PLCB3_RAT
ID PLCB3_RAT Reviewed; 1234 AA.
AC Q99JE6; Q62887; Q9QW29;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 {ECO:0000305};
DE EC=3.1.4.11 {ECO:0000269|PubMed:8454637};
DE AltName: Full=Phosphoinositide phospholipase C-beta-3;
DE AltName: Full=Phospholipase C-beta-3;
DE Short=PLC-beta-3;
GN Name=Plcb3 {ECO:0000312|RGD:61993};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|EMBL:AAK14906.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
RX PubMed=9332346; DOI=10.1016/s0378-1119(97)00213-8;
RA Kang J.S., Lee H.B., Rhee S.G., Park K., Yoo O.J.;
RT "The 5'-upstream region of the rat phospholipase C-beta 3 gene contains two
RT critical Sp1 sites and an HIV Inr-like element.";
RL Gene 197:19-28(1997).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-1234, FUNCTION, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RC STRAIN=Fischer; TISSUE=Thyroid;
RX PubMed=8454637; DOI=10.1016/s0021-9258(18)53300-7;
RA Jhon D.-Y., Lee H.-H., Park D., Lee C.-W., Lee K.-H., Yoo O.J., Rhee S.G.;
RT "Cloning, sequencing, purification, and Gq-dependent activation of
RT phospholipase C-beta 3.";
RL J. Biol. Chem. 268:6654-6661(1993).
RN [3]
RP INTERACTION WITH SHANK2.
RX PubMed=15632121; DOI=10.1074/jbc.m410740200;
RA Hwang J.-I., Kim H.S., Lee J.R., Kim E., Ryu S.H., Suh P.-G.;
RT "The interaction of phospholipase C-beta3 with Shank2 regulates mGluR-
RT mediated calcium signal.";
RL J. Biol. Chem. 280:12467-12473(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535 AND SER-1105, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: The production of the second messenger molecules
CC diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated
CC by activated phosphatidylinositol-specific phospholipase C enzymes.
CC {ECO:0000250|UniProtKB:P51432, ECO:0000269|PubMed:8454637}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-
CC diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456,
CC ChEBI:CHEBI:203600; EC=3.1.4.11;
CC Evidence={ECO:0000269|PubMed:8454637};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000305|PubMed:8454637};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + H2O =
CC 1D-myo-inositol 1-phosphate + a 1,2-diacyl-sn-glycerol + H(+);
CC Xref=Rhea:RHEA:43484, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:57880, ChEBI:CHEBI:58433;
CC Evidence={ECO:0000269|PubMed:8454637};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485;
CC Evidence={ECO:0000305|PubMed:8454637};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:8454637};
CC -!- SUBUNIT: Interacts with LPAR2 (By similarity). Interacts with SHANK2
CC (PubMed:15632121). {ECO:0000250|UniProtKB:Q01970,
CC ECO:0000269|PubMed:15632121}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8454637}. Membrane
CC {ECO:0000269|PubMed:8454637}. Nucleus {ECO:0000250|UniProtKB:P51432}.
CC Note=And particulate fractions.
CC -!- TISSUE SPECIFICITY: Expressed in parotid gland, brain, liver, uterus,
CC lung, heart, adrenal gland, and ovary. Not detected in spleen,
CC pancreas, intestine, thymus or kidney. {ECO:0000269|PubMed:8454637}.
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DR EMBL; U41411; AAC53366.1; -; Genomic_DNA.
DR EMBL; M99567; AAK14906.1; -; mRNA.
DR PIR; A45493; A45493.
DR AlphaFoldDB; Q99JE6; -.
DR SMR; Q99JE6; -.
DR STRING; 10116.ENSRNOP00000028720; -.
DR SwissLipids; SLP:000000945; -.
DR iPTMnet; Q99JE6; -.
DR PhosphoSitePlus; Q99JE6; -.
DR jPOST; Q99JE6; -.
DR PaxDb; Q99JE6; -.
DR PeptideAtlas; Q99JE6; -.
DR UCSC; RGD:61993; rat.
DR RGD; 61993; Plcb3.
DR eggNOG; KOG1265; Eukaryota.
DR InParanoid; Q99JE6; -.
DR BRENDA; 3.1.4.11; 5301.
DR Reactome; R-RNO-112043; PLC beta mediated events.
DR Reactome; R-RNO-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-RNO-399997; Acetylcholine regulates insulin secretion.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR Reactome; R-RNO-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
DR PRO; PR:Q99JE6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0099524; C:postsynaptic cytosol; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0042383; C:sarcolemma; IDA:RGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; ISO:RGD.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IDA:UniProtKB.
DR GO; GO:0004629; F:phospholipase C activity; TAS:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0032957; P:inositol trisphosphate metabolic process; IDA:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; NAS:UniProtKB.
DR GO; GO:0031161; P:phosphatidylinositol catabolic process; IDA:RGD.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; ISO:RGD.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IDA:UniProtKB.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; IDA:RGD.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; NAS:UniProtKB.
DR GO; GO:0003073; P:regulation of systemic arterial blood pressure; ISO:RGD.
DR CDD; cd13361; PH_PLC_beta; 1.
DR Gene3D; 1.20.1230.10; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR Gene3D; 3.20.20.190; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR016280; PLC-beta.
DR InterPro; IPR014815; PLC-beta_C.
DR InterPro; IPR042531; PLC-beta_C_sf.
DR InterPro; IPR037862; PLC-beta_PH.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR015359; PLC_EF-hand-like.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336; PTHR10336; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF09279; EF-hand_like; 1.
DR Pfam; PF17787; PH_14; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR Pfam; PF08703; PLC-beta_C; 1.
DR PIRSF; PIRSF000956; PLC-beta; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 1.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Calcium; Cytoplasm; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q01970"
FT CHAIN 2..1234
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase beta-3"
FT /id="PRO_0000088493"
FT DOMAIN 315..466
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 589..705
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 706..834
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 465..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1234
FT /note="Interaction with SHANK2"
FT /evidence="ECO:0000269|PubMed:15632121"
FT COMPBIAS 482..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 330
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 377
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q01970"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01970"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01970"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01970"
FT MOD_RES 535
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 925
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01970"
FT MOD_RES 1105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 17
FT /note="T -> A (in Ref. 2; AAK14906)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1234 AA; 139450 MW; 2EBD7282F052CA6A CRC64;
MAGARPGVHA LQLEPPTVVE TLRRGSKFIK WDEEASSRNL VTLRLDPNGF FLYWTGPNME
VDTLDISSIR DTRTGRYARL PKDPKIREVL GFGGPDTRLE EKLMTVVAGP DPVNTTFLNF
MAVQDDTVKV WSEELFKLAM NILAQNAPEH VLRKAYTKLK LQVNQDGRIP VKNILKMFSA
DKKRVETALI CGLNFNRSES IRPDEFSLEI FERFLNKLLL RPDIDKILLE IGAKGKPYLT
LEQLMDFINQ KQRDPRLNEV LYPPLRSSQA RLLIEKYEPN KQFLERDQMS MEGFSRYLGG
EENGILPLEA LDLSMDMTQP LSAYFINSSH NTYLTAGQLA GTSSVEMYRQ ALLWGCRCVE
LDVWKGRPPE EEPFITHGFT MTTEVPLRDV LEAIAETAFK TSPYPVILSF ENHVDSAKQQ
AKMAEYCRSI FGEALLIDPL DKYPLSAGTP LPSPQDLMGR ILVKNKKRHR PSTGVPDSSV
AKRPLEQSNS ALSESSAATE PSSPQLGSPS SDSCPGLSNG EEVGLEKTSL EPQKSLGEEG
LNRGPNVLMP DRDREDEEED EEEEETTDPK KPTTDEGTAS SEVNATEEMS TLVNYVEPVK
FKSFEASRKR NKCFEMSSFV ETKAMEQLTK SPMEFVEYNK QQLSRIYPKG TRVDSSNYMP
QLFWNVGCQL VALNFQTLDL PMQLNAGVFE YNGRSGYLLK PEFMRRPDKS FDPFTEVIVD
GIVANALRVK VISGQFLSDR KVGIYVEVDM FGLPVDTRRK YRTRTSQGNS FNPVWDEEPF
DFPKVVLPTL ASLRIAAFEE GGRFVGHRIL PVSAIRSGYH YVCLRNEANQ PLCLPALLIY
TEASDYIPDD HQDYAEALIN PIKHVSLMDQ RAKQLAALIG ESEAQASTEM CQETPSQQQG
SQLSSNPVPN PLDDSPRWPP GPTTSPTSTS LSSPGQRDDL IASILSEVTP TPLEELRSHK
AMVKLRSRQD RDLRELHKKH QRKAVALTRR LLDGLAQARA EGKCRPSSSA LSRATNVEDV
KEEEKEAARQ YREFQNRQVQ SLLELREAQA DAETERRLEH LKQAQQRLRE VVLDAHTTQF
KRLKELNERE KKELQKILDR KRNNSISEAK TREKHKKEVE LTEINRRHIT ESVNSIRRLE
EAQKQRHERL LAGQQQVLQQ LVEEEPKLVA QLTQECQEQR ERLPQEIRRC LLGETSEGLG
DGPLVACASN GHAAGSGGHQ SGADSESQEE NTQL
