Q8VID6 (PDE11_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 71.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames 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 |
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| Organism | Rattus norvegicus (Rat) [Reference proteome] | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus![]() |
Protein attributes
| Sequence length | 935 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 By similarity. Ref.1 |
| 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. |
| Enzyme regulation | Inhibited by 3-isobutyl-1-methylxanthine (IBMX), zaprinast and dipyridamole. cGMP acts as an allosteric activator. Ref.1 |
| Subcellular location | |
| Tissue specificity | Isoform 1 is expressed in brain, heart, kidney and liver, but not in prostate. Isoform 2 is specifically expressed in testis. Isoform 3 is expressed in various tissues including brain, lung, skeletal muscle, spleen, testis and prostate. Ref.1 |
| Domain | The tandem GAF domains bind cGMP, and regulate enzyme activity. The binding of cGMP stimulates enzyme activity By similarity. |
| Sequence similarities | Belongs to the cyclic nucleotide phosphodiesterase family. Contains 2 GAF domains. |
| Biophysicochemical properties | Kinetic parameters: KM=3.9 µM for cAMP (isoform 1) Ref.1 KM=1.6 µM for cGMP (isoform 1) KM=4.0 µM for cAMP (isoform 2) KM=1.6 µM for cGMP (isoform 2) KM=2.2 µM for cAMP (isoform 3) KM=1.3 µM for cGMP (isoform 3) |
Ontologies
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q8VID6-1) Also known as: PDE11A4; 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. | ||||||
| Isoform 2 (identifier: Q8VID6-2) Also known as: PDE11A3; The sequence of this isoform differs from the canonical sequence as follows: 1-250: Missing. 251-304: KTLVSKFFDV...ETVNIPDAYQ → MLKQARRFSF...FLTRMQTRTK | ||||||
| Isoform 3 (identifier: Q8VID6-3) Also known as: PDE11A2; The sequence of this isoform differs from the canonical sequence as follows: 1-354: Missing. 355-357: DEK → MSW |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 935 | 935 | Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A | PRO_0000247042 | |||||
Regions | |||||||||
| Domain | 217 – 370 | 154 | GAF 1 | ||||||
| Domain | 402 – 558 | 157 | GAF 2 | ||||||
| Region | 640 – 905 | 266 | Catalytic By similarity | ||||||
Sites | |||||||||
| Active site | 664 | 1 | Proton donor By similarity | ||||||
| Metal binding | 668 | 1 | Divalent metal cation 1 By similarity | ||||||
| Metal binding | 704 | 1 | Divalent metal cation 1 By similarity | ||||||
| Metal binding | 705 | 1 | Divalent metal cation 1 By similarity | ||||||
| Metal binding | 705 | 1 | Divalent metal cation 2 By similarity | ||||||
| Metal binding | 708 | 1 | Divalent metal cation 2 By similarity | ||||||
| Metal binding | 734 | 1 | Divalent metal cation 2 By similarity | ||||||
| Metal binding | 816 | 1 | Divalent metal cation 1 By similarity | ||||||
| Binding site | 869 | 1 | cAMP or cGMP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 162 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 239 | 1 | Phosphoserine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 354 | 354 | Missing in isoform 3. | VSP_019902 | |||||
| Alternative sequence | 1 – 250 | 250 | Missing in isoform 2. | VSP_019903 | |||||
| Alternative sequence | 251 – 304 | 54 | KTLVS…PDAYQ → MLKQARRFSFRNVRSATQWR KVGSTRQGQISGAFLAERLD KHQDFLTRMQTRTK in isoform 2. | VSP_019904 | |||||
| Alternative sequence | 355 – 357 | 3 | DEK → MSW in isoform 3. | VSP_019905 | |||||
Sequences
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References
| [1] | "Identification of rat cyclic nucleotide phosphodiesterase 11A (PDE11A): comparison of rat and human PDE11A splicing variants." Yuasa K., Ohgaru T., Asahina M., Omori K. Eur. J. Biochem. 268:4440-4448(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, TISSUE SPECIFICITY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB059360 mRNA. Translation: BAB79627.1. AB059361 mRNA. Translation: BAB79628.1. AB059362 mRNA. Translation: BAB79629.1. |
| IPI | IPI00363646. IPI00515811. IPI00561502. |
| RefSeq | NP_001120952.1. NM_001127480.1. NP_001120953.1. NM_001127481.2. NP_543169.1. NM_080893.1. |
| UniGene | Rn.88630. |
3D structure databases | |
| ProteinModelPortal | Q8VID6. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | Q8VID6. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSRNOT00000008301; ENSRNOP00000008300; ENSRNOG00000024457. ENSRNOT00000050355; ENSRNOP00000051289; ENSRNOG00000024457. |
| GeneID | 140928. |
| KEGG | rno:140928. |
Organism-specific databases | |
| CTD | 50940. |
| RGD | 621793. Pde11a. |
Phylogenomic databases | |
| GeneTree | ENSGT00690000102141. |
| HOGENOM | HOG000007068. |
| HOVERGEN | HBG101207. |
| InParanoid | Q8VID6. |
| KO | K13298. |
Gene expression databases | |
| ArrayExpress | Q8VID6. |
| Genevestigator | Q8VID6. |
| GermOnline | ENSRNOG00000024457. Rattus norvegicus. |
Family and domain databases | |
| Gene3D | 1.10.1300.10. 1 hit. |
| InterPro | IPR003018. GAF. IPR003607. HD/PDEase_dom. IPR023088. PDEase. IPR002073. PDEase_catalytic_dom. IPR023174. PDEase_CS. [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 | |
| NextBio | 620787. |
Entry information
| Entry name | PDE11_RAT | ||||||||
| Accession | Primary (citable) accession number: Q8VID6 Secondary accession number(s): Q8VID7, Q8VID8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
