PLCB2_MOUSE
ID PLCB2_MOUSE Reviewed; 1181 AA.
AC A3KGF7; Q2M4J1; Q3TER8; Q8BI81;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2 {ECO:0000305};
DE EC=3.1.4.11 {ECO:0000250|UniProtKB:Q00722};
DE AltName: Full=Phosphoinositide phospholipase C-beta-2;
DE AltName: Full=Phospholipase C-beta-2;
DE Short=PLC-beta-2;
GN Name=Plcb2 {ECO:0000312|MGI:MGI:107465};
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 [GENOMIC DNA] (ISOFORM 3).
RA Farber C.R., Corva P.M., Medrano J.F.;
RT "Characterization of quantitative trait loci influencing growth and
RT adiposity using congenic mouse strains.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Thymus;
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], AND ALTERNATIVE SPLICING.
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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:Q00722}.
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:Q00722};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000250|UniProtKB:Q00722};
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:Q00722};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485;
CC Evidence={ECO:0000250|UniProtKB:Q00722};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Interacts with RAC1. Forms a complex composed of at least
CC WDR26, a G-beta:gamma unit, and PLCB2. {ECO:0000250|UniProtKB:Q00722}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=A3KGF7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A3KGF7-2; Sequence=VSP_026982, VSP_026985, VSP_026986;
CC Name=3;
CC IsoId=A3KGF7-3; Sequence=VSP_026985, VSP_026986;
CC Name=4;
CC IsoId=A3KGF7-4; Sequence=VSP_026981, VSP_026983, VSP_026984;
CC -!- MISCELLANEOUS: The receptor-mediated activation of PLC-beta-2 is most
CC effectively mediated by one G-protein alpha subunit, alpha-16.
CC {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY902324; AAX90609.1; -; Genomic_DNA.
DR EMBL; AK045469; BAC32384.1; -; mRNA.
DR EMBL; AK169442; BAE41180.1; -; mRNA.
DR EMBL; AL772255; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS16582.1; -. [A3KGF7-1]
DR RefSeq; NP_001277719.1; NM_001290790.1.
DR RefSeq; NP_808236.2; NM_177568.2. [A3KGF7-1]
DR AlphaFoldDB; A3KGF7; -.
DR SMR; A3KGF7; -.
DR BioGRID; 202233; 2.
DR CORUM; A3KGF7; -.
DR IntAct; A3KGF7; 6.
DR STRING; 10090.ENSMUSP00000099583; -.
DR iPTMnet; A3KGF7; -.
DR PhosphoSitePlus; A3KGF7; -.
DR EPD; A3KGF7; -.
DR MaxQB; A3KGF7; -.
DR PaxDb; A3KGF7; -.
DR PeptideAtlas; A3KGF7; -.
DR PRIDE; A3KGF7; -.
DR ProteomicsDB; 289525; -. [A3KGF7-1]
DR ProteomicsDB; 289526; -. [A3KGF7-2]
DR ProteomicsDB; 289527; -. [A3KGF7-3]
DR ProteomicsDB; 289528; -. [A3KGF7-4]
DR Antibodypedia; 4002; 183 antibodies from 28 providers.
DR DNASU; 18796; -.
DR Ensembl; ENSMUST00000102524; ENSMUSP00000099583; ENSMUSG00000040061. [A3KGF7-1]
DR GeneID; 18796; -.
DR KEGG; mmu:18796; -.
DR UCSC; uc008lsi.1; mouse. [A3KGF7-1]
DR UCSC; uc008lsk.1; mouse. [A3KGF7-2]
DR UCSC; uc008lsl.1; mouse. [A3KGF7-4]
DR CTD; 5330; -.
DR MGI; MGI:107465; Plcb2.
DR VEuPathDB; HostDB:ENSMUSG00000040061; -.
DR eggNOG; KOG1265; Eukaryota.
DR GeneTree; ENSGT00940000159326; -.
DR HOGENOM; CLU_002738_2_0_1; -.
DR InParanoid; A3KGF7; -.
DR OMA; NMALFEY; -.
DR OrthoDB; 368239at2759; -.
DR PhylomeDB; A3KGF7; -.
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; 18796; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Plcb2; mouse.
DR PRO; PR:A3KGF7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A3KGF7; protein.
DR Bgee; ENSMUSG00000040061; Expressed in granulocyte and 88 other tissues.
DR ExpressionAtlas; A3KGF7; baseline and differential.
DR Genevisible; A3KGF7; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031680; C:G-protein beta/gamma-subunit complex; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; ISO:MGI.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; ISS:UniProtKB.
DR GO; GO:0004629; F:phospholipase C activity; ISO:MGI.
DR GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR GO; GO:0001580; P:detection of chemical stimulus involved in sensory perception of bitter taste; ISO:MGI.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; ISS:UniProtKB.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0050913; P:sensory perception of bitter taste; IMP: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; IPR028403; PLC-beta2.
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 PANTHER; PTHR10336:SF10; PTHR10336:SF10; 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 Alternative splicing; Calcium; Coiled coil; Hydrolase; Lipid degradation;
KW Lipid metabolism; Metal-binding; Phosphoprotein; Reference proteome;
KW Transducer.
FT CHAIN 1..1181
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase beta-2"
FT /id="PRO_0000295683"
FT DOMAIN 312..463
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 547..663
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 666..791
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 465..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 847..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 893..940
FT /evidence="ECO:0000255"
FT COILED 974..1026
FT /evidence="ECO:0000255"
FT COILED 1075..1141
FT /evidence="ECO:0000255"
FT COMPBIAS 499..522
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 327
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 374
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT BINDING 328
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 357
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 359
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 408
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 950
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00722"
FT VAR_SEQ 1..55
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026981"
FT VAR_SEQ 55..77
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026982"
FT VAR_SEQ 637..688
FT /note="DLPMQQNMALFEFNGQSGYLLKHEFMRRLDKQFNPFSVDRIDVVVATTLSIT
FT -> GKNTSKTREPSPGPLTTSPEPSPGPCIPRCPPSEPSSGPCLSDPYSSLDKEL (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026983"
FT VAR_SEQ 689..1181
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026984"
FT VAR_SEQ 689..702
FT /note="IISGQFLSERSVRT -> ARPRADKWLGGLGS (in isoform 2 and
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026985"
FT VAR_SEQ 703..1181
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026986"
SQ SEQUENCE 1181 AA; 134546 MW; 8E23BD29391ABE4E CRC64;
MSLLNPVLLP PNVKAYLSQG ERFIKWDDET SIASPVILRV DPKGYYLYWT YQNQEMEFLD
VTSIRDTRFG KFAKIPKSQK LREVFNMDFP DNHFLLKTLT VVSGPDMVDL TFYNFVSYKE
NVGKDWAEDV LALAKHPMTV NAPRSTFLDK ILVKLKMQLN PEGKIPVKNF FQMFPADRKR
VEAALGACHL AKGKNDAINP EDFPESVYKS FLMSLCPRPE IDEIFTSYHS KAKPYMTKEH
LTKFINQKQR DPRLNSLLFP PARPEQVQVL IDKYEPSGIN VQRGQLSPEG MVWFLCGPEN
SVLAHDTLLI HQDMTQPLNH YFINSSHNTY LTAGQFSGLS SAEMYRQVLL SGCRCVELDC
WKGKPPDEEP IITHGFTMTT DILFKEAIEA IAESAFKTSP YPVILSFENH VDSPRQQAKM
AEYCRSMFGE TLLTDPLENF PLKPGIPLPS PEDLRGKILI KNKKNQFSGP ASPSKKPGGV
AEGSLPSSVP VEEDTGWTAE DRTEVEEEEV VEEEEEEESG NLDEEEIKKM QSDEGTAGLE
VTAYEEMSSL VNYIQPTKFI SFEFSAQKNR SYVVSSFTEL KAYELLSKAS MQFVDYNKRQ
MSRVYPKGTR MDSSNYMPQM FWNAGCQMVA LNFQTMDLPM QQNMALFEFN GQSGYLLKHE
FMRRLDKQFN PFSVDRIDVV VATTLSITII SGQFLSERSV RTYVEVELFG LPGDPKRRYR
TKLSPTANSI NPVWKEEPFI FEKILMPELA SLRIAVMEEG SKFLGHRIIP INALHSGYHH
LCLRSESNMA LTMPALFVFL EMKDYIPDTW ADLTVALANP IKYFNAQDKK SVKLKGVTGS
LPEKLFSGTP VASQSNGAPV SAGNGSTAPG TKATGEEATK EVTEPQTASL EELRELKGVV
KLQRRHEKEL RELERRGARR WEELLQRGAA QLAELQTQAA GCKLRPGKGS RKKRTLPCEE
TVVAPSEPHD RADPRVQELK DRLEQELQQQ GEEQYRSVLK RKEQHVTEQI AKMMELAREK
QAAELKTFKE TSETDTKEMK KKLEAKRLER IQAMTKVTTD KVAQERLKRE INNSHIQEVV
QAVKQMTETL ERHQEKLEER QTACLEQIQA MEKQFQEKAL AEYEAKMKGL EAEVKESVRA
YFKDCFPTEA EDKPERSCEA SEESCPQEPL VSKADTQESR L
