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Q61409 (PDE3B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 105. 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 B

EC=3.1.4.17
Alternative name(s):
CGIPDE1
Cyclic GMP-inhibited phosphodiesterase B
Short name=CGI-PDE B
Gene names
Name:Pde3b
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1100 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. May play a role in fat metabolism. Regulates cAMP binding of RAPGEF3. Through simultaneous binding to RAPGEF3 and PIK3R6 assembles a signaling complex in which the PI3K gamma complex is activated by RAPGEF3 and which is involved in angiogenesis 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.

Subunit structure

Interacts with PIK3CG. Interacts with RAPGEF3 and PIK3R6 By similarity. Ref.4

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Tissue specificity

Abundant in adipose tissues.

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family. PDE3 subfamily.

Ontologies

Keywords
   Biological processAngiogenesis
   Cellular componentMembrane
   DomainCoiled coil
Transmembrane
Transmembrane helix
   LigandcAMP
cGMP
Metal-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to insulin stimulus

Inferred from expression pattern Ref.1. Source: BHF-UCL

endocrine pancreas development

Inferred from direct assay PubMed 14736883. Source: MGI

glucose homeostasis

Inferred from direct assay PubMed 14736883. Source: MGI

negative regulation of angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of insulin secretion

Inferred from direct assay PubMed 14736883. Source: MGI

signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 10952971. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

endoplasmic reticulum

Inferred from direct assay PubMed 10952971. Source: BHF-UCL

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Inferred from direct assay PubMed 10952971. Source: BHF-UCL

   Molecular_function3',5'-cyclic-nucleotide phosphodiesterase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein kinase B binding

Inferred from physical interaction Ref.1. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11001100cGMP-inhibited 3',5'-cyclic phosphodiesterase B
PRO_0000198803

Regions

Transmembrane69 – 8921Helical; Potential
Transmembrane110 – 13021Helical; Potential
Transmembrane140 – 16021Helical; Potential
Transmembrane170 – 19021Helical; Potential
Transmembrane198 – 21821Helical; Potential
Transmembrane225 – 24521Helical; Potential
Region1 – 2828Interaction with RAPGEF3 By similarity
Region415 – 43925Interaction with PIK3R6 By similarity
Region689 – 1054366Catalytic By similarity
Coiled coil1044 – 107936 Potential

Sites

Active site7131Proton donor By similarity
Metal binding7171Divalent metal cation 1 By similarity
Metal binding7971Divalent metal cation 1 By similarity
Metal binding7981Divalent metal cation 1 By similarity
Metal binding7981Divalent metal cation 2 By similarity
Metal binding9131Divalent metal cation 1 By similarity

Amino acid modifications

Modified residue2731Phosphoserine; by PKB/AKT1 or PKB/AKT2 Ref.1
Modified residue4211Phosphoserine By similarity

Experimental info

Sequence conflict101A → T in CAA10639. Ref.1
Sequence conflict2611E → D in CAA10639. Ref.1
Sequence conflict288 – 2903SGK → IPE in CAA64775. Ref.3
Sequence conflict4391S → G in CAA10639. Ref.1
Sequence conflict4441Y → H in CAA10639. Ref.1
Sequence conflict4651F → M in CAA10639. Ref.1
Sequence conflict7561G → S in CAA10639. Ref.1
Sequence conflict9441A → T in CAA10639. Ref.1
Sequence conflict9441A → T in CAA64775. Ref.3
Sequence conflict10821A → T in CAA64775. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q61409 [UniParc].

Last modified January 9, 2007. Version 2.
Checksum: 92E36B28D4A5FDF1

FASTA1,100122,154
        10         20         30         40         50         60 
MRKDERERDA PAMRSPPPPP ASAASPPESL RNGYVKSCVS PLRQDPPRSF FFHLCRFCNV 

        70         80         90        100        110        120 
EPPAASLRAG ARLSLGVLAA FVLAALLGAR PERWAAAAAG LRTLLSACSL SLSPLFSIAC 

       130        140        150        160        170        180 
AFFFLTCFLT RAQRGPGRGA GSWWLLALPA CCYLGDFAAW QWWSWLRGEP AAAGRLCLVL 

       190        200        210        220        230        240 
SCVGLLTLAP RVRLRHGVLV LLFAGLVWWV SFSGLGALPP ALRPLLSCLV GGAGCLLALG 

       250        260        270        280        290        300 
LDHFFHVRGA SPPPRSASTA EEKVPVIRPR RRSSCVSLGE SAAGYYGSGK MFRRPSLPCI 

       310        320        330        340        350        360 
SREQMILWDW DLKQWCKPHY QNSGGGNGVD LSVLNEARNM VSDLLIDPSL PPQVISSLRS 

       370        380        390        400        410        420 
ISSLMGAFSG SCRPKINSFT PFPGFYPCSE VEDPVEKGDR KLHKGLSGRT SFPTPQLRRS 

       430        440        450        460        470        480 
SGASSLLTNE HCSRWDRSSG KRSYQELSVS SHGCHLNGPF SSNLFTIPKQ RSSSVSLTHH 

       490        500        510        520        530        540 
AGLRRAGALP SHSLLNSSSH VPVSAGSLTN RSPIGFPDTT DFLTKPNIIL HRSLGSVSSA 

       550        560        570        580        590        600 
ADFHQYLRNS DSNLCSSCGH QILKYVSTCE PDGTDHPSEK SGEEDSSVFS KEPLNIVETQ 

       610        620        630        640        650        660 
EEETMKKACR ELFLEGDSHL MEEAQQPNID QEVSLDPMLV EDYDSLIEKM NNWNFQIFEL 

       670        680        690        700        710        720 
VEKMGEKSGR ILSQVMYTLF QDTGLLETFK IPTQEFMNYF RALENGYRDI PYHNRVHATD 

       730        740        750        760        770        780 
VLHAVWYLTT RPIPGLPQIH NNHETETKAD SDGRLGSGQI AYISSKSCCI PDMSYGCLSS 

       790        800        810        820        830        840 
NIPALELMAL YVAAAMHDYD HPGRTNAFLV ATNAPQAVLY NDRSVLENHH AASAWNLYLS 

       850        860        870        880        890        900 
RPEYNFLLNL DHMEFKRFRF LVIEAILATD LKKHFDFLAE FNAKANDVNS NGIEWSSEND 

       910        920        930        940        950        960 
RLLVCQVCIK LADINGPAKD RDLHLRWTEG IVNEFYEQGD EEAALGLPIS PFMDRSSPQL 

       970        980        990       1000       1010       1020 
AKLQESFITH IVGPLCNSYD AAGLLPGQWI ETEEGDDTES DDDDDDDDGD GGEELDSDDE 

      1030       1040       1050       1060       1070       1080 
ETEDNLNPKP QRRKGRRRIF CQLMHHLTEN HKIWKEIIEE EEEKCKAEGN KLQVDNASLP 

      1090       1100 
QADEIQVIEE ADEEEEQMFE 

« Hide

References

[1]"Insulin-induced phosphorylation and activation of cyclic nucleotide phosphodiesterase 3B by the serine-threonine kinase Akt."
Kitamura T., Kitamura Y., Kuroda S., Hino Y., Ando M., Kotani K., Konishi H., Matsuzaki H., Kikkawa U., Ogawa W., Kasuga M.
Mol. Cell. Biol. 19:6286-6296(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT SER-273.
[2]"Importance of cAMP-response element-binding protein in regulation of expression of the murine cyclic nucleotide phosphodiesterase 3B (Pde3b) gene in differentiating 3T3-L1 preadipocytes."
Liu H., Tang J.R., Choi Y.H., Napolitano M., Hockman S., Taira M., Degerman E., Manganiello V.C.
J. Biol. Chem. 281:21096-21113(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: J125.
[3]"Molecular cloning and chromosomal assignment of the human homologue of the rat cGMP-inhibited phosphodiesterase 1 (PDE3A) -- a gene involved in fat metabolism located at 11p15.1."
Loebbert R.W., Winterpacht A., Seipel B., Zabel B.U.
Genomics 37:211-218(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 287-1085.
Strain: Swiss.
Tissue: Adipose tissue.
[4]"PI3Kgamma modulates the cardiac response to chronic pressure overload by distinct kinase-dependent and -independent effects."
Patrucco E., Notte A., Barberis L., Selvetella G., Maffei A., Brancaccio M., Marengo S., Russo G., Azzolino O., Rybalkin S.D., Silengo L., Altruda F., Wetzker R., Wymann M.P., Lembo G., Hirsch E.
Cell 118:375-387(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PIK3CG.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ132271 mRNA. Translation: CAA10639.1.
AF547435 mRNA. Translation: AAN52086.1.
X95521 mRNA. Translation: CAA64775.1.
RefSeqNP_035185.2. NM_011055.2.
UniGeneMm.430730.

3D structure databases

ProteinModelPortalQ61409.
SMRQ61409. Positions 632-1055.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4997265.

Proteomic databases

PaxDbQ61409.
PRIDEQ61409.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID18576.
KEGGmmu:18576.

Organism-specific databases

CTD5140.
MGIMGI:1333863. Pde3b.

Phylogenomic databases

eggNOGNOG145074.
HOGENOMHOG000060144.
HOVERGENHBG053541.
InParanoidQ61409.
KOK13296.
PhylomeDBQ61409.

Enzyme and pathway databases

ReactomeREACT_188257. Signal Transduction.

Gene expression databases

CleanExMM_PDE3B.
GenevestigatorQ61409.

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

ChiTaRSPDE3B. mouse.
NextBio294434.
PROQ61409.
SOURCESearch...

Entry information

Entry namePDE3B_MOUSE
AccessionPrimary (citable) accession number: Q61409
Secondary accession number(s): Q8CIX5, Q9Z1J9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 9, 2007
Last modified: May 14, 2014
This is version 105 of the entry and version 2 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