PLCD7_ARATH
ID PLCD7_ARATH Reviewed; 584 AA.
AC Q9LY51;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Phosphoinositide phospholipase C 7;
DE EC=3.1.4.11;
DE AltName: Full=Phosphoinositide phospholipase PLC7;
DE Short=AtPLC10;
DE Short=AtPLC7;
DE Short=PI-PLC7;
GN Name=PLC7; Synonyms=PLC10; OrderedLocusNames=At3g55940;
GN ORFNames=F27K19.120;
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 [MRNA] (ISOFORM 2), FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
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 [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(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, ECO:0000269|Ref.3}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LY51-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LY51-2; Sequence=VSP_032149, VSP_032150;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, roots, flowers and siliques.
CC {ECO:0000269|Ref.3}.
CC -!- MISCELLANEOUS: [Isoform 2]: Potentially inactive. {ECO:0000305}.
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DR EMBL; AL163832; CAB87848.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79459.1; -; Genomic_DNA.
DR PIR; T49206; T49206.
DR RefSeq; NP_191153.1; NM_115452.2. [Q9LY51-1]
DR AlphaFoldDB; Q9LY51; -.
DR SMR; Q9LY51; -.
DR BioGRID; 10076; 1.
DR STRING; 3702.AT3G55940.1; -.
DR iPTMnet; Q9LY51; -.
DR PaxDb; Q9LY51; -.
DR PRIDE; Q9LY51; -.
DR ProteomicsDB; 234920; -. [Q9LY51-1]
DR EnsemblPlants; AT3G55940.1; AT3G55940.1; AT3G55940. [Q9LY51-1]
DR GeneID; 824760; -.
DR Gramene; AT3G55940.1; AT3G55940.1; AT3G55940. [Q9LY51-1]
DR KEGG; ath:AT3G55940; -.
DR Araport; AT3G55940; -.
DR TAIR; locus:2082018; AT3G55940.
DR eggNOG; KOG0169; Eukaryota.
DR HOGENOM; CLU_002738_3_2_1; -.
DR InParanoid; Q9LY51; -.
DR OMA; PETMILN; -.
DR OrthoDB; 368239at2759; -.
DR PhylomeDB; Q9LY51; -.
DR BioCyc; ARA:AT3G55940-MON; -.
DR BRENDA; 3.1.4.11; 399.
DR PRO; PR:Q9LY51; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LY51; baseline and differential.
DR Genevisible; Q9LY51; AT.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Phosphoprotein; Reference proteome; Transducer.
FT CHAIN 1..584
FT /note="Phosphoinositide phospholipase C 7"
FT /id="PRO_0000324132"
FT DOMAIN 26..102
FT /note="EF-hand-like"
FT DOMAIN 103..248
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 323..439
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 433..566
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 285..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..310
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:14506206"
FT VAR_SEQ 212..214
FT /note="MVT -> GNV (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_032149"
FT VAR_SEQ 215..584
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_032150"
SQ SEQUENCE 584 AA; 66462 MW; 16A8C5A402A8BA05 CRC64;
MSKQTYKVCF CFRRRYRHTV SVAPAEIKTL FDNYSDKGLM TTDLLLRFLI DVQKQDKATK
EEAQDIVNAS SSLLHRNGLH LDAFFKYLFA VTNSPLSSLE VHQDMDAPLS HYFIYTGHNS
YLTGNQLSSD CSELPIIEAL KKGVRVIELD IWPNSDEDGI DVLHGRTLTS PVELIKCLRA
IREHAFDVSD YPVVVTLEDH LTPKLQAKVA EMVTDIFGEM LFTPPSGECL KEFPSPAFLK
KRIMISTKPP KEYKAATDDD LVKKGRDLGD KEVWGREVPS FIRRDRSVDK NDSNGDDDDD
DDDDDDDDDG DDKIKKNAPP EYKHLIAIEA GKPKGGITEC LKVDPDKVRR LSLSEEQLEK
ASEKYAKQIV RFTQRNLLRV YPKGTRITSS NYNPLIAWSH GAQMVAFNMQ GLGRSLWVMQ
GMFRGNGGCG YIKKPDLLLK SNAVFDPEAT LPVKTTLRVT IYMGEGWYYD FPHTHFDRYS
PPDFYTRVGI AGVPADTVMK KTKTLEDNWI PAWDEVFEFP LTVPELALLR IEVHEYDMSE
KDDFGGQICL PVWELRQGIR AVPLRNQDGV KCRSVKLLVR LEFV
