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Protein

cAMP-specific 3',5'-cyclic phosphodiesterase 7B

Gene

Pde7b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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 activityi

Adenosine 3',5'-cyclic phosphate + H2O = adenosine 5'-phosphate.

Cofactori

a divalent metal cationBy similarityNote: 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 regulationi

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

Pathway:i3',5'-cyclic AMP degradation

This protein is involved in step 1 of the subpathway that synthesizes AMP from 3',5'-cyclic AMP.
Proteins known to be involved in this subpathway in this organism are:
  1. cAMP-specific 3',5'-cyclic phosphodiesterase 4A (Pde4a), High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B (Pde8b), cAMP-specific 3',5'-cyclic phosphodiesterase 4C (Pde4c), High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A (Pde8a), cAMP-specific 3',5'-cyclic phosphodiesterase 4D (Pde4d), High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A (Pde7a), cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A (Pde10a), cAMP-specific 3',5'-cyclic phosphodiesterase 7B (Pde7b)
This subpathway is part of the pathway 3',5'-cyclic AMP degradation, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes AMP from 3',5'-cyclic AMP, the pathway 3',5'-cyclic AMP degradation and in Purine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei173 – 1731Proton donorBy similarity
Metal bindingi177 – 1771Divalent metal cation 1By similarity
Metal bindingi213 – 2131Divalent metal cation 1By similarity
Metal bindingi214 – 2141Divalent metal cation 1By similarity
Metal bindingi214 – 2141Divalent metal cation 2By similarity
Metal bindingi323 – 3231Divalent metal cation 1By similarity

GO - Molecular functioni

  • 3',5'-cyclic-AMP phosphodiesterase activity Source: MGI
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

cAMP, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.4.53. 3474.
ReactomeiREACT_313192. G alpha (s) signalling events.
UniPathwayiUPA00762; UER00747.

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP-specific 3',5'-cyclic phosphodiesterase 7B (EC:3.1.4.53)
Gene namesi
Name:Pde7b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1352752. Pde7b.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 446446cAMP-specific 3',5'-cyclic phosphodiesterase 7BPRO_0000198837Add
BLAST

Proteomic databases

PaxDbiQ9QXQ1.
PRIDEiQ9QXQ1.

PTM databases

PhosphoSiteiQ9QXQ1.

Expressioni

Tissue specificityi

Highly expressed in brain.

Gene expression databases

BgeeiQ9QXQ1.
CleanExiMM_PDE7B.
ExpressionAtlasiQ9QXQ1. baseline and differential.
GenevisibleiQ9QXQ1. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000020165.

Structurei

3D structure databases

ProteinModelPortaliQ9QXQ1.
SMRiQ9QXQ1. Positions 100-416.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni172 – 410239CatalyticBy similarityAdd
BLAST

Domaini

Composed of a C-terminal catalytic domain containing two putative divalent metal sites and an N-terminal regulatory domain.

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG300643.
GeneTreeiENSGT00760000118889.
HOGENOMiHOG000220881.
HOVERGENiHBG053543.
InParanoidiQ9QXQ1.
KOiK18436.
OrthoDBiEOG7M98G3.
PhylomeDBiQ9QXQ1.
TreeFamiTF314638.

Family and domain databases

Gene3Di1.10.1300.10. 1 hit.
InterProiIPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamiPF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSiPR00387. PDIESTERASE1.
SMARTiSM00471. HDc. 1 hit.
[Graphical view]
PROSITEiPS00126. PDEASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9QXQ1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSCLMVERCG EVLFESPEQS VKCVCMLGDV RLRGQTGVPA ERRGSYPFID
60 70 80 90 100
FRLLNNTTHS GEIGTKKKVK RLLSFQRYFH ASRLLRGIIP QAPLHLLDED
110 120 130 140 150
YLGQARHMLS KVGTWDFDIF LFDRLTNGNS LVTLLCHLFN SHGLIHHFKL
160 170 180 190 200
DMVTLHRFLV MVQEDYHGHN PYHNAVHAAD VTQAMHCYLK EPKLASFLTP
210 220 230 240 250
LDIMLGLLAA AAHDVDHPGV NQPFLIKTNH HLANLYQNMS VLENHHWRST
260 270 280 290 300
IGMLRESRLL AHLPKEMTQD IEQQLGSLIL ATDINRQNEF LTRLKAHLHN
310 320 330 340 350
KDLRLENVQD RHFMLQIALK CADICNPCRI WEMSKQWSER VCEEFYRQGD
360 370 380 390 400
LEQKFELEIS PLCNQQKDSI PSIQIGFMTY IVEPLFREWA RFTGNSTLSE
410 420 430 440
NMLSHLAHNK AQWKSLLSNQ HRRRGSGQDL AGPAPETLEQ TEGATP
Length:446
Mass (Da):51,337
Last modified:May 1, 2000 - v1
Checksum:i7C052664B693A5A8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF190639 mRNA. Translation: AAF25195.1.
AJ251859 mRNA. Translation: CAB92530.1.
BC130267 mRNA. Translation: AAI30268.1.
CCDSiCCDS35859.1.
RefSeqiNP_038903.3. NM_013875.5.
UniGeneiMm.425617.

Genome annotation databases

EnsembliENSMUST00000020165; ENSMUSP00000020165; ENSMUSG00000019990.
GeneIDi29863.
KEGGimmu:29863.
UCSCiuc007eoa.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF190639 mRNA. Translation: AAF25195.1.
AJ251859 mRNA. Translation: CAB92530.1.
BC130267 mRNA. Translation: AAI30268.1.
CCDSiCCDS35859.1.
RefSeqiNP_038903.3. NM_013875.5.
UniGeneiMm.425617.

3D structure databases

ProteinModelPortaliQ9QXQ1.
SMRiQ9QXQ1. Positions 100-416.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000020165.

PTM databases

PhosphoSiteiQ9QXQ1.

Proteomic databases

PaxDbiQ9QXQ1.
PRIDEiQ9QXQ1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020165; ENSMUSP00000020165; ENSMUSG00000019990.
GeneIDi29863.
KEGGimmu:29863.
UCSCiuc007eoa.2. mouse.

Organism-specific databases

CTDi27115.
MGIiMGI:1352752. Pde7b.

Phylogenomic databases

eggNOGiNOG300643.
GeneTreeiENSGT00760000118889.
HOGENOMiHOG000220881.
HOVERGENiHBG053543.
InParanoidiQ9QXQ1.
KOiK18436.
OrthoDBiEOG7M98G3.
PhylomeDBiQ9QXQ1.
TreeFamiTF314638.

Enzyme and pathway databases

UniPathwayiUPA00762; UER00747.
BRENDAi3.1.4.53. 3474.
ReactomeiREACT_313192. G alpha (s) signalling events.

Miscellaneous databases

NextBioi307074.
PROiQ9QXQ1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QXQ1.
CleanExiMM_PDE7B.
ExpressionAtlasiQ9QXQ1. baseline and differential.
GenevisibleiQ9QXQ1. MM.

Family and domain databases

Gene3Di1.10.1300.10. 1 hit.
InterProiIPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamiPF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSiPR00387. PDIESTERASE1.
SMARTiSM00471. HDc. 1 hit.
[Graphical view]
PROSITEiPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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].

Entry informationi

Entry nameiPDE7B_MOUSE
AccessioniPrimary (citable) accession number: Q9QXQ1
Secondary accession number(s): A1L3T2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 2000
Last modified: June 24, 2015
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.