PLCD1_ARATH
ID PLCD1_ARATH Reviewed; 561 AA.
AC Q39032; O49970;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Phosphoinositide phospholipase C 1;
DE EC=3.1.4.11;
DE AltName: Full=Phosphoinositide phospholipase PLC1;
DE Short=AtPLC1;
DE Short=AtPLC1S;
DE Short=PI-PLC1;
GN Name=PLC1; Synonyms=ATHATPLC1G; OrderedLocusNames=At5g58670;
GN ORFNames=MZN1.12;
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], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=7732004; DOI=10.1073/pnas.92.9.3903;
RA Hirayama T., Ohto C., Mizoguchi T., Shinozaki K.;
RT "A gene encoding a phosphatidylinositol-specific phospholipase C is induced
RT by dehydration and salt stress in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3903-3907(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. C24;
RX PubMed=9427559; DOI=10.1016/s0378-1119(97)00441-1;
RA Hartweck L.M., Llewellyn D.J., Dennis E.S.;
RT "The Arabidopsis thaliana genome has multiple divergent forms of
RT phosphoinositol-specific phospholipase C1.";
RL Gene 202:151-156(1997).
RN [3]
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 [4]
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 [5]
RP FUNCTION.
RX PubMed=11340187; DOI=10.2307/3871369;
RA Sanchez J.-P., Chua N.-H.;
RT "Arabidopsis PLC1 is required for secondary responses to abscisic acid
RT signals.";
RL Plant Cell 13:1143-1154(2001).
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).
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 Required for secondary responses to abscisic acid signals.
CC {ECO:0000269|PubMed:11340187, ECO:0000269|PubMed:7732004,
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 Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in stems, leaves, roots, flowers and
CC siliques. Predominant in the vascular tissues of roots and leaves.
CC {ECO:0000269|PubMed:7732004, ECO:0000269|Ref.7}.
CC -!- INDUCTION: By abscisic acid, osmotic stress and environmental stresses
CC such as dehydration, salinity and low temperature.
CC {ECO:0000269|PubMed:7732004, ECO:0000269|Ref.7}.
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DR EMBL; D38544; BAA07547.1; -; mRNA.
DR EMBL; U76423; AAC05023.1; -; Genomic_DNA.
DR EMBL; AB020755; BAA97336.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97083.1; -; Genomic_DNA.
DR RefSeq; NP_568881.1; NM_125254.2.
DR AlphaFoldDB; Q39032; -.
DR SMR; Q39032; -.
DR BioGRID; 21225; 1.
DR STRING; 3702.AT5G58670.1; -.
DR iPTMnet; Q39032; -.
DR SwissPalm; Q39032; -.
DR PaxDb; Q39032; -.
DR PRIDE; Q39032; -.
DR ProteomicsDB; 236631; -.
DR EnsemblPlants; AT5G58670.1; AT5G58670.1; AT5G58670.
DR GeneID; 835981; -.
DR Gramene; AT5G58670.1; AT5G58670.1; AT5G58670.
DR KEGG; ath:AT5G58670; -.
DR Araport; AT5G58670; -.
DR TAIR; locus:2178803; AT5G58670.
DR eggNOG; KOG0169; Eukaryota.
DR HOGENOM; CLU_002738_3_2_1; -.
DR InParanoid; Q39032; -.
DR OMA; LFQCTDE; -.
DR OrthoDB; 368239at2759; -.
DR PhylomeDB; Q39032; -.
DR BioCyc; ARA:AT5G58670-MON; -.
DR BioCyc; MetaCyc:MON-1622; -.
DR BRENDA; 3.1.4.11; 399.
DR PRO; PR:Q39032; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q39032; baseline and differential.
DR Genevisible; Q39032; AT.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0009738; P:abscisic acid-activated signaling pathway; TAS:TAIR.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP: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; IPR018247; EF_Hand_1_Ca_BS.
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; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cell membrane; Hydrolase; Lipid degradation; Lipid metabolism;
KW Membrane; Metal-binding; Reference proteome; Transducer.
FT CHAIN 1..561
FT /note="Phosphoinositide phospholipase C 1"
FT /id="PRO_0000324126"
FT DOMAIN 21..54
FT /note="EF-hand"
FT DOMAIN 105..249
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 294..410
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 414..541
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 256..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT BINDING 452
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 452
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 458
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 510
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 510
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 512
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 512
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 518
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT CONFLICT 87
FT /note="R -> G (in Ref. 2; AAC05023)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 561 AA; 64314 MW; A05AD123411352E8 CRC64;
MKESFKVCFC CVRNFKVKSS EPPEEIKNLF HDYSQDDRMS ADEMLRFVIQ VQGETHADIN
YVKDIFHRLK HHGVFHPRGI HLEGFYRYLL SDFNSPLPLT REVWQDMNQP LSHYFLYTGH
NSYLTGNQLN SNSSIEPIVK ALRNGVRVIE LDLWPNSSGK EAEVRHGGTL TSREDLQKCL
NVVKENAFQV SAYPVVLTLE DHLTPILQKK VAKMVSKTFG GSLFQCTDET TECFPSPESL
KNKILISTKP PKEYLQTQIS KGSTTDESTR AKKISDAEEQ VQEEDEESVA IEYRDLISIH
AGNRKGGLKN CLNGDPNRVI RLSMSEQWLE TLAKTRGPDL VKFTQRNLLR IFPKTTRFDS
SNYDPLVGWI HGAQMVAFNM QSHGRYLWMM QGMFKANGGC GYVKKPDVLL SNGPEGEIFD
PCSQNLPIKT TLKVKIYTGE GWNMDFPLDH FDRYSPPDFY AKVGIAGVPL DTASYRTEID
KDEWFPIWDK EFEFPLRVPE LSLLCITVKD YDSNTQNDFA GQTCFPLSEV RPGIRAVRLH
DRAGEVYKHV RLLMRFVLEP R
