B4PSS5 (PDE6_DROYA) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 24.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: cGMP-specific 3',5'-cyclic phosphodiesterase EC=3.1.4.35 | ||||
| Gene names |
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| Organism | Drosophila yakuba (Fruit fly) [Complete proteome] | ||||
| Taxonomic identifier | 7245 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora |
Protein attributes
| Sequence length | 1149 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Has a role regulating cGMP transport in Malpighian tubule principal cells By similarity. UniProtKB Q9VFI9 |
| Catalytic activity | Guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate. UniProtKB Q9VFI9 |
| 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. |
| Subunit structure | Interacts with PrBP By similarity. UniProtKB Q9VFI9 |
| Subcellular location | Cell membrane; Lipid-anchor; Cytoplasmic side By similarity UniProtKB Q9VFI9. |
| Sequence similarities | Belongs to the cyclic nucleotide phosphodiesterase family. Contains 2 GAF domains. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell membrane Membrane |
| Domain | Repeat |
| Ligand | Metal-binding cGMP |
| Molecular function | Hydrolase |
| PTM | Lipoprotein Methylation Prenylation |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | cGMP metabolic process Inferred from sequence or structural similarity. Source: UniProtKB signal transductionInferred from electronic annotation. Source: InterPro |
| Cellular component | plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 3',5'-cyclic-GMP phosphodiesterase activity Inferred from sequence or structural similarity. Source: UniProtKB 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 – 1146 | 1146 | cGMP-specific 3',5'-cyclic phosphodiesterase UniProtKB Q9VFI9 | PRO_0000363704 | |||||
| Propeptide | 1147 – 1149 | 3 | Removed in mature form By similarity UniProtKB Q9VFI9 | PRO_0000363705 | |||||
Regions | |||||||||
| Domain | 278 – 430 | 153 | GAF 1 | ||||||
| Domain | 462 – 643 | 182 | GAF 2 | ||||||
| Compositional bias | 6 – 150 | 145 | Ser-rich | ||||||
Sites | |||||||||
| Active site | 749 | 1 | Proton donor By similarity | ||||||
| Metal binding | 753 | 1 | Divalent metal cation 1 By similarity | ||||||
| Metal binding | 789 | 1 | Divalent metal cation 1 By similarity | ||||||
| Metal binding | 790 | 1 | Divalent metal cation 1 By similarity | ||||||
| Metal binding | 790 | 1 | Divalent metal cation 2 By similarity | ||||||
| Metal binding | 900 | 1 | Divalent metal cation 1 By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1146 | 1 | Cysteine methyl ester By similarity UniProtKB Q9VFI9 | ||||||
| Lipidation | 1146 | 1 | S-farnesyl cysteine By similarity UniProtKB Q9VFI9 | ||||||
Sequences
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References
| [1] | "Evolution of genes and genomes on the Drosophila phylogeny." Drosophila 12 genomes consortium Nature 450:203-218(2007) [PubMed: 17994087] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tai18E2 / Tucson 14021-0261.01. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CM000160 Genomic DNA. Translation: EDW97571.1. |
| RefSeq | XP_002097859.1. XM_002097823.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | B4PSS5. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblMetazoa | FBtr0272963; FBpp0271455; FBgn0243466. |
| GeneID | 6537301. |
| KEGG | dya:Dyak_GE26445. |
Organism-specific databases | |
| FlyBase | FBgn0243466. Dyak\GE26445. |
Phylogenomic databases | |
| GeneTree | EMGT00050000002162. |
| OrthoDB | EOG41RN8T. |
| PhylomeDB | B4PSS5. |
Family and domain databases | |
| InterPro | IPR003018. GAF. IPR003607. Metal-dep_PHydrolase_HD_dom. IPR023088. PDEase. IPR002073. PDEase_catalytic_dom. IPR023174. PDEase_CS. [Graphical view] |
| Gene3D | G3DSA:1.10.1300.10. PDEase_catalytic_dom. 1 hit. |
| KO | K13763. |
| 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 | PDE6_DROYA | ||||||||
| Accession | Primary (citable) accession number: B4PSS5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | 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