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Q9Z0X4 (PDE3A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. 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:
cGMP-inhibited 3',5'-cyclic phosphodiesterase A

EC=3.1.4.17
Alternative name(s):
Cyclic GMP-inhibited phosphodiesterase A
Short name=CGI-PDE A
Gene names
Name:Pde3a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1141 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Involved in oocyte maturation. Ref.1

Catalytic activity

Nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 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 cGMP By similarity.

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family. PDE3 subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=0.2 µM for cAMP Ref.1

Ontologies

Keywords
   Cellular componentMembrane
   DomainTransmembrane
Transmembrane helix
   LigandcAMP
cGMP
Metal-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcAMP catabolic process

Inferred from electronic annotation. Source: Ensembl

cAMP-mediated signaling

Inferred from electronic annotation. Source: Ensembl

cGMP-mediated signaling

Inferred from electronic annotation. Source: Ensembl

cellular response to cGMP

Inferred from electronic annotation. Source: Ensembl

cellular response to transforming growth factor beta stimulus

Inferred from electronic annotation. Source: Ensembl

diterpenoid metabolic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of vascular permeability

Inferred from electronic annotation. Source: Ensembl

oocyte maturation

Inferred from direct assay Ref.1. Source: MGI

positive regulation of oocyte development

Inferred from genetic interaction PubMed 19474061. Source: MGI

positive regulation of vascular permeability

Inferred from electronic annotation. Source: Ensembl

regulation of meiosis

Inferred from direct assay Ref.1. Source: MGI

response to cAMP

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from direct assay Ref.1. Source: MGI

   Cellular_componentcytosol

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_function3',5'-cyclic-AMP phosphodiesterase activity

Inferred from direct assay Ref.1. Source: MGI

cAMP binding

Inferred from electronic annotation. Source: Ensembl

cGMP-inhibited cyclic-nucleotide phosphodiesterase activity

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11411141cGMP-inhibited 3',5'-cyclic phosphodiesterase A
PRO_0000198800

Regions

Transmembrane62 – 8221Helical; Potential
Transmembrane127 – 14721Helical; Potential
Transmembrane157 – 17721Helical; Potential
Transmembrane182 – 20221Helical; Potential
Transmembrane207 – 22721Helical; Potential
Transmembrane229 – 24921Helical; Potential
Region728 – 1086359Catalytic By similarity

Sites

Active site7521Proton donor By similarity
Metal binding7561Divalent metal cation 1 By similarity
Metal binding8361Divalent metal cation 1 By similarity
Metal binding8371Divalent metal cation 1 By similarity
Metal binding8371Divalent metal cation 2 By similarity
Metal binding9501Divalent metal cation 1 By similarity

Amino acid modifications

Modified residue3101Phosphoserine By similarity
Modified residue5201Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9Z0X4 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 3D9ACCFF928219D8

FASTA1,141124,513
        10         20         30         40         50         60 
MAVRGEAAQD LAKPGLGGAS PARVARGNHR HRGESSPSPR GSGCCWRALA LQPLRRSPQL 

        70         80         90        100        110        120 
SSALCAGSLS VLLALLVRLV GGEVGGELEK SQEAAAEEEE EEGARGGVFP GPRGGAPGGG 

       130        140        150        160        170        180 
AQLSPWLQPA ALLFSLLCAF FWMGLCLLRA GVRLPLAVAL LAACCAGEAL VQLSLGVGDG 

       190        200        210        220        230        240 
RLLSLPAAGV LLSCLGGATW LVLRLRLGVL MVAWTSVLRT VALVSLERFK VAWRPYLAYL 

       250        260        270        280        290        300 
AAVLGLLLAR YAEQILPQCS GPAPPRERFG SQLSARTKEE IPGWKRRRRS SSVVAGEMSG 

       310        320        330        340        350        360 
CSGKSHRRTS LPCIPREQLM GHSEWDHKRG PRGSQSGTSI TVDIAVMGEA HGLITDLLAD 

       370        380        390        400        410        420 
PSLPPNVCTS LRAVSNLLST QLTFQAIHKP RVNPTVTFSE NYTCSDSEEG LEKDKQAISK 

       430        440        450        460        470        480 
RLRRSLPPGL LRRVSSTWTT TTSATGLPTL EPAPVRRDRS ASIKPHEAPS PSAVNPDSWN 

       490        500        510        520        530        540 
APGLTTLTKS RSFTSSYAVS AANHVKAKKQ NRPGGLAKIS PVPSPSSSPP QGSPASSPVS 

       550        560        570        580        590        600 
NSASQQFPES PEVTIKRGPG SHRALTYTQS APDLSPQIPP PSVICSSCGR PYSQGNPADG 

       610        620        630        640        650        660 
PSERSGPAML KPNRTDDTSQ VTSDYETNNN SDSSDILQNE EEAECQREPQ RKASACGTYT 

       670        680        690        700        710        720 
SQTMIFLDKP ILAPEPLVMD NLDSIMDQLN TWNFPIFDLM ENIGRKCGRI LSQVSYRLFE 

       730        740        750        760        770        780 
DMGLFEAFKI PVREFMNYFH ALEIGYRDIP YHNRIHATDV LHAVWYLTTQ PIPGLPSVIG 

       790        800        810        820        830        840 
DHGSASDSDS DSGFTHGHMG YVFSKMYHVP DDKYGCLSGN IPALELMALY VAAAMHDYDH 

       850        860        870        880        890        900 
PGRTNAFLVA TSAPQAVLYN DRSVLENHHA AAAWNLFMSR PEYNFLVNLD HVEFKHFRFL 

       910        920        930        940        950        960 
VIEAILATDL KKHFDFVAKF NAKVNDDVGI DWTNENDRLL VCQMCIKLAD INGPAKCKEL 

       970        980        990       1000       1010       1020 
HLRWTEGIAS EFYEQGDEEA SLGLPISPFM DRSAPQLANL QESFISHIVG PLCHSYDSAG 

      1030       1040       1050       1060       1070       1080 
LMPGKWVDDS DDSGDTDDPE EEEEEAETPH EDEACESSIA PRKKSFKRRR IYCQITQHLL 

      1090       1100       1110       1120       1130       1140 
QNHMMWKKVI EEEQCLSGTE NQSLDQVPLQ HPSEQIQAIK EEEEEKGKPR AEETLAPQPD 


L 

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References

[1]"Cloning and characterization of the cyclic guanosine monophosphate-inhibited phosphodiesterase PDE3A expressed in mouse oocyte."
Shitsukawa K., Andersen C.B., Richard F.J., Horner A.K., Wiersma A., van Duin M., Conti M.
Biol. Reprod. 65:188-196(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: C57BL/6J.
Tissue: Ovary.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF099187 mRNA. Translation: AAD16300.1.
RefSeqNP_061249.1. NM_018779.1.
UniGeneMm.103728.
Mm.485878.

3D structure databases

ProteinModelPortalQ9Z0X4.
SMRQ9Z0X4. Positions 677-1087.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9Z0X4. 3 interactions.
MINTMINT-4049569.
STRING10090.ENSMUSP00000038749.

PTM databases

PhosphoSiteQ9Z0X4.

Proteomic databases

PaxDbQ9Z0X4.
PRIDEQ9Z0X4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000043259; ENSMUSP00000038749; ENSMUSG00000041741.
GeneID54611.
KEGGmmu:54611.
UCSCuc009eon.1. mouse.

Organism-specific databases

CTD5139.
MGIMGI:1860764. Pde3a.

Phylogenomic databases

eggNOGNOG145074.
GeneTreeENSGT00750000117528.
HOGENOMHOG000060144.
HOVERGENHBG053541.
InParanoidQ9Z0X4.
KOK13296.
OMAPETMMFL.
OrthoDBEOG7KDF95.
PhylomeDBQ9Z0X4.
TreeFamTF329631.

Gene expression databases

ArrayExpressQ9Z0X4.
BgeeQ9Z0X4.
CleanExMM_PDE3A.
GenevestigatorQ9Z0X4.

Family and domain databases

Gene3D1.10.1300.10. 2 hits.
InterProIPR003607. HD/PDEase_dom.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamPF00233. PDEase_I. 1 hit.
[Graphical view]
SMARTSM00471. HDc. 1 hit.
[Graphical view]
PROSITEPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio311416.
PROQ9Z0X4.
SOURCESearch...

Entry information

Entry namePDE3A_MOUSE
AccessionPrimary (citable) accession number: Q9Z0X4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 102 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

MGD cross-references

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