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Q63085 (PDE3B_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length1108 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. 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.

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
   DomainTransmembrane
Transmembrane helix
   LigandMetal-binding
cAMP
cGMP
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

cAMP catabolic process

Inferred from direct assay PubMed 12181425PubMed 9648839PubMed 9884079. Source: RGD

cellular response to insulin stimulus

Inferred from sequence or structural similarity. Source: BHF-UCL

diterpenoid metabolic process

Inferred from expression pattern PubMed 9884079. Source: RGD

negative regulation of angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of insulin secretion

Inferred from mutant phenotype PubMed 18706893. Source: RGD

signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_function3',5'-cyclic-AMP phosphodiesterase activity

Inferred from direct assay PubMed 12169692PubMed 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 9648839PubMed 9884079. Source: RGD

drug binding

Inferred from direct assay PubMed 18706893. Source: RGD

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoprotein binding

Inferred from direct assay PubMed 16225849. Source: RGD

protein kinase B binding

Inferred from sequence or structural similarity. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11081108cGMP-inhibited 3',5'-cyclic phosphodiesterase B
PRO_0000198804

Regions

Transmembrane73 – 9321Helical; Potential
Transmembrane114 – 13421Helical; Potential
Transmembrane144 – 16421Helical; Potential
Transmembrane175 – 19521Helical; Potential
Transmembrane204 – 22421Helical; Potential
Transmembrane231 – 25121Helical; Potential
Region1 – 3232Interaction with RAPGEF3 By similarity
Region421 – 44525Interaction with PIK3R6 By similarity
Region695 – 1063369Catalytic By similarity
Compositional bias16 – 227Poly-Pro
Compositional bias99 – 1024Poly-Ala
Compositional bias175 – 1795Poly-Ala
Compositional bias1007 – 102115Poly-Asp
Compositional bias1068 – 10714Poly-Glu
Compositional bias1101 – 11044Poly-Glu

Sites

Active site7191Proton donor By similarity
Metal binding7231Divalent metal cation 1 By similarity
Metal binding8031Divalent metal cation 1 By similarity
Metal binding8041Divalent metal cation 1 By similarity
Metal binding8041Divalent metal cation 2 By similarity
Metal binding9191Divalent metal cation 1 By similarity

Amino acid modifications

Modified residue2791Phosphoserine; by PKB/AKT1 or PKB/AKT2 By similarity
Modified residue4271Phosphoserine By similarity
Modified residue6101Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q63085 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: C9B5078C7D3ADD6D

FASTA1,108123,107
        10         20         30         40         50         60 
MRKDERERDT PAMRSPPPPP PPATATAASP PESLRNGYVK SCVSPLRQDP PRSFFFHLCR 

        70         80         90        100        110        120 
FCNVEPPAAS LRAGARLSLA ALAAFVLAAL LGAGPERWAA AATGLRTLLS ACSLSLSPLF 

       130        140        150        160        170        180 
SIACAFFFLT CFLTRAQRGP DRGAGSWWLL ALPACCYLGD FAAWQWWSWL RGEPAAAAAG 

       190        200        210        220        230        240 
RLCLVLSCVG LLTLAPRVRL RHGVLVLLFA GLVWWVSFSG LGALPPALRP LLSCLVGGAG 

       250        260        270        280        290        300 
CLLALGLDHF FHVRGASPPP RSASTADEKV PVIRPRRRSS CVSLGESAAG YYGSGKMFRR 

       310        320        330        340        350        360 
PSLPCISREQ MILWDWDLKQ WCKPHYQNSG GGNGVDLSVL NEARNMVSDL LIDPSLPPQV 

       370        380        390        400        410        420 
ISSLRSISSL MGAFSGSCRP KINSFTPFPG FYPCSEVEDP VEKGDRKLHK GLSSKPSFPT 

       430        440        450        460        470        480 
AQLRRSSGAS GLLTSEHHSR WDRSGGKRPY QELSVSSHGC HLNGPFSSNL MTIPKQRSSS 

       490        500        510        520        530        540 
VSLTHHAGLR RAGALPSPSL LNSSSHVPVS AGCLTNRSPV GFLDTSDFLT KPSVTLHRSL 

       550        560        570        580        590        600 
GSVSSAADFH QYLRNSDSSL CSSCGHQILK YVSTCEPDGT DHHNEKSGEE DSTVFSKERL 

       610        620        630        640        650        660 
NIVETQEEET VKEDCRELFL EGDDHLMEEA QQPNIDQEVL LDPMLVEDYD SLIEKMSNWN 

       670        680        690        700        710        720 
FQIFELVEKM GEKSGRILSQ VMYTLFQDTG LLETFKIPTQ EFMNYFRALE NGYRDIPYHN 

       730        740        750        760        770        780 
RVHATDVLHA VWYLTTRPIP GLQQLHNNHE TETKADSDAR LSSGQIAYLS SKSCCIPDKS 

       790        800        810        820        830        840 
YGCLSSNIPA LELMALYVAA AMHDYDHPGR TNAFLVATNA PQAVLYNDRS VLENHHAASA 

       850        860        870        880        890        900 
WNLYLSRPEY NFLLNLDHME FKRFRFLVIE AILATDLKKH FDFLAEFNAK ANDVNSNGIE 

       910        920        930        940        950        960 
WSSENDRLLV CQVCIKLADI NGPAKDRDLH LRWTEGIVNE FYEQGDEEAT LGLPISPFMD 

       970        980        990       1000       1010       1020 
RSSPQLAKLQ ESFITHIVGP LCNSYDAAGL LPGQWIEAEE GDDTESDDDD DDDDDDDDDD 

      1030       1040       1050       1060       1070       1080 
DEELDSDDEE TEDNLNPKPQ RRKGRRRIFC QLMHHLTENH KIWKEIIEEE EKCKAEGNKL 

      1090       1100 
QVDNASLPQA DEIQVIEEAD EEEEQMFE

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References

[1]"Molecular cloning of the rat adipocyte hormone-sensitive cyclic GMP-inhibited cyclic nucleotide phosphodiesterase."
Taira M., Hockman S.C., Calvo J.C., Taira M., Belfrage P., Manganiello V.C.
J. Biol. Chem. 268:18573-18579(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Adipose tissue.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z22867 mRNA. Translation: CAA80489.1.
IPIIPI00951591.
PIRA48508.
RefSeqNP_058925.1. NM_017229.1.
UniGeneRn.10322.

3D structure databases

ProteinModelPortalQ63085.
SMRQ63085. Positions 638-1064.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000015498.

PTM databases

PhosphoSiteQ63085.

Proteomic databases

PaxDbQ63085.
PRIDEQ63085.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID29516.
KEGGrno:29516.
UCSCRGD:61943. rat.

Organism-specific databases

CTD5140.
RGD61943. Pde3b.

Phylogenomic databases

eggNOGNOG145074.
HOGENOMHOG000060144.
HOVERGENHBG053541.
InParanoidQ63085.
KOK13296.
OrthoDBEOG4GB75F.

Gene expression databases

ArrayExpressQ63085.
GenevestigatorQ63085.

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

BindingDBQ63085.
ChEMBLCHEMBL3580.
NextBio609453.

Entry information

Entry namePDE3B_RAT
AccessionPrimary (citable) accession number: Q63085
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: May 1, 2013
This is version 93 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

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