PLCD9_ARATH
ID PLCD9_ARATH Reviewed; 531 AA.
AC Q6NMA7; Q9SD51;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Phosphoinositide phospholipase C 9;
DE EC=3.1.4.11;
DE AltName: Full=Phosphoinositide phospholipase PLC9;
DE Short=AtPLC9;
DE Short=PI-PLC9;
GN Name=PLC9; OrderedLocusNames=At3g47220; ORFNames=F13I12.270;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) 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, roots, flowers and siliques.
CC {ECO:0000269|Ref.6}.
CC -!- CAUTION: Contains substitutions of several amino acids thought to be
CC essential for catalytic activity. Its enzyme activity is therefore
CC unsure. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB61968.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL133292; CAB61968.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78257.1; -; Genomic_DNA.
DR EMBL; BT011755; AAS49118.1; -; mRNA.
DR EMBL; AK226689; BAE98796.1; -; mRNA.
DR PIR; T45658; T45658.
DR RefSeq; NP_190306.2; NM_114589.5.
DR AlphaFoldDB; Q6NMA7; -.
DR SMR; Q6NMA7; -.
DR BioGRID; 9195; 13.
DR IntAct; Q6NMA7; 13.
DR STRING; 3702.AT3G47220.1; -.
DR PaxDb; Q6NMA7; -.
DR PRIDE; Q6NMA7; -.
DR ProteomicsDB; 235069; -.
DR EnsemblPlants; AT3G47220.1; AT3G47220.1; AT3G47220.
DR GeneID; 823875; -.
DR Gramene; AT3G47220.1; AT3G47220.1; AT3G47220.
DR KEGG; ath:AT3G47220; -.
DR Araport; AT3G47220; -.
DR TAIR; locus:2075696; AT3G47220.
DR eggNOG; KOG0169; Eukaryota.
DR HOGENOM; CLU_002738_3_2_1; -.
DR InParanoid; Q6NMA7; -.
DR OrthoDB; 368239at2759; -.
DR PhylomeDB; Q6NMA7; -.
DR BioCyc; ARA:AT3G47220-MON; -.
DR BRENDA; 3.1.4.11; 399.
DR PRO; PR:Q6NMA7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q6NMA7; baseline and differential.
DR Genevisible; Q6NMA7; AT.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IMP:TAIR.
DR GO; GO:0055074; P:calcium ion homeostasis; IMP:TAIR.
DR GO; GO:0010286; P:heat acclimation; IMP:TAIR.
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; 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; 2.
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; 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 Phosphoprotein; Reference proteome; Transducer.
FT CHAIN 1..531
FT /note="Phosphoinositide phospholipase C 9"
FT /id="PRO_0000324134"
FT DOMAIN 107..253
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 265..385
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 386..513
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LY51"
SQ SEQUENCE 531 AA; 61165 MW; 44297407ACADA151 CRC64;
MVNLRKKFEM KQANQPGRVP NYFRNKYHGY DDDMPNLLPT FIKLLDTEKD EDGAGLNAAE
QIDRELKSRK CDILKFRNLT ILELPHLNEF LFSTELNPPI SDQVRHRDMN APLSHYFIHT
SLKSYFTGNN VFGRLYSIEP IIDALKQGVR VVELDLLPFG KDGICVRPKW NFEKPLELQE
CLDAIKQHAF TPTRSYPVII TIKDSLKPDL QSKVTQMIDQ TFGDMVYHED PQQSLEEFPS
PAELQNKILI SRRPPTKLLY AKAVENGVEL EIQEGSTDKN YQSVVGFHAV EPRGMLQKAL
TDDVQQPGWY ERDVISFTQN KFLRTRPKKR NLLSNPPYKP QRAWMHGAQM IALSRQDDKE
KLWLMQGMFR ANGGCGYVKK PNFLLNAGSS GVFYPTENPV VVKTLKVKIY MGDGWIVDFK
KRIGRLSKPD LYVRISIAGV PHDEKIMNTT VKNNEWKPTW GEEFTFPLTY PDLALISFEV
YDYEVSTPDY FCGQTCLPVS ELIEGIRAVP LYDERGKACS STMLLTRFKW S
