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Q9QXQ1 (PDE7B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
cAMP-specific 3',5'-cyclic phosphodiesterase 7B

EC=3.1.4.53
Gene names
Name:Pde7b
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length446 AA.
Sequence statusComplete.
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 be involved in the control of cAMP-mediated neural activity and cAMP metabolism in the brain.

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

Inhibited by dipyridamole, IBMX and SCH 51866. Insensitive to zaprinast, rolipram, and milrinone.

Pathway

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

Tissue specificity

Highly expressed in brain.

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.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 446446cAMP-specific 3',5'-cyclic phosphodiesterase 7B
PRO_0000198837

Regions

Region172 – 410239Catalytic By similarity

Sites

Active site1731Proton donor By similarity
Metal binding1771Divalent metal cation 1 By similarity
Metal binding2131Divalent metal cation 1 By similarity
Metal binding2141Divalent metal cation 1 By similarity
Metal binding2141Divalent metal cation 2 By similarity
Metal binding3231Divalent metal cation 1 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9QXQ1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 7C052664B693A5A8

FASTA44651,337
        10         20         30         40         50         60 
MSCLMVERCG EVLFESPEQS VKCVCMLGDV RLRGQTGVPA ERRGSYPFID FRLLNNTTHS 

        70         80         90        100        110        120 
GEIGTKKKVK RLLSFQRYFH ASRLLRGIIP QAPLHLLDED YLGQARHMLS KVGTWDFDIF 

       130        140        150        160        170        180 
LFDRLTNGNS LVTLLCHLFN SHGLIHHFKL DMVTLHRFLV MVQEDYHGHN PYHNAVHAAD 

       190        200        210        220        230        240 
VTQAMHCYLK EPKLASFLTP LDIMLGLLAA AAHDVDHPGV NQPFLIKTNH HLANLYQNMS 

       250        260        270        280        290        300 
VLENHHWRST IGMLRESRLL AHLPKEMTQD IEQQLGSLIL ATDINRQNEF LTRLKAHLHN 

       310        320        330        340        350        360 
KDLRLENVQD RHFMLQIALK CADICNPCRI WEMSKQWSER VCEEFYRQGD LEQKFELEIS 

       370        380        390        400        410        420 
PLCNQQKDSI PSIQIGFMTY IVEPLFREWA RFTGNSTLSE NMLSHLAHNK AQWKSLLSNQ 

       430        440 
HRRRGSGQDL AGPAPETLEQ TEGATP 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of PDE7B, a cAMP-specific phosphodiesterase."
Hetman J.M., Soderling S.H., Glavas N.A., Beavo J.A.
Proc. Natl. Acad. Sci. U.S.A. 97:472-476(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning and characterisation of the human and mouse PDE7B, a novel cAMP-specific nucleotide phosphodiesterase."
Gardner C.E., Robas N.M., Cawkill D., Fidock M.D.
Biochem. Biophys. Res. Commun. 272:186-192(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6J.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF190639 mRNA. Translation: AAF25195.1.
AJ251859 mRNA. Translation: CAB92530.1.
BC130267 mRNA. Translation: AAI30268.1.
RefSeqNP_038903.3. NM_013875.5.
UniGeneMm.425617.

3D structure databases

ProteinModelPortalQ9QXQ1.
SMRQ9QXQ1. Positions 100-416.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9QXQ1.

Proteomic databases

PaxDbQ9QXQ1.
PRIDEQ9QXQ1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020165; ENSMUSP00000020165; ENSMUSG00000019990.
GeneID29863.
KEGGmmu:29863.
UCSCuc007eoa.2. mouse.

Organism-specific databases

CTD27115.
MGIMGI:1352752. Pde7b.

Phylogenomic databases

eggNOGNOG300643.
GeneTreeENSGT00730000110321.
HOGENOMHOG000220881.
HOVERGENHBG053543.
InParanoidA1L3T2.
KOK01120.
OrthoDBEOG7M98G3.
PhylomeDBQ9QXQ1.
TreeFamTF314638.

Enzyme and pathway databases

UniPathwayUPA00762; UER00747.

Gene expression databases

ArrayExpressQ9QXQ1.
BgeeQ9QXQ1.
CleanExMM_PDE7B.
GenevestigatorQ9QXQ1.

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

NextBio307074.
PROQ9QXQ1.
SOURCESearch...

Entry information

Entry namePDE7B_MOUSE
AccessionPrimary (citable) accession number: Q9QXQ1
Secondary accession number(s): A1L3T2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 105 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot