Reviewed,
UniProtKB/Swiss-Prot P70453 (PDE7A_MOUSE)
Last modified
October 13, 2009.
Version 77.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A EC=3.1.4.17 Alternative name(s): P2A | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 456 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase is highly specific for cAMP and may have a role in muscle signal transduction. |
| Catalytic activity | Adenosine 3',5'-cyclic phosphate + H2O = adenosine 5'-phosphate. |
| Cofactor | Divalent cations. |
| Enzyme regulation | Insensitive to all selective PDE inhibitors. |
| Pathway | Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1. |
| Subunit structure | Interacts with CBFA2T3 By similarity. |
| Tissue specificity | Widely expressed with highest levels in the skeletal muscle. |
| Domain | Composed of a C-terminal catalytic domain containing two putative divalent metal sites and an N-terminal regulatory domain. |
| Sequence similarities | Belongs to the cyclic nucleotide phosphodiesterase family. |
Ontologies
| Keywords | |
|---|---|
| Coding sequence diversity | Alternative splicing |
| Ligand | cAMP |
| Molecular function | Hydrolase |
| Gene Ontology (GO) | |
| Biological process | signal transduction Inferred from electronic annotation. Source: InterPro |
| Molecular function | 3',5'-cyclic-nucleotide phosphodiesterase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] Note: Additional isoforms seem to exist. | ||||||
| Isoform 1 (identifier: P70453-1) Also known as: PDE7A2; 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: P70453-2) Also known as: PDE7A1; The sequence of this isoform differs from the canonical sequence as follows: 1-20: MGITLIWCLALVLIKWITSK → MEVCYQLPVLPLDRPVPQHVLSRRGAISFSSSSALFGCPHPRQLSQ |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 456 | 456 | High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A | PRO_0000198834 | |||||
Regions | |||||||||
| Region | 161 – 425 | 265 | Catalytic By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 20 | 20 | MGITL…WITSK → MEVCYQLPVLPLDRPVPQHV LSRRGAISFSSSSALFGCPH PRQLSQ in isoform 2. | VSP_004594 | |||||
Experimental info | |||||||||
| Sequence conflict | 407 | 1 | A → D in AAG16295. Ref.2 | ||||||
Sequences
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References
| [1] | "Identification and tissue-specific expression of PDE7 phosphodiesterase splice variants." Bloom T.J., Beavo J.A. Proc. Natl. Acad. Sci. U.S.A. 93:14188-14192(1996) [PubMed: 8943082] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Skeletal muscle. |
| [2] | "Cloning, characterization, and tissue distribution of mouse phosphodiesterase 7A1." Wang P., Wu P., Egan R.W., Billah M.M. Biochem. Biophys. Res. Commun. 276:1271-1277(2000) [PubMed: 11027622] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Brain and Testis. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| U68171 mRNA. Translation: AAB08479.1. AY007702 mRNA. Translation: AAG16295.1. | |
| IPI | IPI00230552. IPI00762046. |
| RefSeq | NP_001116231.1. |
| UniGene | Mm.355614 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1OYN based on UniProtKB Q08499. |
| SMR | P70453. Positions 113-429. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P70453. |
PTM databases | |
| PhosphoSite | P70453. |
Proteomic databases | |
| PRIDE | P70453. |
Genome annotation databases | |
| Ensembl | ENSMUST00000091314; ENSMUSP00000088863; ENSMUSG00000069094; Mus musculus. [Genome view] ENSMUST00000099195; ENSMUSP00000096800; ENSMUSG00000069094; Mus musculus. [Genome view] |
| GeneID | 18583. |
| KEGG | mmu:18583. |
| UCSC | uc008ort.1. mouse. |
Organism-specific databases | |
| MGI | MGI:1202402. Pde7a. |
Phylogenomic databases | |
| HOVERGEN | P70453. |
Enzyme and pathway databases | |
| BRENDA | 3.1.4.17. 244. |
Gene expression databases | |
| ArrayExpress | P70453. |
| Bgee | P70453. |
| CleanEx | MM_PDE7A. |
| Genevestigator | P70453. |
| GermOnline | ENSMUSG00000069094. Mus musculus. |
Family and domain databases | |
| InterPro | IPR003607. Met-dep_phosphohydro_HD. IPR002073. PDEase. [Graphical view] |
| Pfam | PF00233. PDEase_I. 1 hit. [Graphical view] |
| PRINTS | PR00387. PDIESTERASE1. |
| SMART | SM00471. HDc. 1 hit. [Graphical view] |
| PROSITE | PS00126. PDEASE_I. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| SOURCE | Search... |
Entry information
| Entry name | PDE7A_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P70453 Secondary accession number(s): Q9ERB3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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