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Q62865 (PDE3A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1141 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

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.

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family. PDE3 subfamily.

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 direct assay PubMed 12181425PubMed 12834273PubMed 9648839PubMed 9884079. Source: RGD

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 expression pattern PubMed 9884079. Source: RGD

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 15867171. Source: RGD

negative regulation of vascular permeability

Inferred from electronic annotation. Source: Ensembl

oocyte maturation

Inferred from expression pattern PubMed 11673261. Source: RGD

positive regulation of oocyte development

Inferred from electronic annotation. Source: Ensembl

positive regulation of vascular permeability

Inferred from electronic annotation. Source: Ensembl

regulation of meiosis

Inferred from electronic annotation. Source: Ensembl

response to cAMP

Inferred from expression pattern PubMed 12181425. Source: RGD

response to drug

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytosol

Inferred from direct assay PubMed 11916944. Source: RGD

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_function3',5'-cyclic-AMP phosphodiesterase activity

Inferred from direct assay PubMed 12181425. Source: RGD

cAMP binding

Inferred from direct assay PubMed 9648839PubMed 9884079. Source: RGD

cGMP-inhibited cyclic-nucleotide phosphodiesterase activity

Inferred from direct assay PubMed 12834273PubMed 9648839PubMed 9884079. Source: RGD

cyclic-nucleotide phosphodiesterase activity

Traceable author statement PubMed 11673261. Source: RGD

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_0000198801

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
Q62865 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: A333DFB44F6F33F3

FASTA1,141124,301
        10         20         30         40         50         60 
MAVRGEAAQD WAKPGLRGPS PAPVARGDHR CRGGSPSSPR GSGCCWRALA LQPLRRSPQL 

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

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

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

       250        260        270        280        290        300 
AAVLGLLLAR YAEQLLPQCS GPAPPRERFG SQSSARTKEE IPGWKRRRRS SSVVAGEMSG 

       310        320        330        340        350        360 
CGGKSHRRTS LPCIPREQLM GHSEWDHKRG SRGSQSGTSV TVDIAVMGEA HGLITDLLAD 

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

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

       490        500        510        520        530        540 
APVLMTLTKS RSFTSSYAVS AANHVKAKKQ NRPGGLDKIS PVPSPSSSPP QGSPTSSPVS 

       550        560        570        580        590        600 
GIASVQFPES PEVTTKRGPG SHRALTYTQS APDLSPQIPP SPVICSSCGR PYSQGNPADG 

       610        620        630        640        650        660 
PSERSGPAMQ KPNRTDDTSQ VTSDYETNNN SDSSDILQND EEAECQREPL RKASACGTYT 

       670        680        690        700        710        720 
PQTMIFLDKP ILAPEPLVMD NLDSIMDQLN TWNFPIFDLV ENIGRKCGRI LSQVSYRLFE 

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

       790        800        810        820        830        840 
DHGSASDSDS DSGFTHGHMG YVFSKAYHVP 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 INGPAKCKDL 

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

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

      1090       1100       1110       1120       1130       1140 
QNHMMWKKVI EEEQCLSGTE NQAPDQAPLQ HSSEQIQAIK EEEEEKGKPR AEETLAPQPD 


L 

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References

[1]"Expression and characterization of deletion recombinants of two cGMP-inhibited cyclic nucleotide phosphodiesterases (PDE-3)."
He R., Komas N., Ekholm D., Murata T., Taira M., Hockman S.C., Degerman E., Manganiello V.C.
Cell Biochem. Biophys. 29:89-111(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Adipose tissue.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U38179 mRNA. Translation: AAA84964.1.
RefSeqNP_059033.1. NM_017337.1.
UniGeneRn.44403.

3D structure databases

ProteinModelPortalQ62865.
SMRQ62865. Positions 677-1087.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000032282.

Chemistry

BindingDBQ62865.

Proteomic databases

PRIDEQ62865.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000032843; ENSRNOP00000032282; ENSRNOG00000025042.
GeneID50678.
KEGGrno:50678.
UCSCRGD:61942. rat.

Organism-specific databases

CTD5139.
RGD61942. Pde3a.

Phylogenomic databases

eggNOGNOG145074.
GeneTreeENSGT00750000117528.
HOGENOMHOG000060144.
HOVERGENHBG053541.
InParanoidQ62865.
KOK13296.
OMAPETMMFL.
OrthoDBEOG7KDF95.
PhylomeDBQ62865.
TreeFamTF329631.

Gene expression databases

GenevestigatorQ62865.

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

NextBio610514.
PROQ62865.

Entry information

Entry namePDE3A_RAT
AccessionPrimary (citable) accession number: Q62865
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 99 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