PLCB3_MOUSE
ID PLCB3_MOUSE Reviewed; 1234 AA.
AC P51432; Q3UIS0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 {ECO:0000305};
DE EC=3.1.4.11 {ECO:0000250|UniProtKB:Q99JE6};
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|MGI:MGI:104778};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Kidney;
RX PubMed=9714794; DOI=10.1016/s0005-2760(98)00074-5;
RA Wang S., Zhou Y., Lukinius A., Oberg K., Skogseid B., Gobl A.;
RT "Molecular cloning and characterization of a cDNA encoding mouse
RT phospholipase C-beta3.";
RL Biochim. Biophys. Acta 1393:173-178(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:Q99JE6}.
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:0000250|UniProtKB:Q99JE6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000250|UniProtKB:Q99JE6};
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:0000250|UniProtKB:Q99JE6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485;
CC Evidence={ECO:0000250|UniProtKB:Q99JE6};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with SHANK2 (By similarity). Interacts with LPAR2
CC (By similarity). {ECO:0000250|UniProtKB:Q01970,
CC ECO:0000250|UniProtKB:Q99JE6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99JE6}.
CC Membrane {ECO:0000250|UniProtKB:Q99JE6}. Nucleus
CC {ECO:0000269|PubMed:9714794}. Note=And particulate fractions.
CC {ECO:0000250|UniProtKB:Q99JE6}.
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney, skeletal muscle, liver,
CC lung, heart and brain. {ECO:0000269|PubMed:9714794}.
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DR EMBL; U43144; AAA85199.1; -; mRNA.
DR EMBL; AK146793; BAE27436.1; -; mRNA.
DR EMBL; CH466612; EDL33267.1; -; Genomic_DNA.
DR CCDS; CCDS70925.1; -.
DR RefSeq; NP_001277278.1; NM_001290349.1.
DR RefSeq; NP_032900.2; NM_008874.4.
DR AlphaFoldDB; P51432; -.
DR SMR; P51432; -.
DR BioGRID; 202234; 5.
DR IntAct; P51432; 1.
DR MINT; P51432; -.
DR STRING; 10090.ENSMUSP00000025912; -.
DR iPTMnet; P51432; -.
DR PhosphoSitePlus; P51432; -.
DR EPD; P51432; -.
DR jPOST; P51432; -.
DR MaxQB; P51432; -.
DR PaxDb; P51432; -.
DR PeptideAtlas; P51432; -.
DR PRIDE; P51432; -.
DR ProteomicsDB; 289672; -.
DR Antibodypedia; 3983; 413 antibodies from 36 providers.
DR DNASU; 18797; -.
DR Ensembl; ENSMUST00000025912; ENSMUSP00000025912; ENSMUSG00000024960.
DR GeneID; 18797; -.
DR KEGG; mmu:18797; -.
DR UCSC; uc008gjr.2; mouse.
DR CTD; 5331; -.
DR MGI; MGI:104778; Plcb3.
DR VEuPathDB; HostDB:ENSMUSG00000024960; -.
DR eggNOG; KOG1265; Eukaryota.
DR GeneTree; ENSGT00940000160539; -.
DR HOGENOM; CLU_002738_2_0_1; -.
DR InParanoid; P51432; -.
DR OMA; PNMEVDI; -.
DR OrthoDB; 368239at2759; -.
DR PhylomeDB; P51432; -.
DR TreeFam; TF313216; -.
DR Reactome; R-MMU-112043; PLC beta mediated events.
DR Reactome; R-MMU-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-MMU-399997; Acetylcholine regulates insulin secretion.
DR Reactome; R-MMU-4086398; Ca2+ pathway.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-418217; G beta:gamma signalling through PLC beta.
DR Reactome; R-MMU-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
DR Reactome; R-MMU-500657; Presynaptic function of Kainate receptors.
DR BioGRID-ORCS; 18797; 4 hits in 70 CRISPR screens.
DR ChiTaRS; Plcb3; mouse.
DR PRO; PR:P51432; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P51432; protein.
DR Bgee; ENSMUSG00000024960; Expressed in crypt of Lieberkuhn of small intestine and 215 other tissues.
DR ExpressionAtlas; P51432; baseline and differential.
DR Genevisible; P51432; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0099524; C:postsynaptic cytosol; IDA:SynGO.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; ISO:MGI.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0032957; P:inositol trisphosphate metabolic process; ISO:MGI.
DR GO; GO:0031161; P:phosphatidylinositol catabolic process; ISO:MGI.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; ISS:UniProtKB.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISO:MGI.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; ISO:MGI.
DR GO; GO:0003073; P:regulation of systemic arterial blood pressure; ISO:MGI.
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_0000088492"
FT DOMAIN 318..468
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 591..707
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 708..836
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 466..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1001..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1207..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1234
FT /note="Interaction with SHANK2"
FT /evidence="ECO:0000250"
FT COMPBIAS 484..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..920
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..938
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 332
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 379
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q01970"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01970"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01970"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01970"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 927
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01970"
FT MOD_RES 1105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01970"
FT CONFLICT 16
FT /note="P -> S (in Ref. 1; AAA85199)"
FT /evidence="ECO:0000305"
FT CONFLICT 20
FT /note="E -> K (in Ref. 1; AAA85199)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="A -> S (in Ref. 1; AAA85199)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1234 AA; 139487 MW; E055744A33C5F6B0 CRC64;
MAGARPGVHA LQLEPPTVVE TLRRGSKFIK WDEEASSRNL VTLRVDPNGF FLYWTGPNME
VDTLDISSIR DTRTGRYARL PKDPKIREVL GFGGPDTRLE EKLMTVVAGP DPVNTTFLNF
MAVQDDTVKV WSEELFKLAM NILAQNASRN TFLRKAYTKL KLQVNQDGRI PVKNILKMFS
ADKKRVETAL ESCGLNFNRS ESIRPDEFPL EIFERFLNKL CLRPDIDKIL LEIGAKGKPY
LTLEQLMDFI NQKQRDPRLN EVLYPPLRSS QARLLIEKYE TNKQFLERDQ MSMEGFSRYL
GGEENGILPL EALDLSMDMT QPLSAYFINS SHNTYLTAGQ LAGPSSVEMY RQALLWGCRC
VELDVWKGRP PEEEPFITHG FTMTTEVPLR DVLEAIAEAA FKTSPYPVIL SFENHVDSAK
QQAKMAEYCR SIFGDALLID PLDKYPLSAG IPLPSPQDLM GRILVKNKKR HRPSTGVPDS
SVRKRPLEQS NSALSESSAA TEPSSPQLGS PSSDSCPGLS NGEEVGLEKT SLEPQKSLGE
ESLSREPNVP MPDRDREDEE EDEEEEETTD PKKPTTDEGT ASSEVNATEE MSTLVNYVEP
VKFKSFEAAR KRNKCFEMSS FVETKAMEQL TKSPMEFVEY NKQQLSRIYP KGTRVDSSNY
MPQLFWNVGC QLVALNFQTL DLPMQLNAGV FEYNGRSGYL LKPEFMRRPD KSFDPFTEVI
VDGIVANALR VKVISGQFLS DKKVGIYVEV DMFGLPVDTR RKYRTRTSQG NSFNPVWDEE
PFDFPKVVLP TLASLRIAAF EEGGKFVGHR ILPVSAIRSG YHYVCLRNEA NQPLCLPALL
IYTEASDYIP DDHQDYAEAL INPIKHVSLM DQRAKQLAAL IGESEAQAST ETYQETPCQQ
PGSQLPSNPT PNPLDASPRW PPGPTTSSTS SSLSSPGQRD DLIASILSEV TPTPLEELRS
HKAMVKLRSR QDRDLRELHK KHQRKAVALT RRLLDGLAQA RAEGKCRPSP SALGKATNSE
DVKEEEEAKQ YREFQNRQVQ SLLELREAQA DVETKRKLEH LRQAHQRLKE VVLDTHTTQF
KRLKELNERE KKELQKILDR KRNNSISEAK TREKHKKEVE LTEINRRHIT ESVNSIRRLE
EAQKQRHERL VAGQQQVLQQ LEEEEPKLLA QLTQECQEQR ERLPQEIRRC LLGETAEGLG
DGPLVACASN GHAPGSGGHL SSADSESQEE NTQL
