PLCD2_ARATH
ID PLCD2_ARATH Reviewed; 581 AA.
AC Q39033; Q56XL3; Q8LG47;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Phosphoinositide phospholipase C 2;
DE EC=3.1.4.11;
DE AltName: Full=Phosphoinositide phospholipase PLC2;
DE Short=AtPLC2;
DE Short=PI-PLC2;
GN Name=PLC2; OrderedLocusNames=At3g08510; ORFNames=T8G24.4;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND LACK OF INDUCTION.
RX PubMed=9177324; DOI=10.1023/a:1005885230896;
RA Hirayama T., Mitsukawa N., Shibata D., Shinozaki K.;
RT "AtPLC2, a gene encoding phosphoinositide-specific phospholipase C, is
RT constitutively expressed in vegetative and floral tissues in Arabidopsis
RT thaliana.";
RL Plant Mol. Biol. 34:175-180(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 309-581.
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 319-581.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11377433; DOI=10.1016/s0014-5793(01)02453-x;
RA Otterhag L., Sommarin M., Pical C.;
RT "N-terminal EF-hand-like domain is required for phosphoinositide-specific
RT phospholipase C activity in Arabidopsis thaliana.";
RL FEBS Lett. 497:165-170(2001).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12226484; DOI=10.1104/pp.004770;
RA Mueller-Roeber B., Pical C.;
RT "Inositol phospholipid metabolism in Arabidopsis. Characterized and
RT putative isoforms of inositol phospholipid kinase and phosphoinositide-
RT specific phospholipase C.";
RL Plant Physiol. 130:22-46(2002).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [10]
RP FUNCTION, LACK OF INDUCTION, AND TISSUE SPECIFICITY.
RX AGRICOLA=IND43668249; DOI=10.1111/j.1469-8137.2004.01069.x;
RA Hunt L., Otterhag L., Lee J.C., Lasheen T., Hunt J., Seki M., Shinozaki K.,
RA Sommarin M., Gilmour D.J., Pical C., Gray J.E.;
RT "Gene-specific expression and calcium activation of Arabidopsis thaliana
RT phospholipase C isoforms.";
RL New Phytol. 162:643-654(2004).
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. At
CC physiological calcium concentration, the preferred substrate is
CC phosphatidylinositol 4,5-bisphosphate versus phosphatidylinositol.
CC {ECO:0000269|PubMed:11377433, ECO:0000269|Ref.10}.
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11377433};
CC Peripheral membrane protein {ECO:0000269|PubMed:11377433}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q39033-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, shoots, leaves and flowers.
CC {ECO:0000269|PubMed:9177324, ECO:0000269|Ref.10}.
CC -!- INDUCTION: Not induced by environmental stresses such as dehydration,
CC salinity and low temperature.
CC -!- DOMAIN: Amino acids 23-36 of the EF-hand-like domain are necessary
CC catalysis but not for binding to lipid vesicles.
CC -!- PTM: Phosphorylation level varies significantly during early response
CC to bacterial elicitor.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM61037.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; D50804; BAA09432.1; -; mRNA.
DR EMBL; AC074395; AAG50827.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74640.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74641.1; -; Genomic_DNA.
DR EMBL; AF360206; AAK25916.1; -; mRNA.
DR EMBL; AY040054; AAK64112.1; -; mRNA.
DR EMBL; AY084465; AAM61037.1; ALT_SEQ; mRNA.
DR EMBL; AK221660; BAD95335.1; -; mRNA.
DR PIR; S71170; S71170.
DR RefSeq; NP_001030660.1; NM_001035583.1. [Q39033-1]
DR RefSeq; NP_187464.1; NM_111686.6. [Q39033-1]
DR AlphaFoldDB; Q39033; -.
DR SMR; Q39033; -.
DR BioGRID; 5334; 34.
DR IntAct; Q39033; 11.
DR MINT; Q39033; -.
DR STRING; 3702.AT3G08510.1; -.
DR iPTMnet; Q39033; -.
DR SwissPalm; Q39033; -.
DR PaxDb; Q39033; -.
DR PRIDE; Q39033; -.
DR ProteomicsDB; 236632; -. [Q39033-1]
DR EnsemblPlants; AT3G08510.1; AT3G08510.1; AT3G08510. [Q39033-1]
DR EnsemblPlants; AT3G08510.2; AT3G08510.2; AT3G08510. [Q39033-1]
DR GeneID; 819999; -.
DR Gramene; AT3G08510.1; AT3G08510.1; AT3G08510. [Q39033-1]
DR Gramene; AT3G08510.2; AT3G08510.2; AT3G08510. [Q39033-1]
DR KEGG; ath:AT3G08510; -.
DR Araport; AT3G08510; -.
DR TAIR; locus:2103437; AT3G08510.
DR eggNOG; KOG0169; Eukaryota.
DR HOGENOM; CLU_002738_3_2_1; -.
DR InParanoid; Q39033; -.
DR OMA; FTCIQAG; -.
DR PhylomeDB; Q39033; -.
DR BioCyc; ARA:MONQT-8777; -.
DR BioCyc; MetaCyc:MON-1621; -.
DR BRENDA; 3.1.4.11; 399.
DR PRO; PR:Q39033; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q39033; baseline and differential.
DR Genevisible; Q39033; AT.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IBA:GO_Central.
DR GO; GO:0004629; F:phospholipase C activity; IDA:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0009553; P:embryo sac development; IMP:TAIR.
DR GO; GO:0048437; P:floral organ development; IMP:TAIR.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009556; P:microsporogenesis; IMP:TAIR.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0010601; P:positive regulation of auxin biosynthetic process; IMP:TAIR.
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; 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; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 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; Cell membrane; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Phosphoprotein; Reference proteome; Transducer.
FT CHAIN 1..581
FT /note="Phosphoinositide phospholipase C 2"
FT /id="PRO_0000324127"
FT DOMAIN 26..102
FT /note="EF-hand-like"
FT DOMAIN 103..248
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 317..433
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 434..563
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 279..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
SQ SEQUENCE 581 AA; 66122 MW; E337EB95EC16FC0B CRC64;
MSKQTYKVCF CFRRRFRYTA SEAPREIKTI FEKYSENGVM TVDHLHRFLI DVQKQDKATR
EDAQSIINSA SSLLHRNGLH LDAFFKYLFG DNNPPLALHK VHHDMDAPIS HYFIFTGHNS
YLTGNQLSSD CSEVPIIDAL KKGVRVIELD IWPNSNKDDI DVLHGMTLTT PVGLIKCLKA
IRAHAFDVSD YPVVVTLEDH LTPDLQSKVA EMVTEIFGEI LFTPPVGESL KEFPSPNSLK
RRIIISTKPP KEYKEGKDVE VVQKGKDLGD EEVWGREVPS FIQRNKSEAK DDLDGNDDDD
DDDDEDKSKI NAPPQYKHLI AIHAGKPKGG ITECLKVDPD KVRRLSLSEE QLEKAAEKYA
KQIVRFTQHN LLRIYPKGTR VTSSNYNPLV GWSHGAQMVA FNMQGYGRSL WLMQGMFRAN
GGCGYIKKPD LLLKSGSDSD IFDPKATLPV KTTLRVTVYM GEGWYFDFRH THFDQYSPPD
FYTRVGIAGV PGDTVMKKTK TLEDNWIPAW DEVFEFPLTV PELALLRLEV HEYDMSEKDD
FGGQTCLPVW ELSEGIRAFP LHSRKGEKYK SVKLLVKVEF V
