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   24-JAN-2024, entry version 165.
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.Q944C1; -.
DR   iPTMnet; Q944C1; -.
DR   PaxDb; 3702-AT5G58700-1; -.
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; AT5G58700; PLC4.
DR   eggNOG; KOG0169; Eukaryota.
DR   InParanoid; Q944C1; -.
DR   OMA; LAVYCHA; -.
DR   OrthoDB; 882863at2759; -.
DR   PhylomeDB; Q944C1; -.
DR   BioCyc; ARA:AT5G58700-MONOMER; -.
DR   BRENDA; 3.1.4.11; 399.
DR   PRO; PR:Q944C1; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q944C1; baseline and differential.
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; IEA:UniProtKB-EC.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00275; C2_PLC_like; 1.
DR   CDD; cd08599; PI-PLCc_plant; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 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:SF204; PHOSPHOINOSITIDE PHOSPHOLIPASE C 4-RELATED; 1.
DR   PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 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; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
DR   Genevisible; Q944C1; AT.
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
//