Reviewed,
UniProtKB/Swiss-Prot Q9VJ79 (PDE11_DROME)
Last modified
January 19, 2010.
Version 61.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
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Names and origin
| Protein names | Recommended name: Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11 EC=3.1.4.17 EC=3.1.4.35 Alternative name(s): cAMP and cGMP phosphodiesterase 11 | ||||
| Gene names |
| ||||
| Organism | Drosophila melanogaster (Fruit fly) [Complete proteome] | ||||
| Taxonomic identifier | 7227 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora |
Protein attributes
| Sequence length | 1451 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
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. Ref.4 |
| Catalytic activity | Guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate. Adenosine 3',5'-cyclic phosphate + H2O = adenosine 5'-phosphate. |
| Cofactor | 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 By similarity. |
| Tissue specificity | In adults, it is enriched in Malpighian tubules. Ref.4 |
| Sequence similarities | Belongs to the cyclic nucleotide phosphodiesterase family. Contains 2 GAF domains. |
| Biophysicochemical properties | Kinetic parameters: KM=18.5 µM for cAMP KM=6 µM for cGMP |
Ontologies
| Keywords | |
|---|---|
| Coding sequence diversity | Alternative splicing |
| Domain | Repeat |
| Ligand | Metal-binding cAMP cGMP |
| Molecular function | Hydrolase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | cAMP metabolic process Ref.4 Inferred from direct assay. Source: UniProtKB cGMP metabolic process Ref.4Inferred from direct assay. Source: UniProtKB signal transductionInferred from electronic annotation. Source: InterPro |
| Molecular function | 3',5'-cyclic-AMP phosphodiesterase activity Ref.4 Inferred from direct assay. Source: UniProtKB 3',5'-cyclic-GMP phosphodiesterase activity Ref.4Inferred from direct assay. Source: UniProtKB metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform B (identifier: Q9VJ79-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform C (identifier: Q9VJ79-3) The sequence of this isoform differs from the canonical sequence as follows: 1-44: Missing. 45-64: QTPSHSPQIQHHSEIIPATT → MASSPNNAAPPVLWRARRKI | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform D (identifier: Q9VJ79-2) The sequence of this isoform differs from the canonical sequence as follows: 1-1: M → MKVTQSEENT...GLTFALLAGP | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1451 | 1451 | Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11 | PRO_0000247044 | |||||
Regions | |||||||||
| Domain | 419 – 572 | 154 | GAF 1 | ||||||
| Domain | 604 – 754 | 151 | GAF 2 | ||||||
| Region | 836 – 1100 | 265 | Catalytic By similarity | ||||||
| Compositional bias | 1121 – 1124 | 4 | Poly-Gln | ||||||
| Compositional bias | 1328 – 1436 | 109 | His-rich | ||||||
Sites | |||||||||
| Active site | 860 | 1 | Proton donor By similarity | ||||||
| Metal binding | 864 | 1 | Divalent metal cation 1 By similarity | ||||||
| Metal binding | 900 | 1 | Divalent metal cation 1 By similarity | ||||||
| Metal binding | 901 | 1 | Divalent metal cation 1 By similarity | ||||||
| Metal binding | 901 | 1 | Divalent metal cation 2 By similarity | ||||||
| Metal binding | 904 | 1 | Divalent metal cation 2 By similarity | ||||||
| Metal binding | 929 | 1 | Divalent metal cation 2 By similarity | ||||||
| Metal binding | 1011 | 1 | Divalent metal cation 1 By similarity | ||||||
| Binding site | 1064 | 1 | cAMP or cGMP By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 44 | 44 | Missing in isoform C. | VSP_030328 | |||||
| Alternative sequence | 1 | 1 | M → MKVTQSEENTRNTSDRSKSV QTNRKFDNFNWLLSCGLLAA VKSTKLIPQLPRQQQPKKYN LRYAAELLKFDKIQFIKTEG LTFALLAGP in isoform D. | VSP_019906 | |||||
| Alternative sequence | 45 – 64 | 20 | QTPSH…IPATT → MASSPNNAAPPVLWRARRKI in isoform C. | VSP_030329 | |||||
Experimental info | |||||||||
| Sequence conflict | 38 | 1 | Q → QQQ in AAM52774. Ref.3 | ||||||
| Sequence conflict | 1192 | 1 | V → A in AAM52774. Ref.3 | ||||||
| Sequence conflict | 1196 | 1 | A → V in AAM52774. Ref.3 | ||||||
| Sequence conflict | 1232 | 1 | C → R in AAM52774. Ref.3 | ||||||
| Sequence conflict | 1342 | 1 | H → HNH in AAM52774. Ref.3 | ||||||
Sequences
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References
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE014134 Genomic DNA. Translation: AAF53675.3. AE014134 Genomic DNA. Translation: AAF53676.2. AY122262 mRNA. Translation: AAM52774.1. |
| RefSeq | NP_001097177.1. NP_609885.2. |
| UniGene | Dm.13948 |
3D structure databases | |
| SMR | Q9VJ79. Positions 408-763, 787-1105. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q9VJ79. 6 interactions. |
Genome annotation databases | |
| Ensembl | FBtr0112544; FBpp0111456; FBgn0085370; Drosophila melanogaster. [Genome view] FBtr0112545; FBpp0111457; FBgn0085370; Drosophila melanogaster. [Genome view] |
| GeneID | 35107. |
| KEGG | dme:Dmel_CG34341. |
Organism-specific databases | |
| CTD | 35107. |
| FlyBase | FBgn0085370. Pde11. |
Phylogenomic databases | |
| eggNOG | inNOG05173. |
| InParanoid | Q9VJ79. |
| OrthoDB | EOG9MCX5S. |
| PhylomeDB | Q9VJ79. |
Enzyme and pathway databases | |
| BRENDA | 3.1.4.17. 48. 3.1.4.35. 48. |
Gene expression databases | |
| ArrayExpress | Q9VJ79. |
| GermOnline | CG10231. Drosophila melanogaster. |
Family and domain databases | |
| InterPro | IPR003018. GAF. IPR003607. Metal-dep_PHydrolase_HD_dom. 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... |
Other Resources | |
| NextBio | 791899. |
Entry information
| Entry name | PDE11_DROME | ||||||||
| Accession | Primary (citable) accession number: Q9VJ79 Secondary accession number(s): Q8MQW0, Q9VJ78 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Drosophila annotation project | ||||||||
Relevant documents
| Drosophila Drosophila: entries, gene names and cross-references to FlyBase |
| SIMILARITY comments Index of protein domains and families |

Clusters with


