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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 protein 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.

Pathwayi: 3',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), High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A (Pde7a), cAMP-specific 3',5'-cyclic phosphodiesterase 4D (Pde4d), 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)DescriptionActionsGraphical viewLength
Active sitei173Proton donorBy similarity1
Metal bindingi177Divalent metal cation 1By similarity1
Metal bindingi213Divalent metal cation 1By similarity1
Metal bindingi214Divalent metal cation 1By similarity1
Metal bindingi214Divalent metal cation 2By similarity1
Metal bindingi323Divalent metal cation 1By similarity1

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.
ReactomeiR-MMU-418555. 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
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1352752. Pde7b.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001988371 – 446cAMP-specific 3',5'-cyclic phosphodiesterase 7BAdd BLAST446

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei426PhosphoserineCombined sources1
Modified residuei445PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9QXQ1.
PRIDEiQ9QXQ1.

PTM databases

iPTMnetiQ9QXQ1.
PhosphoSitePlusiQ9QXQ1.

Expressioni

Tissue specificityi

Highly expressed in brain.

Gene expression databases

BgeeiENSMUSG00000019990.
CleanExiMM_PDE7B.
ExpressionAtlasiQ9QXQ1. baseline and differential.
GenevisibleiQ9QXQ1. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000020165.

Structurei

3D structure databases

ProteinModelPortaliQ9QXQ1.
SMRiQ9QXQ1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni172 – 410CatalyticBy similarityAdd BLAST239

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3689. Eukaryota.
ENOG410XRI7. LUCA.
GeneTreeiENSGT00760000118889.
HOGENOMiHOG000220881.
HOVERGENiHBG053543.
InParanoidiQ9QXQ1.
KOiK18436.
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000020165.

PTM databases

iPTMnetiQ9QXQ1.
PhosphoSitePlusiQ9QXQ1.

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

eggNOGiKOG3689. Eukaryota.
ENOG410XRI7. LUCA.
GeneTreeiENSGT00760000118889.
HOGENOMiHOG000220881.
HOVERGENiHBG053543.
InParanoidiQ9QXQ1.
KOiK18436.
PhylomeDBiQ9QXQ1.
TreeFamiTF314638.

Enzyme and pathway databases

UniPathwayiUPA00762; UER00747.
BRENDAi3.1.4.53. 3474.
ReactomeiR-MMU-418555. G alpha (s) signalling events.

Miscellaneous databases

PROiQ9QXQ1.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000019990.
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...

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: November 2, 2016
This is version 119 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

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 one 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.