PLCD6_ARATH
ID PLCD6_ARATH Reviewed; 613 AA.
AC Q8GV43;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Phosphoinositide phospholipase C 6;
DE EC=3.1.4.11;
DE AltName: Full=Phosphoinositide phospholipase PLC6;
DE Short=AtPLC6;
DE Short=AtPLC8;
DE Short=PI-PLC6;
GN Name=PLC6; Synonyms=PLC8; OrderedLocusNames=At2g40116; ORFNames=F27I1;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 70-613.
RA Tasma I.M., Brendel V., Bhattacharyya M.K.;
RT "Arabidopsis thaliana phosphoinositide-specific phospholipase C 8
RT (AtPLC8).";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP 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.
CC {ECO:0000250}.
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:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, flowers and siliques, but not
CC in roots. {ECO:0000269|Ref.6}.
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; CP002685; AEC09783.1; -; Genomic_DNA.
DR EMBL; BX819512; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY150803; AAN75042.1; -; Genomic_DNA.
DR RefSeq; NP_850327.2; NM_179996.3.
DR AlphaFoldDB; Q8GV43; -.
DR SMR; Q8GV43; -.
DR STRING; 3702.AT2G40116.1; -.
DR PaxDb; Q8GV43; -.
DR PRIDE; Q8GV43; -.
DR ProteomicsDB; 234672; -.
DR EnsemblPlants; AT2G40116.1; AT2G40116.1; AT2G40116.
DR GeneID; 818602; -.
DR Gramene; AT2G40116.1; AT2G40116.1; AT2G40116.
DR KEGG; ath:AT2G40116; -.
DR Araport; AT2G40116; -.
DR TAIR; locus:504956034; AT2G40116.
DR eggNOG; KOG0169; Eukaryota.
DR HOGENOM; CLU_002738_3_2_1; -.
DR InParanoid; Q8GV43; -.
DR OMA; YLTCTLV; -.
DR OrthoDB; 368239at2759; -.
DR PhylomeDB; Q8GV43; -.
DR BioCyc; ARA:AT2G40116-MON; -.
DR BRENDA; 3.1.4.11; 399.
DR PRO; PR:Q8GV43; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8GV43; baseline and differential.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IBA:GO_Central.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
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; 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; 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 2: Evidence at transcript level;
KW Cell membrane; Hydrolase; Lipid degradation; Lipid metabolism; Membrane;
KW Reference proteome; Transducer.
FT CHAIN 1..613
FT /note="Phosphoinositide phospholipase C 6"
FT /id="PRO_0000324131"
FT DOMAIN 137..281
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 349..465
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 466..595
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 288..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 152
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
SQ SEQUENCE 613 AA; 70038 MW; F248C0B821903E6D CRC64;
MGKEKKTESY NNDSGSYNYR MFKFYNRKFK INEVTPTDDV RDAFCQFAVG GGGGGTDGDS
SDGDGSTGVM GAEQLCSFLD DHGESTTVAE AQRLIDEVIR RRHHVTRFTR HGLDLDDFFN
FLFYDDLNPP ITPHVHQDMT APLSHYFIYT GHNSYLTGNQ LSSDCSEVPV IKALQRGVRV
IELDLWPNST GTDINVLHGR TLTTPVPLMK CLKSIRDYAF SSSPYPVIIT LEDHLTPDLQ
AKVAEMATQI FGQMLYYPES DSLLEFPSPA SLLHRIIIST KPPKEYLESR NPIVKQKDNN
VSPSSEDETP RTEEIQTLES MLFDQDFESK SDSDQEDEEA SEDQKPAYKR LITIHAGKPK
GTVKEEMKVV VDKVRRLSLS EQELDRTCSS NSQDVVRFTQ RNLLRIYPKG TRFNSSNYKP
LIGWTHGAQM IAFNMQGYGK SLWLMHGMFR ANGGCGYVKK PNFLMKKGFH DEVFDPRKKL
PVKETLKVKV YMGDGWRMDF SHTHFDAYSP PDFYTKMFIV GVPADNAKKK TKIIEDNWYP
IWDEEFSFPL TVPELALLRI EVREYDMSEK DDFGGQTCLP VAELRPGIRS VPLYDKKGEK
MKSVRLLMRF IFE
