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O88502 (PDE8A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. 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:
High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A

Short name=MmPDE8
EC=3.1.4.53
Gene names
Name:Pde8a
Synonyms:Pde8
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length823 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in maintaining basal levels of the cyclic nucleotide and/or in the cAMP regulation of germ cell development 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

Inhibited by dipyridimole. Insensitive to selective PDE inhibitor rolipram and to the non-selective inhibitor, IBMX.

Pathway

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

Tissue specificity

Highest levels in testis > eye > liver > skeletal muscle > heart > 7-day embryo > kidney > ovary > brain. In the testis, expressed specifically in the seminiferous epithelium in a spatial and temporal manner.

Developmental stage

Levels of expression decrease sometime between embryo day 7 and day 11. In the testis, expression restricted to middle and late pachytene spermatocytes.

Domain

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

Post-translational modification

Phosphorylated at Ser-355 by PKA under elevated cAMP conditions, this enhances catalytic activity By similarity.

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family. PDE8 subfamily.

Contains 1 PAC (PAS-associated C-terminal) domain.

Contains 1 PAS (PER-ARNT-SIM) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 823823High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A
PRO_0000198839

Regions

Domain209 – 28072PAS
Domain283 – 32543PAC
Region526 – 807282Catalytic By similarity

Sites

Active site5511Proton donor By similarity
Metal binding5551Divalent metal cation 1 By similarity
Metal binding5911Divalent metal cation 1 By similarity
Metal binding5921Divalent metal cation 1 By similarity
Metal binding5921Divalent metal cation 2 By similarity
Metal binding7201Divalent metal cation 1 By similarity

Amino acid modifications

Modified residue3551Phosphoserine; by PKA By similarity
Modified residue4521Phosphoserine By similarity
Modified residue4561Phosphotyrosine Ref.3

Sequences

Sequence LengthMass (Da)Tools
O88502 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 7FD9BE4BAEB9BCF2

FASTA82393,171
        10         20         30         40         50         60 
MGCAPSIHTS ENRTFSHSDG EDEDVDVDVP GPAPRSIQRW STAPGLVEPQ PRDNGASKVS 

        70         80         90        100        110        120 
VADVQFGPMR FHQDQLQVLL VFTKEDSQCN GFHRACEKAG FKCTVTKEVQ TVLTCFQDKL 

       130        140        150        160        170        180 
HDIIIIDHRY PRQMDAETLC RSIRSSKFSE NTVIVGVVRR VDKEESSLMP FLAAGFTRRF 

       190        200        210        220        230        240 
IENPNVMACY NELLQLACGE VRSQLKLRAC NSVFTALEKS QEAIEITSED HIIQYANPAF 

       250        260        270        280        290        300 
ESTMGYQSGE LIGKELAQVP INEKKGDLLD AINSCVTVDK EWQGVYHTQK KNGDNIQQNV 

       310        320        330        340        350        360 
KIIPVIGQGG KIRHYVSIIR VCNGNNKVET TTECVQTDSQ TDNQAGKHKD RRKHSMDAKA 

       370        380        390        400        410        420 
VSSRTSDVSS QRRHSSLARI HSMMIEAPIT KVINIINAAQ ENSPVPVTEA LNRVLDILRT 

       430        440        450        460        470        480 
TELYSPQFNA QDDPHATDLV GGLMSDGLRR FSGNEYILAT KNLPPLSNNL ATPVSLHDVP 

       490        500        510        520        530        540 
PRIALAIENE EQWDFDIFEL EVATQNRPLI YLGLKTFARF GMCEFLQCSE TTLRSWFQMI 

       550        560        570        580        590        600 
ESNYHSSNPY HNSTHAADVL HATAYFLSRD KIKETLDRID EVAALIAATV HDVDHPGRTN 

       610        620        630        640        650        660 
SFLCNAGNQL AVLYNDTAVL ESHHVALAFQ LTLENDQCNI FKQMERNDYR TLRQSIIDMV 

       670        680        690        700        710        720 
LATEMTKHFE HVNKFINSIN KPLTAQESEE PDRSLEDIKA MLKTPESRAL IKRMMIKCAD 

       730        740        750        760        770        780 
VSNPCRPLEH CIEWAARISE EYFSQTDEEK QLDLPVVMPV FDRNTCSIPK SQISFIDYFI 

       790        800        810        820 
TDMFDAWDAF VDLPNLMQHL DDNFRYWKGL DEKKLRSLRP PPE 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of a cAMP-specific cyclic nucleotide phosphodiesterase."
Soderling S.H., Bayuga S.J., Beavo J.A.
Proc. Natl. Acad. Sci. U.S.A. 95:8991-8996(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[2]"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].
Tissue: Brain.
[3]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-456, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF067806 mRNA. Translation: AAC40194.1.
BC125578 mRNA. Translation: AAI25579.1.
BC132145 mRNA. Translation: AAI32146.1.
RefSeqNP_032829.1. NM_008803.2.
UniGeneMm.371577.

3D structure databases

ProteinModelPortalO88502.
SMRO88502. Positions 216-325, 425-813.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202082. 1 interaction.
MINTMINT-4996272.

PTM databases

PhosphoSiteO88502.

Proteomic databases

PaxDbO88502.
PRIDEO88502.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026672; ENSMUSP00000026672; ENSMUSG00000025584.
GeneID18584.
KEGGmmu:18584.
UCSCuc009ibt.1. mouse.

Organism-specific databases

CTD5151.
MGIMGI:1277116. Pde8a.

Phylogenomic databases

eggNOGNOG282089.
GeneTreeENSGT00730000110321.
HOVERGENHBG053544.
InParanoidQ059P6.
KOK01120.
OMAETTTECV.
OrthoDBEOG7X3QQM.
PhylomeDBO88502.
TreeFamTF314638.

Enzyme and pathway databases

UniPathwayUPA00762; UER00747.

Gene expression databases

BgeeO88502.
CleanExMM_PDE8A.
GenevestigatorO88502.

Family and domain databases

Gene3D1.10.1300.10. 1 hit.
InterProIPR003607. HD/PDEase_dom.
IPR000014. PAS.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamPF13426. PAS_9. 1 hit.
PF00233. PDEase_I. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PRINTSPR00387. PDIESTERASE1.
SMARTSM00471. HDc. 1 hit.
SM00091. PAS. 1 hit.
[Graphical view]
SUPFAMSSF55785. SSF55785. 1 hit.
TIGRFAMsTIGR00229. sensory_box. 1 hit.
PROSITEPS50112. PAS. 1 hit.
PS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio294456.
PROO88502.
SOURCESearch...

Entry information

Entry namePDE8A_MOUSE
AccessionPrimary (citable) accession number: O88502
Secondary accession number(s): Q059P6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 121 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