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O08593 (PDE7A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A

EC=3.1.4.53
Alternative name(s):
Rolipram-insensitive phosphodiesterase type 7
Gene names
Name:Pde7a
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length426 AA.
Sequence statusFragment.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May have a role in muscle signal transduction By similarity.

Catalytic activity

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

Insensitive to all selective PDE inhibitors By similarity.

Pathway

Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1.

Subunit structure

Interacts with CBFA2T3 By similarity.

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. PDE7 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 426›426High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A
PRO_0000198835

Regions

Region131 – 395265Catalytic By similarity

Sites

Active site1561Proton donor By similarity
Metal binding1601Divalent metal cation 1 By similarity
Metal binding1961Divalent metal cation 1 By similarity
Metal binding1971Divalent metal cation 1 By similarity
Metal binding1971Divalent metal cation 2 By similarity
Metal binding3061Divalent metal cation 1 By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
O08593 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 129BDC01C9351D26

FASTA42649,274
        10         20         30         40         50         60 
DQTALYIRML GDVRVRSRAG FETERRGSHP YIDFRIFHAQ SEIEASVSAR NIRRLLSFQR 

        70         80         90        100        110        120 
YLRSSRFFRG ATVCRSLNIL DEDYNGQAKC MLEKVGNWNF DIFLFDRLTN GNSLVSLTFH 

       130        140        150        160        170        180 
LFSLHGLIEY FHLDMVKLRR FLVMIQEDYH SQNPYHNAVH AADVTQAMHC YLKEPKLANS 

       190        200        210        220        230        240 
VTPWDILLSL IAAATHDLDH PGVNQPFLIK TNHYLATLYK NTSVLENHHW RSAVGLLRES 

       250        260        270        280        290        300 
GLFSHLPLES RHEMEAQIGA LILATDISRQ NEYLSLFRSH LDKGDLHLDD GRHRHLVLQM 

       310        320        330        340        350        360 
ALKCADICNP CRNWELSKQW SEKVTEEFFH QGDIEKKYHL GVSPLCDRQT ESIANIQIGF 

       370        380        390        400        410        420 
MTYLQEPLFT EWARFSDTRL SQTMLGHVGL NKASWKGLQR QQPSSEDASA AFELNSQLLT 


QENRLS 

« Hide

References

[1]"Differential distribution of rat PDE-7 mRNA in embryonic and adult rat brain."
Hoffmann R., Abdel'Al S., Engels P.
Cell Biochem. Biophys. 28:103-113(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U77880 mRNA. Translation: AAB51234.1.
UniGeneRn.39142.

3D structure databases

ProteinModelPortalO08593.
SMRO08593. Positions 83-399.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000040981.

Chemistry

BindingDBO08593.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:68391. rat.

Organism-specific databases

RGD68391. Pde7a.

Phylogenomic databases

eggNOGNOG300643.
HOGENOMHOG000220881.
HOVERGENHBG053543.
InParanoidO08593.

Enzyme and pathway databases

UniPathwayUPA00762; UER00747.

Gene expression databases

GenevestigatorO08593.

Family and domain databases

Gene3D1.10.1300.10. 1 hit.
InterProIPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamPF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSPR00387. PDIESTERASE1.
SMARTSM00471. HDc. 1 hit.
[Graphical view]
PROSITEPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROO08593.

Entry information

Entry namePDE7A_RAT
AccessionPrimary (citable) accession number: O08593
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: April 16, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways