Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

cGMP-inhibited 3',5'-cyclic phosphodiesterase B

Gene

Pde3b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

a divalent metal cationBy similarityNote: 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 regulationi

Inhibited by cGMP.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei713Proton donorBy similarity1
Metal bindingi717Divalent metal cation 1By similarity1
Metal bindingi797Divalent metal cation 1By similarity1
Metal bindingi798Divalent metal cation 1By similarity1
Metal bindingi798Divalent metal cation 2By similarity1
Metal bindingi913Divalent metal cation 1By similarity1

GO - Molecular functioni

GO - Biological processi

  • angiogenesis Source: UniProtKB-KW
  • cellular response to insulin stimulus Source: BHF-UCL
  • endocrine pancreas development Source: MGI
  • glucose homeostasis Source: MGI
  • negative regulation of angiogenesis Source: UniProtKB
  • negative regulation of cell adhesion Source: MGI
  • negative regulation of lipid catabolic process Source: MGI
  • regulation of insulin secretion Source: MGI
  • signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Angiogenesis

Keywords - Ligandi

cAMP, cGMP, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-165160. PDE3B signalling.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Pde3b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1333863. Pde3b.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei69 – 89HelicalSequence analysisAdd BLAST21
Transmembranei110 – 130HelicalSequence analysisAdd BLAST21
Transmembranei140 – 160HelicalSequence analysisAdd BLAST21
Transmembranei170 – 190HelicalSequence analysisAdd BLAST21
Transmembranei198 – 218HelicalSequence analysisAdd BLAST21
Transmembranei225 – 245HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

  • cytosol Source: Reactome
  • endoplasmic reticulum Source: BHF-UCL
  • Golgi apparatus Source: BHF-UCL
  • guanyl-nucleotide exchange factor complex Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001988031 – 1100cGMP-inhibited 3',5'-cyclic phosphodiesterase BAdd BLAST1100

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei15PhosphoserineCombined sources1
Modified residuei273Phosphoserine; by PKB/AKT1 or PKB/AKT2Combined sources1 Publication1
Modified residuei274PhosphoserineCombined sources1
Modified residuei421PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ61409.
MaxQBiQ61409.
PaxDbiQ61409.
PRIDEiQ61409.

PTM databases

iPTMnetiQ61409.
PhosphoSitePlusiQ61409.

Expressioni

Tissue specificityi

Abundant in adipose tissues.

Gene expression databases

CleanExiMM_PDE3B.

Interactioni

Subunit structurei

Interacts with PIK3CG. Interacts with RAPGEF3 and PIK3R6 (By similarity).By similarity

GO - Molecular functioni

  • protein kinase B binding Source: BHF-UCL

Protein-protein interaction databases

MINTiMINT-4997265.
STRINGi10090.ENSMUSP00000032909.

Structurei

3D structure databases

ProteinModelPortaliQ61409.
SMRiQ61409.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 28Interaction with RAPGEF3By similarityAdd BLAST28
Regioni415 – 439Interaction with PIK3R6By similarityAdd BLAST25
Regioni689 – 1054CatalyticBy similarityAdd BLAST366

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1044 – 1079Sequence analysisAdd BLAST36

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IEGG. Eukaryota.
ENOG410XT2V. LUCA.
HOGENOMiHOG000060144.
HOVERGENiHBG053541.
InParanoidiQ61409.
KOiK13296.
PhylomeDBiQ61409.

Family and domain databases

Gene3Di1.10.1300.10. 2 hits.
InterProiIPR003607. HD/PDEase_dom.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamiPF00233. PDEase_I. 1 hit.
[Graphical view]
SMARTiSM00471. HDc. 1 hit.
[Graphical view]
PROSITEiPS00126. PDEASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q61409-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKDERERDA PAMRSPPPPP ASAASPPESL RNGYVKSCVS PLRQDPPRSF
60 70 80 90 100
FFHLCRFCNV EPPAASLRAG ARLSLGVLAA FVLAALLGAR PERWAAAAAG
110 120 130 140 150
LRTLLSACSL SLSPLFSIAC AFFFLTCFLT RAQRGPGRGA GSWWLLALPA
160 170 180 190 200
CCYLGDFAAW QWWSWLRGEP AAAGRLCLVL SCVGLLTLAP RVRLRHGVLV
210 220 230 240 250
LLFAGLVWWV SFSGLGALPP ALRPLLSCLV GGAGCLLALG LDHFFHVRGA
260 270 280 290 300
SPPPRSASTA EEKVPVIRPR RRSSCVSLGE SAAGYYGSGK MFRRPSLPCI
310 320 330 340 350
SREQMILWDW DLKQWCKPHY QNSGGGNGVD LSVLNEARNM VSDLLIDPSL
360 370 380 390 400
PPQVISSLRS ISSLMGAFSG SCRPKINSFT PFPGFYPCSE VEDPVEKGDR
410 420 430 440 450
KLHKGLSGRT SFPTPQLRRS SGASSLLTNE HCSRWDRSSG KRSYQELSVS
460 470 480 490 500
SHGCHLNGPF SSNLFTIPKQ RSSSVSLTHH AGLRRAGALP SHSLLNSSSH
510 520 530 540 550
VPVSAGSLTN RSPIGFPDTT DFLTKPNIIL HRSLGSVSSA ADFHQYLRNS
560 570 580 590 600
DSNLCSSCGH QILKYVSTCE PDGTDHPSEK SGEEDSSVFS KEPLNIVETQ
610 620 630 640 650
EEETMKKACR ELFLEGDSHL MEEAQQPNID QEVSLDPMLV EDYDSLIEKM
660 670 680 690 700
NNWNFQIFEL VEKMGEKSGR ILSQVMYTLF QDTGLLETFK IPTQEFMNYF
710 720 730 740 750
RALENGYRDI PYHNRVHATD VLHAVWYLTT RPIPGLPQIH NNHETETKAD
760 770 780 790 800
SDGRLGSGQI AYISSKSCCI PDMSYGCLSS NIPALELMAL YVAAAMHDYD
810 820 830 840 850
HPGRTNAFLV ATNAPQAVLY NDRSVLENHH AASAWNLYLS RPEYNFLLNL
860 870 880 890 900
DHMEFKRFRF LVIEAILATD LKKHFDFLAE FNAKANDVNS NGIEWSSEND
910 920 930 940 950
RLLVCQVCIK LADINGPAKD RDLHLRWTEG IVNEFYEQGD EEAALGLPIS
960 970 980 990 1000
PFMDRSSPQL AKLQESFITH IVGPLCNSYD AAGLLPGQWI ETEEGDDTES
1010 1020 1030 1040 1050
DDDDDDDDGD GGEELDSDDE ETEDNLNPKP QRRKGRRRIF CQLMHHLTEN
1060 1070 1080 1090 1100
HKIWKEIIEE EEEKCKAEGN KLQVDNASLP QADEIQVIEE ADEEEEQMFE
Length:1,100
Mass (Da):122,154
Last modified:January 9, 2007 - v2
Checksum:i92E36B28D4A5FDF1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti10A → T in CAA10639 (PubMed:10454575).Curated1
Sequence conflicti261E → D in CAA10639 (PubMed:10454575).Curated1
Sequence conflicti288 – 290SGK → IPE in CAA64775 (PubMed:8921398).Curated3
Sequence conflicti439S → G in CAA10639 (PubMed:10454575).Curated1
Sequence conflicti444Y → H in CAA10639 (PubMed:10454575).Curated1
Sequence conflicti465F → M in CAA10639 (PubMed:10454575).Curated1
Sequence conflicti756G → S in CAA10639 (PubMed:10454575).Curated1
Sequence conflicti944A → T in CAA10639 (PubMed:10454575).Curated1
Sequence conflicti944A → T in CAA64775 (PubMed:8921398).Curated1
Sequence conflicti1082A → T in CAA64775 (PubMed:8921398).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ132271 mRNA. Translation: CAA10639.1.
AF547435 mRNA. Translation: AAN52086.1.
X95521 mRNA. Translation: CAA64775.1.
RefSeqiNP_035185.2. NM_011055.2.
UniGeneiMm.430730.

Genome annotation databases

GeneIDi18576.
KEGGimmu:18576.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ132271 mRNA. Translation: CAA10639.1.
AF547435 mRNA. Translation: AAN52086.1.
X95521 mRNA. Translation: CAA64775.1.
RefSeqiNP_035185.2. NM_011055.2.
UniGeneiMm.430730.

3D structure databases

ProteinModelPortaliQ61409.
SMRiQ61409.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4997265.
STRINGi10090.ENSMUSP00000032909.

PTM databases

iPTMnetiQ61409.
PhosphoSitePlusiQ61409.

Proteomic databases

EPDiQ61409.
MaxQBiQ61409.
PaxDbiQ61409.
PRIDEiQ61409.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi18576.
KEGGimmu:18576.

Organism-specific databases

CTDi5140.
MGIiMGI:1333863. Pde3b.

Phylogenomic databases

eggNOGiENOG410IEGG. Eukaryota.
ENOG410XT2V. LUCA.
HOGENOMiHOG000060144.
HOVERGENiHBG053541.
InParanoidiQ61409.
KOiK13296.
PhylomeDBiQ61409.

Enzyme and pathway databases

ReactomeiR-MMU-165160. PDE3B signalling.

Miscellaneous databases

ChiTaRSiPde3b. mouse.
PROiQ61409.
SOURCEiSearch...

Gene expression databases

CleanExiMM_PDE3B.

Family and domain databases

Gene3Di1.10.1300.10. 2 hits.
InterProiIPR003607. HD/PDEase_dom.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamiPF00233. PDEase_I. 1 hit.
[Graphical view]
SMARTiSM00471. HDc. 1 hit.
[Graphical view]
PROSITEiPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPDE3B_MOUSE
AccessioniPrimary (citable) accession number: Q61409
Secondary accession number(s): Q8CIX5, Q9Z1J9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 9, 2007
Last modified: November 2, 2016
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.