PLCG_CAEEL
ID PLCG_CAEEL Reviewed; 1350 AA.
AC Q22070;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma plc-3 {ECO:0000305};
DE EC=3.1.4.11 {ECO:0000255|RuleBase:RU361133};
DE AltName: Full=Phosphoinositide phospholipase C-gamma plc-3 {ECO:0000305};
DE AltName: Full=Phospholipase C-gamma plc-3 {ECO:0000305};
DE Short=PLC-gamma plc-3 {ECO:0000305};
GN Name=plc-3 {ECO:0000312|WormBase:T01E8.3};
GN ORFNames=T01E8.3 {ECO:0000312|WormBase:T01E8.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15194811; DOI=10.1091/mbc.e04-03-0198;
RA Yin X., Gower N.J., Baylis H.A., Strange K.;
RT "Inositol 1,4,5-trisphosphate signaling regulates rhythmic contractile
RT activity of myoepithelial sheath cells in Caenorhabditis elegans.";
RL Mol. Biol. Cell 15:3938-3949(2004).
RN [3] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16186564; DOI=10.1085/jgp.200509355;
RA Espelt M.V., Estevez A.Y., Yin X., Strange K.;
RT "Oscillatory Ca2+ signaling in the isolated Caenorhabditis elegans
RT intestine: role of the inositol-1,4,5-trisphosphate receptor and
RT phospholipases C beta and gamma.";
RL J. Gen. Physiol. 126:379-392(2005).
RN [4] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=15958491; DOI=10.1091/mbc.e05-02-0096;
RA Gower N.J., Walker D.S., Baylis H.A.;
RT "Inositol 1,4,5-trisphosphate signaling regulates mating behavior in
RT Caenorhabditis elegans males.";
RL Mol. Biol. Cell 16:3978-3986(2005).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=17891142; DOI=10.1038/nn1981;
RA Van Buskirk C., Sternberg P.W.;
RT "Epidermal growth factor signaling induces behavioral quiescence in
RT Caenorhabditis elegans.";
RL Nat. Neurosci. 10:1300-1307(2007).
RN [6] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18604269; DOI=10.1371/journal.pgen.1000117;
RA Gruninger T.R., Gualberto D.G., Garcia L.R.;
RT "Sensory perception of food and insulin-like signals influence seizure
RT susceptibility.";
RL PLoS Genet. 4:E1000117-E1000117(2008).
RN [7] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18369461; DOI=10.1371/journal.pgen.1000043;
RA Vazquez-Manrique R.P., Nagy A.I., Legg J.C., Bales O.A., Ly S.,
RA Baylis H.A.;
RT "Phospholipase C-epsilon regulates epidermal morphogenesis in
RT Caenorhabditis elegans.";
RL PLoS Genet. 4:E1000043-E1000043(2008).
RN [8] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19380113; DOI=10.1016/j.chom.2009.03.006;
RA Ziegler K., Kurz C.L., Cypowyj S., Couillault C., Pophillat M., Pujol N.,
RA Ewbank J.J.;
RT "Antifungal innate immunity in C. elegans: PKCdelta links G protein
RT signaling and a conserved p38 MAPK cascade.";
RL Cell Host Microbe 5:341-352(2009).
RN [9] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19730689; DOI=10.1371/journal.pgen.1000636;
RA Walker D.S., Vazquez-Manrique R.P., Gower N.J., Gregory E., Schafer W.R.,
RA Baylis H.A.;
RT "Inositol 1,4,5-trisphosphate signalling regulates the avoidance response
RT to nose touch in Caenorhabditis elegans.";
RL PLoS Genet. 5:E1000636-E1000636(2009).
RN [10] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19923421; DOI=10.1152/ajpcell.00394.2009;
RA Xing J., Strange K.;
RT "Phosphatidylinositol 4,5-bisphosphate and loss of PLCgamma activity
RT inhibit TRPM channels required for oscillatory Ca2+ signaling.";
RL Am. J. Physiol. 298:C274-C282(2010).
CC -!- FUNCTION: Mediates the production of the second messenger molecules
CC diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) which plays
CC an important role in the regulation of intracellular signaling cascades
CC (Probable). Regulates basal and ovulatory sheath cell contractions by
CC controlling Ca(2+) oscillations via IP3-mediated activation of IP3
CC receptor itr-1 (PubMed:15194811). In intestinal epithelial cells,
CC regulates Ca(2+) oscillations which control posterior body wall muscle
CC contractions required for defecation by IP3-mediated activation of itr-
CC 1 and probably by activating TRPM channels gon-2 and gtl-1 by reducing
CC PIP2 levels (PubMed:19923421, PubMed:16186564). By activating tpa-1 via
CC DAG production, required for the expression of antimicrobial peptide
CC nlp-29 in the epidermis in response to fungal infection or physical
CC injury (PubMed:19380113). By triggering Ca(2+) transient via IP3-
CC mediated activation of IPR3 receptor itr-1 in ASH sensory neurons,
CC involved in avoidance behavior in response to nose touch
CC (PubMed:19730689). Probably by regulating neuronal transmission in ALA
CC neurons, mediates the decrease in pharyngeal pumping and locomotion
CC during the quiescent state that precedes each larval molt, downstream
CC of lin-3 and receptor let-23 and upstream of tpa-1 but not itr-1
CC (PubMed:17891142). During embryogenesis, may play an role in epidermal
CC morphogenesis together with plc-1 (PubMed:18369461). Probably
CC downstream of receptor daf-2, regulates male-sex muscle excitability in
CC the absence of food (PubMed:18604269). {ECO:0000269|PubMed:15194811,
CC ECO:0000269|PubMed:16186564, ECO:0000269|PubMed:17891142,
CC ECO:0000269|PubMed:18369461, ECO:0000269|PubMed:18604269,
CC ECO:0000269|PubMed:19380113, ECO:0000269|PubMed:19730689,
CC ECO:0000269|PubMed:19923421, ECO:0000305}.
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:0000255|RuleBase:RU361133};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305};
CC -!- TISSUE SPECIFICITY: Expressed in intestine, isthmus of the pharynx,
CC proximal gonad sheath cells, spermatheca and uterine sheath cells
CC (PubMed:15194811, PubMed:16186564). In males, expressed in the valve
CC cell, the vas deferens and retractor and ventral protactor muscles
CC (PubMed:15958491, PubMed:18604269). {ECO:0000269|PubMed:15194811,
CC ECO:0000269|PubMed:15958491, ECO:0000269|PubMed:16186564,
CC ECO:0000269|PubMed:18604269}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes sterility
CC resulting from impaired spermatheca dilatation causing a defect in
CC ovulation, and a severe decrease in sheath cell basal and peak
CC ovulatory contractions (PubMed:15194811, PubMed:18369461). The few
CC embryos laid are arrested at the embryonic stage (PubMed:18369461).
CC Cycles of posterior body wall muscle contractions are prolonged and
CC arrhythmic resulting in a defecation defect (PubMed:16186564). Ca(2+)
CC oscillations in intestinal cells are arrhythmic and the whole cell
CC current amplitude is severely reduced (PubMed:16186564,
CC PubMed:19923421). RNAi-mediated knockdown in males causes an increase
CC in spontaneous muscle seizures in the absence of food in an unc-103
CC mutant background (PubMed:18604269). Ca(2+) transient increase and
CC avoidance behavior are defective in response to nose touch but not to
CC benzaldehyde (PubMed:19730689). nlp-29 expression is abrogated
CC following fungal infection by D.coniospora and severely reduced
CC following physical injury (PubMed:19380113).
CC {ECO:0000269|PubMed:15194811, ECO:0000269|PubMed:16186564,
CC ECO:0000269|PubMed:18369461, ECO:0000269|PubMed:18604269,
CC ECO:0000269|PubMed:19380113, ECO:0000269|PubMed:19730689,
CC ECO:0000269|PubMed:19923421}.
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DR EMBL; BX284602; CAA88745.2; -; Genomic_DNA.
DR RefSeq; NP_496205.2; NM_063804.4.
DR AlphaFoldDB; Q22070; -.
DR SMR; Q22070; -.
DR IntAct; Q22070; 2.
DR STRING; 6239.T01E8.3; -.
DR EPD; Q22070; -.
DR PaxDb; Q22070; -.
DR PeptideAtlas; Q22070; -.
DR PRIDE; Q22070; -.
DR EnsemblMetazoa; T01E8.3.1; T01E8.3.1; WBGene00004038.
DR GeneID; 174586; -.
DR KEGG; cel:CELE_T01E8.3; -.
DR UCSC; T01E8.3; c. elegans.
DR CTD; 174586; -.
DR WormBase; T01E8.3; CE42905; WBGene00004038; plc-3.
DR eggNOG; KOG1264; Eukaryota.
DR GeneTree; ENSGT00940000169016; -.
DR HOGENOM; CLU_002738_5_0_1; -.
DR InParanoid; Q22070; -.
DR OMA; SLDCYAQ; -.
DR OrthoDB; 368239at2759; -.
DR PhylomeDB; Q22070; -.
DR Reactome; R-CEL-114604; GPVI-mediated activation cascade.
DR Reactome; R-CEL-1169408; ISG15 antiviral mechanism.
DR Reactome; R-CEL-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-CEL-186763; Downstream signal transduction.
DR Reactome; R-CEL-202433; Generation of second messenger molecules.
DR Reactome; R-CEL-210990; PECAM1 interactions.
DR Reactome; R-CEL-212718; EGFR interacts with phospholipase C-gamma.
DR Reactome; R-CEL-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-CEL-5621480; Dectin-2 family.
DR Reactome; R-CEL-5654219; Phospholipase C-mediated cascade: FGFR1.
DR Reactome; R-CEL-5654228; Phospholipase C-mediated cascade, FGFR4.
DR PRO; PR:Q22070; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00004038; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-EC.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IBA:GO_Central.
DR GO; GO:0030431; P:sleep; IMP:WormBase.
DR CDD; cd09932; SH2_C-SH2_PLC_gamma_like; 1.
DR CDD; cd10341; SH2_N-SH2_PLC_gamma_like; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR Gene3D; 3.20.20.190; -; 2.
DR Gene3D; 3.30.505.10; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR016279; PLC-gamma.
DR InterPro; IPR035023; PLC-gamma_C-SH2.
DR InterPro; IPR035024; PLC-gamma_N-SH2.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR10336; PTHR10336; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR Pfam; PF00017; SH2; 2.
DR Pfam; PF00018; SH3_1; 1.
DR PIRSF; PIRSF000952; PLC-gamma; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00239; C2; 1.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SMART; SM00252; SH2; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR SUPFAM; SSF55550; SSF55550; 2.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
DR PROSITE; PS50001; SH2; 2.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW Calcium; Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding;
KW Reference proteome; Repeat; SH2 domain; SH3 domain; Transducer.
FT CHAIN 1..1350
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase gamma plc-3"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437463"
FT DOMAIN 352..503
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 605..704
FT /note="SH2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 715..804
FT /note="SH2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 832..890
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 855..960
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 982..1092
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 1099..1220
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1270..1350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1285..1332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 367
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 419
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
SQ SEQUENCE 1350 AA; 154574 MW; 8F636BE56E7F58F1 CRC64;
MQHGSLGPSS SSRKTTVTST AGSVHLHHRS SNGFSTASRA QLNRHNEMDF GKMFAAMEKG
HKVCKIAVLK KWDPAYKQLT LDRYSRQIFL TKLELSAVRN KPTILDIRQI REVQTLNYKL
NTIKVDDKWK KDREIVNFDS KAILIISYGM GFALSYWILL FESEDACKLW SQGLHNLMMD
TRDRDSSPHP LRIERFLHKH FLSLMSPAND AVARKHMKPF VQTSLQFKVQ SDQLQQVTED
QMNSDQFSFA SRQLIHVPEL FSSRFADLAE KHERKGLVVT FQNFLRFLDG KQFDELASNR
TRALEFLNRY FQEDQAYFGD RNEPSMTVFE FCDFLFSREN SLWDPTNEKV THDMSRPLSH
YWIASSHNTY LTGDQLRSES SLDCYAQALL MGCRCIELDC WDGQKKPGSA EFIDIVIYHG
YTMTSKILLR DVLHVIRHYA FVTSEYPVIL SIEDNCSVPA QRLLAQELKD ILGDYLLTQP
ANREEKQLPS PAALKKKIIV KHKKLPIESE DLAAVVKTDE FQDTEIISRE CVKKGILMVK
NNNSHEWTSH VFILFPDRLC YLIQTADPEN PNDDTVSVSG DEEREEETPS GFGVKPEEMH
VTEEWFHGRC ERDEAKKRIL EHKEKGNGLF MIRDSNLFIG DFSLSILHDG KVHHVRIRSK
IIDKEKKYYF MDNKVCDTLY ELVSYYTRHY LTTAHFKMVL TIPCPQPQPH LNQPWFSATA
DKEKAEELLS LVPEDGAFLI RTSSTDSSVY VLSLKVDGEF WHYRLKRDGR IFVVNQKVFE
NLNQIVEFYA NREFVRGISL RFPVNEKDIS HLTAELAEAR TPGCYMDLKD LDKEVQARAL
RPYRGTADDE LSFPANVIIT VLRKEEGLWR GRYGSLTGWF PSAHVQEILP EKVSTSETSN
YNTIELAGTL IERIHDADRP NVIRISQSNQ HWMNKQYYLL AASSSEEADG WQNNLFELTR
SVNTKMSILR TKEKEKRIAA ELSNLVVYCQ AVPFDPAHIY NDAFYEMCSF VEGKLDKLVE
KGLLPFNSRK LSRVYPNGSR ITSNNYSPVP MWNAGCHMVA LNYQTGDKPM QLNQGKFLAN
GRCGYLLKPD YMLTDDFDPT NTEKFATAYP IRLNVQVIGG RHLSRKDKNK GICSPFVEIE
IIGMPCDTKV FQTKTIASNG LNPIWNQTFT FEIQCPEVAL IRFHVEDGDF VGPKTDPFIG
QAVFPVDSIR CGFRSVPLKN QYSEELELSS LLVDVQMCSR EGTQLIRSSS HFLQASRLAP
VFAHRKITNG DSIPREMAPR LRTSATDRSL DSPTNSESRA TLLSGQRGSQ DSMDSAAETS
SIASGTISSR DGKKKQNWLK KFSFGKSSKS
