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Phosphoinositide phospholipase C 4 (EC 3.1.4.11) (Phosphoinositide phospholipase PLC4) (AtPLC4) (PI-PLC4)

 PLCD4_ARATH             Reviewed;         597 AA.
Q944C1; Q2V2X4; Q940R9; Q9LUY9;
18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 2.
25-OCT-2017, entry version 131.
RecName: Full=Phosphoinositide phospholipase C 4;
EC=3.1.4.11;
AltName: Full=Phosphoinositide phospholipase PLC4;
Short=AtPLC4;
Short=PI-PLC4;
Name=PLC4; Synonyms=ATHATPLC5; OrderedLocusNames=At5g58700;
ORFNames=MZN1.19;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Ren D., Bhattacharyya M.K.;
"Arabidopsis thaliana phosphoinositide specific phospholipase C.";
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10718197; DOI=10.1093/dnares/7.1.31;
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
features of the regions of 3,076,755 bp covered by sixty P1 and TAC
clones.";
DNA Res. 7:31-63(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 7-597 (ISOFORM 1).
Pical C.;
Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
[6]
GENE FAMILY, AND NOMENCLATURE.
PubMed=12226484; DOI=10.1104/pp.004770;
Mueller-Roeber B., Pical C.;
"Inositol phospholipid metabolism in Arabidopsis. Characterized and
putative isoforms of inositol phospholipid kinase and
phosphoinositide-specific phospholipase C.";
Plant Physiol. 130:22-46(2002).
[7]
FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
AGRICOLA=IND43668249; DOI=10.1111/j.1469-8137.2004.01069.x;
Hunt L., Otterhag L., Lee J.C., Lasheen T., Hunt J., Seki M.,
Shinozaki K., Sommarin M., Gilmour D.J., Pical C., Gray J.E.;
"Gene-specific expression and calcium activation of Arabidopsis
thaliana phospholipase C isoforms.";
New Phytol. 162:643-654(2004).
[8]
SUBCELLULAR LOCATION.
PubMed=17142056; DOI=10.1016/j.pep.2006.10.007;
Cao Z., Zhang J., Li Y., Xu X., Liu G., Bhattacharrya M.K., Yang H.,
Ren D.;
"Preparation of polyclonal antibody specific for AtPLC4, an
Arabidopsis phosphatidylinositol-specific phospholipase C in
rabbits.";
Protein Expr. Purif. 52:306-312(2007).
-!- FUNCTION: The production of the second messenger molecules
diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is
mediated by activated phosphatidylinositol-specific phospholipase
C enzymes. {ECO:0000269|Ref.7}.
-!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 4,5-
bisphosphate + H(2)O = 1D-myo-inositol 1,4,5-trisphosphate +
diacylglycerol.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:17142056}. Cell membrane
{ECO:0000269|PubMed:17142056}; Peripheral membrane protein
{ECO:0000269|PubMed:17142056}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q944C1-1; Sequence=Displayed;
Name=2;
IsoId=Q944C1-2; Sequence=VSP_032147, VSP_032148;
Note=Derived from EST data. No experimental confirmation
available.;
-!- TISSUE SPECIFICITY: Low expression in leaves, roots, flowers and
siliques. Expressed in pollen and in cells of the stigma surface.
{ECO:0000269|Ref.7}.
-!- INDUCTION: By environmental stresses such as dehydration, salinity
and low temperature. {ECO:0000269|Ref.7}.
-----------------------------------------------------------------------
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EMBL; AF434168; AAL30749.2; -; mRNA.
EMBL; AB020755; BAA97338.1; -; Genomic_DNA.
EMBL; CP002688; AED97086.1; -; Genomic_DNA.
EMBL; CP002688; AED97087.1; -; Genomic_DNA.
EMBL; CP002688; ANM70550.1; -; Genomic_DNA.
EMBL; AY093217; AAM13216.1; -; mRNA.
EMBL; BT008358; AAP37717.1; -; mRNA.
EMBL; AY053422; AAL23439.1; -; mRNA.
RefSeq; NP_001032097.1; NM_001037020.2. [Q944C1-2]
RefSeq; NP_001318832.1; NM_001345319.1. [Q944C1-1]
RefSeq; NP_200678.2; NM_125257.3. [Q944C1-1]
UniGene; At.26665; -.
ProteinModelPortal; Q944C1; -.
SMR; Q944C1; -.
BioGrid; 21228; 1.
STRING; 3702.AT5G58700.1; -.
iPTMnet; Q944C1; -.
PaxDb; Q944C1; -.
EnsemblPlants; AT5G58700.1; AT5G58700.1; AT5G58700. [Q944C1-1]
EnsemblPlants; AT5G58700.2; AT5G58700.2; AT5G58700. [Q944C1-2]
EnsemblPlants; AT5G58700.3; AT5G58700.3; AT5G58700. [Q944C1-1]
GeneID; 835984; -.
Gramene; AT5G58700.1; AT5G58700.1; AT5G58700.
Gramene; AT5G58700.2; AT5G58700.2; AT5G58700.
Gramene; AT5G58700.3; AT5G58700.3; AT5G58700.
KEGG; ath:AT5G58700; -.
Araport; AT5G58700; -.
TAIR; locus:2178848; AT5G58700.
eggNOG; KOG0169; Eukaryota.
eggNOG; ENOG410XPSW; LUCA.
HOGENOM; HOG000244119; -.
InParanoid; Q944C1; -.
KO; K05857; -.
OMA; TEFDPIT; -.
OrthoDB; EOG0936050V; -.
PhylomeDB; Q944C1; -.
BioCyc; ARA:AT5G58700-MONOMER; -.
BRENDA; 3.1.4.11; 399.
Reactome; R-ATH-112043; PLC beta mediated events.
Reactome; R-ATH-114604; GPVI-mediated activation cascade.
Reactome; R-ATH-1855204; Synthesis of IP3 and IP4 in the cytosol.
Reactome; R-ATH-202433; Generation of second messenger molecules.
Reactome; R-ATH-399997; Acetylcholine regulates insulin secretion.
Reactome; R-ATH-416476; G alpha (q) signalling events.
Reactome; R-ATH-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
Reactome; R-ATH-5607764; CLEC7A (Dectin-1) signaling.
PRO; PR:Q944C1; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q944C1; baseline and differential.
Genevisible; Q944C1; AT.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-EC.
GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
Gene3D; 2.60.40.150; -; 1.
Gene3D; 3.20.20.190; -; 1.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR001192; PI-PLC_fam.
InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
InterPro; IPR015359; PLC_EF-hand-like.
InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
PANTHER; PTHR10336; PTHR10336; 1.
Pfam; PF00168; C2; 1.
Pfam; PF09279; EF-hand_like; 1.
Pfam; PF00388; PI-PLC-X; 1.
Pfam; PF00387; PI-PLC-Y; 1.
PRINTS; PR00390; PHPHLIPASEC.
SMART; SM00239; C2; 1.
SMART; SM00148; PLCXc; 1.
SMART; SM00149; PLCYc; 1.
SUPFAM; SSF47473; SSF47473; 1.
SUPFAM; SSF49562; SSF49562; 1.
SUPFAM; SSF51695; SSF51695; 1.
PROSITE; PS50004; C2; 1.
PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
2: Evidence at transcript level;
Alternative splicing; Cell membrane; Complete proteome; Cytoplasm;
Hydrolase; Lipid degradation; Lipid metabolism; Membrane;
Reference proteome; Transducer.
CHAIN 1 597 Phosphoinositide phospholipase C 4.
/FTId=PRO_0000324129.
DOMAIN 26 60 EF-hand.
DOMAIN 114 257 PI-PLC X-box. {ECO:0000255|PROSITE-
ProRule:PRU00270}.
DOMAIN 333 449 PI-PLC Y-box. {ECO:0000255|PROSITE-
ProRule:PRU00271}.
DOMAIN 455 562 C2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
ACT_SITE 129 129 {ECO:0000255|PROSITE-ProRule:PRU00270}.
ACT_SITE 174 174 {ECO:0000255|PROSITE-ProRule:PRU00270}.
VAR_SEQ 1 108 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_032147.
VAR_SEQ 109 111 ADQ -> MFL (in isoform 2). {ECO:0000305}.
/FTId=VSP_032148.
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


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