.
Version 16.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A EC=3.1.4.17 EC=3.1.4.35 Alternative name(s): cAMP and cGMP phosphodiesterase 11A | ||
| Gene names |
| ||
| Organism | Fugu rubripes (Japanese pufferfish) (Takifugu rubripes) | ||
| Taxonomic identifier | 31033 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Euteleostei › Neoteleostei › Acanthomorpha › Acanthopterygii › Percomorpha › Tetraodontiformes › Tetradontoidea › Tetraodontidae › Takifugu |
Protein attributes
| Sequence length | 903 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides cAMP and cGMP. Catalyzes the hydrolysis of both cAMP and cGMP to 5'-AMP and 5'-GMP, respectively By similarity. |
| Catalytic activity | Guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate. Adenosine 3',5'-cyclic phosphate + H2O = adenosine 5'-phosphate. |
| Cofactor | Divalent cations By similarity. |
| Enzyme regulation | Inhibited by 3-isobutyl-1-methylxanthine (IBMX), zaprinast and dipyridamole. cGMP acts as an allosteric activator By similarity. |
| Subcellular location | |
| Domain | The tandem GAF domains bind cGMP, and regulate enzyme activity. The binding of cGMP leading to stimulate the enzyme activity By similarity. |
| Sequence similarities | Belongs to the cyclic nucleotide phosphodiesterase family. Contains 2 GAF domains. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Domain | Repeat |
| Ligand | Metal-binding cAMP cGMP |
| Molecular function | Hydrolase |
| Technical term | Allosteric enzyme |
| Gene Ontology (GO) | |
| Biological process | signal transduction Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 3',5'-cyclic-GMP phosphodiesterase activity Inferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 903 | 903 | Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A | PRO_0000247043 | |||||
Regions | |||||||||
| Domain | 175 – 324 | 150 | GAF 1 | ||||||
| Domain | 356 – 512 | 157 | GAF 2 | ||||||
| Region | 594 – 859 | 266 | Catalytic By similarity | ||||||
Sites | |||||||||
| Metal binding | 622 | 1 | Divalent metal cation 1 By similarity | ||||||
| Metal binding | 658 | 1 | Divalent metal cation 1 By similarity | ||||||
| Metal binding | 659 | 1 | Divalent metal cation 1 By similarity | ||||||
| Metal binding | 659 | 1 | Divalent metal cation 2 By similarity | ||||||
| Metal binding | 662 | 1 | Divalent metal cation 2 By similarity | ||||||
| Metal binding | 688 | 1 | Divalent metal cation 2 By similarity | ||||||
| Metal binding | 770 | 1 | Divalent metal cation 1 By similarity | ||||||
| Binding site | 823 | 1 | cAMP or cGMP By similarity | ||||||
Sequences
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References
| [1] | "Highly conserved syntenic blocks at the vertebrate Hox loci and conserved regulatory elements within and outside Hox gene clusters." Lee A.P., Koh E.G.L., Tay A., Brenner S., Venkatesh B. Proc. Natl. Acad. Sci. U.S.A. 103:6994-6999(2006) [PubMed: 16636282] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| DQ481668 Genomic DNA. Translation: ABF22471.1. | |
3D structure databases | |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | Q1KKS3. |
Enzyme and pathway databases | |
| BRENDA | 3.1.4.17. 281122. 3.1.4.35. 281122. |
Family and domain databases | |
| InterPro | IPR003018. GAF. IPR003607. Met-dep_phosphohydro_HD. IPR002073. PDEase. [Graphical view] |
| Pfam | PF01590. GAF. 2 hits. PF00233. PDEase_I. 1 hit. [Graphical view] |
| PRINTS | PR00387. PDIESTERASE1. |
| SMART | SM00065. GAF. 2 hits. SM00471. HDc. 1 hit. [Graphical view] |
| PROSITE | PS00126. PDEASE_I. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PDE11_FUGRU | ||||||||
| Accession | Primary (citable) accession number: Q1KKS3 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||

Clusters with


