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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_RAT               Reviewed;        1108 AA.
Q63085;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
23-MAY-2018, entry version 121.
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;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Adipose tissue;
PubMed=8395509;
Taira M., Hockman S.C., Calvo J.C., Taira M., Belfrage P.,
Manganiello V.C.;
"Molecular cloning of the rat adipocyte hormone-sensitive cyclic GMP-
inhibited cyclic nucleotide phosphodiesterase.";
J. Biol. Chem. 268:18573-18579(1993).
-!- 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; Z22867; CAA80489.1; -; mRNA.
PIR; A48508; A48508.
RefSeq; NP_058925.1; NM_017229.1.
UniGene; Rn.10322; -.
ProteinModelPortal; Q63085; -.
SMR; Q63085; -.
STRING; 10116.ENSRNOP00000015498; -.
iPTMnet; Q63085; -.
PhosphoSitePlus; Q63085; -.
PaxDb; Q63085; -.
PRIDE; Q63085; -.
GeneID; 29516; -.
KEGG; rno:29516; -.
UCSC; RGD:61943; rat.
CTD; 5140; -.
RGD; 61943; Pde3b.
eggNOG; ENOG410IEGG; Eukaryota.
eggNOG; ENOG410XT2V; LUCA.
HOGENOM; HOG000060144; -.
HOVERGEN; HBG053541; -.
InParanoid; Q63085; -.
KO; K13296; -.
PhylomeDB; Q63085; -.
SABIO-RK; Q63085; -.
PRO; PR:Q63085; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IDA:RGD.
GO; GO:0030552; F:cAMP binding; IDA:RGD.
GO; GO:0004119; F:cGMP-inhibited cyclic-nucleotide phosphodiesterase activity; IDA:RGD.
GO; GO:0008144; F:drug binding; IDA:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0051219; F:phosphoprotein binding; IDA:RGD.
GO; GO:0043422; F:protein kinase B binding; ISS:BHF-UCL.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0006198; P:cAMP catabolic process; IDA:RGD.
GO; GO:0032869; P:cellular response to insulin stimulus; ISS:BHF-UCL.
GO; GO:0016101; P:diterpenoid metabolic process; IEP:RGD.
GO; GO:0016525; P:negative regulation of angiogenesis; ISS:UniProtKB.
GO; GO:0046676; P:negative regulation of insulin secretion; IMP:RGD.
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.
PROSITE; PS51845; PDEASE_I_2; 1.
2: Evidence at transcript level;
Angiogenesis; cAMP; cGMP; Complete proteome; Hydrolase; Membrane;
Metal-binding; Phosphoprotein; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 1108 cGMP-inhibited 3',5'-cyclic
phosphodiesterase B.
/FTId=PRO_0000198804.
TRANSMEM 73 93 Helical. {ECO:0000255}.
TRANSMEM 114 134 Helical. {ECO:0000255}.
TRANSMEM 144 164 Helical. {ECO:0000255}.
TRANSMEM 175 195 Helical. {ECO:0000255}.
TRANSMEM 204 224 Helical. {ECO:0000255}.
TRANSMEM 231 251 Helical. {ECO:0000255}.
DOMAIN 633 1070 PDEase. {ECO:0000255|PROSITE-
ProRule:PRU01192}.
REGION 1 32 Interaction with RAPGEF3. {ECO:0000250}.
REGION 421 445 Interaction with PIK3R6. {ECO:0000250}.
COMPBIAS 16 22 Poly-Pro.
COMPBIAS 99 102 Poly-Ala.
COMPBIAS 175 179 Poly-Ala.
COMPBIAS 1007 1021 Poly-Asp.
COMPBIAS 1068 1071 Poly-Glu.
COMPBIAS 1101 1104 Poly-Glu.
ACT_SITE 719 719 Proton donor. {ECO:0000250}.
METAL 723 723 Divalent metal cation 1. {ECO:0000250}.
METAL 803 803 Divalent metal cation 1. {ECO:0000250}.
METAL 804 804 Divalent metal cation 1. {ECO:0000250}.
METAL 804 804 Divalent metal cation 2. {ECO:0000250}.
METAL 919 919 Divalent metal cation 1. {ECO:0000250}.
MOD_RES 15 15 Phosphoserine.
{ECO:0000250|UniProtKB:Q61409}.
MOD_RES 279 279 Phosphoserine; by PKB/AKT1 or PKB/AKT2.
{ECO:0000250|UniProtKB:Q61409}.
MOD_RES 280 280 Phosphoserine.
{ECO:0000250|UniProtKB:Q61409}.
MOD_RES 427 427 Phosphoserine.
{ECO:0000250|UniProtKB:Q13370}.
SEQUENCE 1108 AA; 123107 MW; C9B5078C7D3ADD6D CRC64;
MRKDERERDT PAMRSPPPPP PPATATAASP PESLRNGYVK SCVSPLRQDP PRSFFFHLCR
FCNVEPPAAS LRAGARLSLA ALAAFVLAAL LGAGPERWAA AATGLRTLLS ACSLSLSPLF
SIACAFFFLT CFLTRAQRGP DRGAGSWWLL ALPACCYLGD FAAWQWWSWL RGEPAAAAAG
RLCLVLSCVG LLTLAPRVRL RHGVLVLLFA GLVWWVSFSG LGALPPALRP LLSCLVGGAG
CLLALGLDHF FHVRGASPPP RSASTADEKV PVIRPRRRSS CVSLGESAAG YYGSGKMFRR
PSLPCISREQ MILWDWDLKQ WCKPHYQNSG GGNGVDLSVL NEARNMVSDL LIDPSLPPQV
ISSLRSISSL MGAFSGSCRP KINSFTPFPG FYPCSEVEDP VEKGDRKLHK GLSSKPSFPT
AQLRRSSGAS GLLTSEHHSR WDRSGGKRPY QELSVSSHGC HLNGPFSSNL MTIPKQRSSS
VSLTHHAGLR RAGALPSPSL LNSSSHVPVS AGCLTNRSPV GFLDTSDFLT KPSVTLHRSL
GSVSSAADFH QYLRNSDSSL CSSCGHQILK YVSTCEPDGT DHHNEKSGEE DSTVFSKERL
NIVETQEEET VKEDCRELFL EGDDHLMEEA QQPNIDQEVL LDPMLVEDYD SLIEKMSNWN
FQIFELVEKM GEKSGRILSQ VMYTLFQDTG LLETFKIPTQ EFMNYFRALE NGYRDIPYHN
RVHATDVLHA VWYLTTRPIP GLQQLHNNHE TETKADSDAR LSSGQIAYLS SKSCCIPDKS
YGCLSSNIPA LELMALYVAA AMHDYDHPGR TNAFLVATNA PQAVLYNDRS VLENHHAASA
WNLYLSRPEY NFLLNLDHME FKRFRFLVIE AILATDLKKH FDFLAEFNAK ANDVNSNGIE
WSSENDRLLV CQVCIKLADI NGPAKDRDLH LRWTEGIVNE FYEQGDEEAT LGLPISPFMD
RSSPQLAKLQ ESFITHIVGP LCNSYDAAGL LPGQWIEAEE GDDTESDDDD DDDDDDDDDD
DEELDSDDEE TEDNLNPKPQ RRKGRRRIFC QLMHHLTENH KIWKEIIEEE EKCKAEGNKL
QVDNASLPQA DEIQVIEEAD EEEEQMFE


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