NPC4_ARATH
ID NPC4_ARATH Reviewed; 538 AA.
AC Q9SRQ7;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Non-specific phospholipase C4;
DE EC=3.1.4.3;
GN Name=NPC4; OrderedLocusNames=At3g03530; ORFNames=T21P5.5;
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, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, INDUCTION BY PHOSPHATE DEPRIVATION, AND DISRUPTION PHENOTYPE.
RX PubMed=15618226; DOI=10.1074/jbc.m408799200;
RA Nakamura Y., Awai K., Masuda T., Yoshioka Y., Takamiya K., Ohta H.;
RT "A novel phosphatidylcholine-hydrolyzing phospholipase C induced by
RT phosphate starvation in Arabidopsis.";
RL J. Biol. Chem. 280:7469-7476(2005).
RN [2]
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 [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].
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 FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20507939; DOI=10.1093/mp/ssq005;
RA Wimalasekera R., Pejchar P., Holk A., Martinec J., Scherer G.F.;
RT "Plant phosphatidylcholine-hydrolyzing phospholipases C NPC3 and NPC4 with
RT roles in root development and brassinolide signaling in Arabidopsis
RT thaliana.";
RL Mol. Plant 3:610-625(2010).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20699393; DOI=10.1105/tpc.109.071720;
RA Peters C., Li M., Narasimhan R., Roth M., Welti R., Wang X.;
RT "Nonspecific phospholipase C NPC4 promotes responses to abscisic acid and
RT tolerance to hyperosmotic stress in Arabidopsis.";
RL Plant Cell 22:2642-2659(2010).
RN [7]
RP FUNCTION, INDUCTION BY SALT, AND DISRUPTION PHENOTYPE.
RX PubMed=21525137; DOI=10.1093/jxb/err039;
RA Kocourkova D., Krckova Z., Pejchar P., Veselkova S., Valentova O.,
RA Wimalasekera R., Scherer G.F., Martinec J.;
RT "The phosphatidylcholine-hydrolysing phospholipase C NPC4 plays a role in
RT response of Arabidopsis roots to salt stress.";
RL J. Exp. Bot. 62:3753-3763(2011).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=23432399; DOI=10.1111/nph.12194;
RA Chandrika N.N., Sundaravelpandian K., Yu S.M., Schmidt W.;
RT "ALFIN-LIKE 6 is involved in root hair elongation during phosphate
RT deficiency in Arabidopsis.";
RL New Phytol. 198:709-720(2013).
CC -!- FUNCTION: Non-specific phospholipase C (PLC) which assumes major PLC
CC activity during inorganic phosphate starvation. Substrate preference is
CC phosphatidylcholine (PC), but can also hydrolyze
CC phosphatidylethanolamine (PE) with lower efficiency. Has no activity
CC toward phosphatidic acid (PA). Plays an important role in the supply of
CC both inorganic phosphate and diacylglycerol from membrane-localized
CC phospholipids during phosphate deprivation. May be required for lipid-
CC derived signaling molecules that positively modulate abscisic acid
CC (ABA) response and promote plant tolerance to drought and salt
CC stresses. May be involved in brassinolide-mediated signaling in root
CC development. {ECO:0000269|PubMed:15618226, ECO:0000269|PubMed:20507939,
CC ECO:0000269|PubMed:20699393, ECO:0000269|PubMed:21525137}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:10604,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:295975; EC=3.1.4.3;
CC Evidence={ECO:0000269|PubMed:15618226};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15618226};
CC Peripheral membrane protein {ECO:0000305|PubMed:15618226}.
CC -!- TISSUE SPECIFICITY: Expressed in root tips, cotyledons, on leaf
CC margins, stems, young anthers and funiculus.
CC {ECO:0000269|PubMed:20507939}.
CC -!- INDUCTION: Induced by auxin, zeatin, salt and inorganic phosphate
CC deprivation. {ECO:0000269|PubMed:15618226, ECO:0000269|PubMed:20507939,
CC ECO:0000269|PubMed:21525137}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants display decreased ABA sensitivity in seed
CC germination, root elongation, and stomatal movement and have decreased
CC tolerance to high salinity and water deficiency. Root hair elongation
CC defects under low inorganic phosphate conditions.
CC {ECO:0000269|PubMed:15618226, ECO:0000269|PubMed:20507939,
CC ECO:0000269|PubMed:20699393, ECO:0000269|PubMed:21525137,
CC ECO:0000269|PubMed:23432399}.
CC -!- SIMILARITY: Belongs to the bacterial phospholipase C family.
CC {ECO:0000305}.
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DR EMBL; AB084293; BAC22508.1; -; mRNA.
DR EMBL; AC009895; AAF01582.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73954.1; -; Genomic_DNA.
DR EMBL; AY037257; AAK59858.1; -; mRNA.
DR EMBL; AY143947; AAN28886.1; -; mRNA.
DR RefSeq; NP_566206.1; NM_111224.3.
DR AlphaFoldDB; Q9SRQ7; -.
DR SMR; Q9SRQ7; -.
DR BioGRID; 6576; 2.
DR IntAct; Q9SRQ7; 1.
DR STRING; 3702.AT3G03530.1; -.
DR iPTMnet; Q9SRQ7; -.
DR PaxDb; Q9SRQ7; -.
DR PRIDE; Q9SRQ7; -.
DR ProteomicsDB; 251119; -.
DR DNASU; 821243; -.
DR EnsemblPlants; AT3G03530.1; AT3G03530.1; AT3G03530.
DR GeneID; 821243; -.
DR Gramene; AT3G03530.1; AT3G03530.1; AT3G03530.
DR KEGG; ath:AT3G03530; -.
DR Araport; AT3G03530; -.
DR TAIR; locus:2099639; AT3G03530.
DR eggNOG; ENOG502QPJ0; Eukaryota.
DR HOGENOM; CLU_029943_1_0_1; -.
DR InParanoid; Q9SRQ7; -.
DR OMA; FYRNMRQ; -.
DR OrthoDB; 430314at2759; -.
DR PhylomeDB; Q9SRQ7; -.
DR BioCyc; ARA:AT3G03530-MON; -.
DR BioCyc; MetaCyc:AT3G03530-MON; -.
DR BRENDA; 3.1.4.3; 399.
DR PRO; PR:Q9SRQ7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SRQ7; baseline and differential.
DR Genevisible; Q9SRQ7; AT.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0034480; F:phosphatidylcholine phospholipase C activity; IEA:UniProtKB-EC.
DR GO; GO:0004629; F:phospholipase C activity; IDA:TAIR.
DR GO; GO:0009395; P:phospholipid catabolic process; IDA:TAIR.
DR Gene3D; 3.40.720.10; -; 2.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR007312; Phosphoesterase.
DR PANTHER; PTHR31956; PTHR31956; 1.
DR Pfam; PF04185; Phosphoesterase; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Hydrolase; Membrane; Reference proteome; Stress response.
FT CHAIN 1..538
FT /note="Non-specific phospholipase C4"
FT /id="PRO_0000424786"
FT REGION 91..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 538 AA; 60723 MW; B559583CB3B9ACE6 CRC64;
MIETTKGGSG SYPIKTIVVL VQENRSFDHT LGWFKELNRE IDGVTKSDPK SNTVSSSDTN
SLRVVFGDQS QYVNPDPGHS IQDIYEQVFG KPWDSGKPDP NPGHPNMSGF AQNAERNKKG
MSSAVMNGFK PNALPVYKEL VQNFAICDRW FASVPASTQP NRLYVHSATS HGATSNDKKL
LLEGFPQKTI FESLDEAGFS FGIYYQFPPS TLFYRNLRKL KYLTHFHQYG IQFKKDCKEG
KLPNYVVVEQ RWFDLLSTPA NDDHPSHDVS EGQKLVKEVY EALRSSPQWN EILFIITYDE
HGGFYDHVPT PVDGVPNPDG ILGPPPYNFE FNRLGVRVPT FFISPWIEPG TVIHGPNGPY
PRSQYEHSSI PATVKTIFKL KDFLSKRDSW AGTFESVITR DSPRQDCPET LSTPIKLRGT
MAKENAQLSE FQEDLVIMAA GLKGDYKNEE LIHKLCKETC VADASKYVTN AFEKFLEESR
KARDRGCDEN DIVYCVDDDD DHVVIPPQSH SEASNAAAQP KTQTSFFNKL FSCFIRHD
