PLCD4_ARATH
ID PLCD4_ARATH Reviewed; 597 AA.
AC Q944C1; Q2V2X4; Q940R9; Q9LUY9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Phosphoinositide phospholipase C 4;
DE EC=3.1.4.11;
DE AltName: Full=Phosphoinositide phospholipase PLC4;
DE Short=AtPLC4;
DE Short=PI-PLC4;
GN Name=PLC4; Synonyms=ATHATPLC5; OrderedLocusNames=At5g58700;
GN ORFNames=MZN1.19;
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] (ISOFORM 1).
RA Ren D., Bhattacharyya M.K.;
RT "Arabidopsis thaliana phosphoinositide specific phospholipase C.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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] (ISOFORM 1).
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 [MRNA] OF 7-597 (ISOFORM 1).
RA Pical C.;
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP FUNCTION, 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).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=17142056; DOI=10.1016/j.pep.2006.10.007;
RA Cao Z., Zhang J., Li Y., Xu X., Liu G., Bhattacharrya M.K., Yang H.,
RA Ren D.;
RT "Preparation of polyclonal antibody specific for AtPLC4, an Arabidopsis
RT phosphatidylinositol-specific phospholipase C in rabbits.";
RL Protein Expr. Purif. 52:306-312(2007).
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:0000269|Ref.7}.
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: Cytoplasm, cytosol {ECO:0000269|PubMed:17142056}.
CC Cell membrane {ECO:0000269|PubMed:17142056}; Peripheral membrane
CC protein {ECO:0000269|PubMed:17142056}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q944C1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q944C1-2; Sequence=VSP_032147, VSP_032148;
CC -!- TISSUE SPECIFICITY: Low expression in leaves, roots, flowers and
CC siliques. Expressed in pollen and in cells of the stigma surface.
CC {ECO:0000269|Ref.7}.
CC -!- INDUCTION: By environmental stresses such as dehydration, salinity and
CC low temperature. {ECO:0000269|Ref.7}.
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DR EMBL; AF434168; AAL30749.2; -; mRNA.
DR EMBL; AB020755; BAA97338.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97086.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97087.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70550.1; -; Genomic_DNA.
DR EMBL; AY093217; AAM13216.1; -; mRNA.
DR EMBL; BT008358; AAP37717.1; -; mRNA.
DR EMBL; AY053422; AAL23439.1; -; mRNA.
DR RefSeq; NP_001032097.1; NM_001037020.2. [Q944C1-2]
DR RefSeq; NP_001318832.1; NM_001345319.1. [Q944C1-1]
DR RefSeq; NP_200678.2; NM_125257.3. [Q944C1-1]
DR AlphaFoldDB; Q944C1; -.
DR SMR; Q944C1; -.
DR BioGRID; 21228; 1.
DR STRING; 3702.AT5G58700.1; -.
DR iPTMnet; Q944C1; -.
DR PaxDb; Q944C1; -.
DR PRIDE; Q944C1; -.
DR ProteomicsDB; 234728; -. [Q944C1-1]
DR EnsemblPlants; AT5G58700.1; AT5G58700.1; AT5G58700. [Q944C1-1]
DR EnsemblPlants; AT5G58700.2; AT5G58700.2; AT5G58700. [Q944C1-2]
DR EnsemblPlants; AT5G58700.3; AT5G58700.3; AT5G58700. [Q944C1-1]
DR GeneID; 835984; -.
DR Gramene; AT5G58700.1; AT5G58700.1; AT5G58700. [Q944C1-1]
DR Gramene; AT5G58700.2; AT5G58700.2; AT5G58700. [Q944C1-2]
DR Gramene; AT5G58700.3; AT5G58700.3; AT5G58700. [Q944C1-1]
DR KEGG; ath:AT5G58700; -.
DR Araport; AT5G58700; -.
DR TAIR; locus:2178848; AT5G58700.
DR eggNOG; KOG0169; Eukaryota.
DR InParanoid; Q944C1; -.
DR OMA; SSYRRCT; -.
DR PhylomeDB; Q944C1; -.
DR BioCyc; ARA:AT5G58700-MON; -.
DR BRENDA; 3.1.4.11; 399.
DR PRO; PR:Q944C1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q944C1; baseline and differential.
DR Genevisible; Q944C1; AT.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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; 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 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Cytoplasm; Hydrolase;
KW Lipid degradation; Lipid metabolism; Membrane; Reference proteome;
KW Transducer.
FT CHAIN 1..597
FT /note="Phosphoinositide phospholipase C 4"
FT /id="PRO_0000324129"
FT DOMAIN 26..60
FT /note="EF-hand"
FT DOMAIN 114..257
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 333..449
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 449..579
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 259..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 174
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT VAR_SEQ 1..108
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_032147"
FT VAR_SEQ 109..111
FT /note="ADQ -> MFL (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_032148"
SQ SEQUENCE 597 AA; 68038 MW; 176D1715653AF82B CRC64;
MEGKKEMGSY KFCLIFTRKF RMTESGPVED VRDLFEKYTE GDAHMSPEQL QKLMTEEGGE
GETSLEEAER IVDEVLRRKH HIAKFTRRNL TLDDFNYYLF STDLNPPIAD QVHQNMDAPL
SHYFIFTGHN SYLTGNQLSS NCSELPIADA LRRGVRVVEL DLWPRGTDDV CVKHGRTLTK
EVKLGKCLES IKANAFAISK YPVIITLEDH LTPKLQFKVA KMITQTFGDM LYYHDSQGCQ
EFPSPEELKE KILISTKPPK EYLEANDTKE KDNGEKGKDS DEDVWGKEPE DLISTQSDLD
KVTSSVNDLN QDDEERGSCE SDTSCQLQAP EYKRLIAIHA GKPKGGLRMA LKVDPNKIRR
LSLSEQLLEK AVASYGADVI RFTQKNFLRI YPKGTRFNSS NYKPQIGWMS GAQMIAFNMQ
GYGRALWLME GMFRANGGCG YVKKPDFLMD ASPNGQDFYP KDNSSPKKTL KVKVCMGDGW
LLDFKKTHFD SYSPPDFFVR VGIAGAPVDE VMEKTKIEYD TWTPIWNKEF TFPLAVPELA
LLRVEVHEHD VNEKDDFGGQ TCLPVSEIRQ GIRAVPLFNR KGVKYSSTRL LMRFEFV
