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cGMP-inhibited 3',5'-cyclic phosphodiesterase B (EC 3.1.4.17) (CGIPDE1) (Cyclic GMP-inhibited phosphodiesterase B) (CGI-PDE B)

 PDE3B_MOUSE             Reviewed;        1100 AA.
Q61409; Q8CIX5; Q9Z1J9;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
09-JAN-2007, sequence version 2.
25-OCT-2017, entry version 127.
RecName: Full=cGMP-inhibited 3',5'-cyclic phosphodiesterase B;
EC=3.1.4.17;
AltName: Full=CGIPDE1;
AltName: Full=Cyclic GMP-inhibited phosphodiesterase B;
Short=CGI-PDE B;
Name=Pde3b;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PHOSPHORYLATION AT SER-273.
PubMed=10454575; DOI=10.1128/MCB.19.9.6286;
Kitamura T., Kitamura Y., Kuroda S., Hino Y., Ando M., Kotani K.,
Konishi H., Matsuzaki H., Kikkawa U., Ogawa W., Kasuga M.;
"Insulin-induced phosphorylation and activation of cyclic nucleotide
phosphodiesterase 3B by the serine-threonine kinase Akt.";
Mol. Cell. Biol. 19:6286-6296(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=J125;
PubMed=16702214; DOI=10.1074/jbc.M601307200;
Liu H., Tang J.R., Choi Y.H., Napolitano M., Hockman S., Taira M.,
Degerman E., Manganiello V.C.;
"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.";
J. Biol. Chem. 281:21096-21113(2006).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 287-1085.
STRAIN=SWR/J; TISSUE=Adipose tissue;
PubMed=8921398; DOI=10.1006/geno.1996.0544;
Loebbert R.W., Winterpacht A., Seipel B., Zabel B.U.;
"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.";
Genomics 37:211-218(1996).
[4]
INTERACTION WITH PIK3CG.
PubMed=15294162; DOI=10.1016/j.cell.2004.07.017;
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.;
"PI3Kgamma modulates the cardiac response to chronic pressure overload
by distinct kinase-dependent and -independent effects.";
Cell 118:375-387(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-273 AND SER-274,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, and Liver;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: Nucleoside 3',5'-cyclic phosphate + H(2)O =
nucleoside 5'-phosphate.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000250};
Note=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. {ECO:0000250};
-!- ENZYME REGULATION: Inhibited by cGMP.
-!- SUBUNIT: Interacts with PIK3CG. Interacts with RAPGEF3 and PIK3R6
(By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Abundant in adipose tissues.
-!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
family. PDE3 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ132271; CAA10639.1; -; mRNA.
EMBL; AF547435; AAN52086.1; -; mRNA.
EMBL; X95521; CAA64775.1; -; mRNA.
RefSeq; NP_035185.2; NM_011055.2.
UniGene; Mm.430730; -.
ProteinModelPortal; Q61409; -.
SMR; Q61409; -.
MINT; MINT-4997265; -.
STRING; 10090.ENSMUSP00000032909; -.
iPTMnet; Q61409; -.
PhosphoSitePlus; Q61409; -.
EPD; Q61409; -.
MaxQB; Q61409; -.
PaxDb; Q61409; -.
PRIDE; Q61409; -.
GeneID; 18576; -.
KEGG; mmu:18576; -.
CTD; 5140; -.
MGI; MGI:1333863; Pde3b.
eggNOG; ENOG410IEGG; Eukaryota.
eggNOG; ENOG410XT2V; LUCA.
HOGENOM; HOG000060144; -.
HOVERGEN; HBG053541; -.
InParanoid; Q61409; -.
KO; K13296; -.
PhylomeDB; Q61409; -.
Reactome; R-MMU-165160; PDE3B signalling.
ChiTaRS; Pde3b; mouse.
PRO; PR:Q61409; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_PDE3B; -.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0005794; C:Golgi apparatus; IDA:BHF-UCL.
GO; GO:0032045; C:guanyl-nucleotide exchange factor complex; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:BHF-UCL.
GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0043422; F:protein kinase B binding; IPI:BHF-UCL.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0032869; P:cellular response to insulin stimulus; IEP:BHF-UCL.
GO; GO:0031018; P:endocrine pancreas development; IDA:MGI.
GO; GO:0042593; P:glucose homeostasis; IDA:MGI.
GO; GO:0016525; P:negative regulation of angiogenesis; ISS:UniProtKB.
GO; GO:0007162; P:negative regulation of cell adhesion; ISO:MGI.
GO; GO:0050995; P:negative regulation of lipid catabolic process; ISO:MGI.
GO; GO:0050796; P:regulation of insulin secretion; IDA:MGI.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
CDD; cd00077; HDc; 1.
Gene3D; 1.10.1300.10; -; 1.
InterPro; IPR003607; HD/PDEase_dom.
InterPro; IPR002073; PDEase_catalytic_dom.
InterPro; IPR036971; PDEase_catalytic_dom_sf.
InterPro; IPR023174; PDEase_CS.
Pfam; PF00233; PDEase_I; 1.
SMART; SM00471; HDc; 1.
PROSITE; PS00126; PDEASE_I; 1.
1: Evidence at protein level;
Angiogenesis; cAMP; cGMP; Coiled coil; Complete proteome; Hydrolase;
Membrane; Metal-binding; Phosphoprotein; Reference proteome;
Transmembrane; Transmembrane helix.
CHAIN 1 1100 cGMP-inhibited 3',5'-cyclic
phosphodiesterase B.
/FTId=PRO_0000198803.
TRANSMEM 69 89 Helical. {ECO:0000255}.
TRANSMEM 110 130 Helical. {ECO:0000255}.
TRANSMEM 140 160 Helical. {ECO:0000255}.
TRANSMEM 170 190 Helical. {ECO:0000255}.
TRANSMEM 198 218 Helical. {ECO:0000255}.
TRANSMEM 225 245 Helical. {ECO:0000255}.
REGION 1 28 Interaction with RAPGEF3. {ECO:0000250}.
REGION 415 439 Interaction with PIK3R6. {ECO:0000250}.
REGION 689 1054 Catalytic. {ECO:0000250}.
COILED 1044 1079 {ECO:0000255}.
ACT_SITE 713 713 Proton donor. {ECO:0000250}.
METAL 717 717 Divalent metal cation 1. {ECO:0000250}.
METAL 797 797 Divalent metal cation 1. {ECO:0000250}.
METAL 798 798 Divalent metal cation 1. {ECO:0000250}.
METAL 798 798 Divalent metal cation 2. {ECO:0000250}.
METAL 913 913 Divalent metal cation 1. {ECO:0000250}.
MOD_RES 15 15 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 273 273 Phosphoserine; by PKB/AKT1 or PKB/AKT2.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:10454575}.
MOD_RES 274 274 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 421 421 Phosphoserine.
{ECO:0000250|UniProtKB:Q13370}.
CONFLICT 10 10 A -> T (in Ref. 1; CAA10639).
{ECO:0000305}.
CONFLICT 261 261 E -> D (in Ref. 1; CAA10639).
{ECO:0000305}.
CONFLICT 288 290 SGK -> IPE (in Ref. 3; CAA64775).
{ECO:0000305}.
CONFLICT 439 439 S -> G (in Ref. 1; CAA10639).
{ECO:0000305}.
CONFLICT 444 444 Y -> H (in Ref. 1; CAA10639).
{ECO:0000305}.
CONFLICT 465 465 F -> M (in Ref. 1; CAA10639).
{ECO:0000305}.
CONFLICT 756 756 G -> S (in Ref. 1; CAA10639).
{ECO:0000305}.
CONFLICT 944 944 A -> T (in Ref. 1; CAA10639 and 3;
CAA64775). {ECO:0000305}.
CONFLICT 1082 1082 A -> T (in Ref. 3; CAA64775).
{ECO:0000305}.
SEQUENCE 1100 AA; 122154 MW; 92E36B28D4A5FDF1 CRC64;
MRKDERERDA PAMRSPPPPP ASAASPPESL RNGYVKSCVS PLRQDPPRSF FFHLCRFCNV
EPPAASLRAG ARLSLGVLAA FVLAALLGAR PERWAAAAAG LRTLLSACSL SLSPLFSIAC
AFFFLTCFLT RAQRGPGRGA GSWWLLALPA CCYLGDFAAW QWWSWLRGEP AAAGRLCLVL
SCVGLLTLAP RVRLRHGVLV LLFAGLVWWV SFSGLGALPP ALRPLLSCLV GGAGCLLALG
LDHFFHVRGA SPPPRSASTA EEKVPVIRPR RRSSCVSLGE SAAGYYGSGK MFRRPSLPCI
SREQMILWDW DLKQWCKPHY QNSGGGNGVD LSVLNEARNM VSDLLIDPSL PPQVISSLRS
ISSLMGAFSG SCRPKINSFT PFPGFYPCSE VEDPVEKGDR KLHKGLSGRT SFPTPQLRRS
SGASSLLTNE HCSRWDRSSG KRSYQELSVS SHGCHLNGPF SSNLFTIPKQ RSSSVSLTHH
AGLRRAGALP SHSLLNSSSH VPVSAGSLTN RSPIGFPDTT DFLTKPNIIL HRSLGSVSSA
ADFHQYLRNS DSNLCSSCGH QILKYVSTCE PDGTDHPSEK SGEEDSSVFS KEPLNIVETQ
EEETMKKACR ELFLEGDSHL MEEAQQPNID QEVSLDPMLV EDYDSLIEKM NNWNFQIFEL
VEKMGEKSGR ILSQVMYTLF QDTGLLETFK IPTQEFMNYF RALENGYRDI PYHNRVHATD
VLHAVWYLTT RPIPGLPQIH NNHETETKAD SDGRLGSGQI AYISSKSCCI PDMSYGCLSS
NIPALELMAL YVAAAMHDYD HPGRTNAFLV ATNAPQAVLY NDRSVLENHH AASAWNLYLS
RPEYNFLLNL DHMEFKRFRF LVIEAILATD LKKHFDFLAE FNAKANDVNS NGIEWSSEND
RLLVCQVCIK LADINGPAKD RDLHLRWTEG IVNEFYEQGD EEAALGLPIS PFMDRSSPQL
AKLQESFITH IVGPLCNSYD AAGLLPGQWI ETEEGDDTES DDDDDDDDGD GGEELDSDDE
ETEDNLNPKP QRRKGRRRIF CQLMHHLTEN HKIWKEIIEE EEEKCKAEGN KLQVDNASLP
QADEIQVIEE ADEEEEQMFE


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