NPC3_ARATH
ID NPC3_ARATH Reviewed; 523 AA.
AC Q9SRQ6; Q8VZ53;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Non-specific phospholipase C3;
DE EC=3.1.3.106 {ECO:0000269|PubMed:20045079};
GN Name=NPC3; OrderedLocusNames=At3g03520; ORFNames=T21P5.6;
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], AND LACK OF INDUCTION BY PHOSPHATE DEPRIVATION.
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, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=20045079; DOI=10.1016/j.bbalip.2009.12.005;
RA Reddy V.S., Rao D.K., Rajasekharan R.;
RT "Functional characterization of lysophosphatidic acid phosphatase from
RT Arabidopsis thaliana.";
RL Biochim. Biophys. Acta 1801:455-461(2010).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY AUXIN, 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).
CC -!- FUNCTION: Possesses specific phosphatase activity toward
CC lysophosphatidic acid (LPA) in vitro. Does not show phospholipase C
CC activity. May play a role in signal transduction and storage lipid
CC synthesis. May be involved in brassinolide-mediated signaling in root
CC development. {ECO:0000269|PubMed:20045079,
CC ECO:0000269|PubMed:20507939}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + H2O = a 1-acyl-sn-glycerol +
CC phosphate; Xref=Rhea:RHEA:33155, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57970, ChEBI:CHEBI:64683;
CC EC=3.1.3.106; Evidence={ECO:0000269|PubMed:20045079};
CC -!- TISSUE SPECIFICITY: Expressed in root tips, cotyledons, on leaf
CC margins, stems, young anthers and funiculus.
CC {ECO:0000269|PubMed:20045079, ECO:0000269|PubMed:20507939}.
CC -!- INDUCTION: Induced by auxin in roots. Not induced by inorganic
CC phosphate deprivation. {ECO:0000269|PubMed:20507939}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:20507939}.
CC -!- SIMILARITY: Belongs to the bacterial phospholipase C family.
CC {ECO:0000305}.
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DR EMBL; AB084295; BAC22510.1; -; mRNA.
DR EMBL; AC009895; AAF01583.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73953.1; -; Genomic_DNA.
DR EMBL; AY065242; AAL38718.1; -; mRNA.
DR EMBL; AY150477; AAN13002.1; -; mRNA.
DR RefSeq; NP_187002.1; NM_111223.5.
DR AlphaFoldDB; Q9SRQ6; -.
DR SMR; Q9SRQ6; -.
DR BioGRID; 6577; 1.
DR IntAct; Q9SRQ6; 1.
DR STRING; 3702.AT3G03520.1; -.
DR SwissPalm; Q9SRQ6; -.
DR PaxDb; Q9SRQ6; -.
DR PRIDE; Q9SRQ6; -.
DR ProteomicsDB; 249046; -.
DR EnsemblPlants; AT3G03520.1; AT3G03520.1; AT3G03520.
DR GeneID; 821244; -.
DR Gramene; AT3G03520.1; AT3G03520.1; AT3G03520.
DR KEGG; ath:AT3G03520; -.
DR Araport; AT3G03520; -.
DR TAIR; locus:2099654; AT3G03520.
DR eggNOG; ENOG502QPJ0; Eukaryota.
DR HOGENOM; CLU_029943_1_0_1; -.
DR InParanoid; Q9SRQ6; -.
DR OMA; IKDIYPF; -.
DR OrthoDB; 430314at2759; -.
DR PhylomeDB; Q9SRQ6; -.
DR BioCyc; ARA:AT3G03520-MON; -.
DR BioCyc; MetaCyc:AT3G03520-MON; -.
DR BRENDA; 3.1.4.3; 399.
DR PRO; PR:Q9SRQ6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SRQ6; baseline and differential.
DR Genevisible; Q9SRQ6; AT.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0052642; F:lysophosphatidic acid phosphatase activity; IDA:TAIR.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IEP:TAIR.
DR GO; GO:0006796; P:phosphate-containing compound metabolic process; IDA:TAIR.
DR GO; GO:0009395; P:phospholipid catabolic process; IBA:GO_Central.
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.
PE 1: Evidence at protein level;
KW Hydrolase; Reference proteome.
FT CHAIN 1..523
FT /note="Non-specific phospholipase C3"
FT /id="PRO_0000424785"
FT REGION 44..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 413
FT /note="E -> G (in Ref. 4; AAL38718)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 523 AA; 59097 MW; 31D10D4985C41533 CRC64;
MVEETSSGGG SSASPIKTIV VLVQENRSFD HMLGWFKELN PEIDGVSESE PRSNPLSTSD
PNSAQIFFGK ESQNIDPDPG HSFQAIYEQV FGKPFSDESP YPDPKMNGFV QNAEAITKGM
SEKVVMQGFP PEKLPVFKEL VQEFAVCDRW FSSLPSSTQP NRLYVHAATS NGAFSNDTNT
LVRGFPQRTV FESLEESGFT FGIYYQSFPN CLFYRNMRKL KYVDNFHQYH LSFKRHCKEG
KLPNYVVIEP RYFKILSAPA NDDHPKNDVV EGQNLVKEIY EALRASPQWN EILFVVVYDE
HGGYYDHVPT PVIGVPNPDG LVGPEPYNFK FDRLGVRVPA LLISPWIEPG TVLHEPNGPE
PTSQFEHSSI PATLKKIFNL KSFLTKRDEW AGTLDAVINR TSPRTDCPVT LPELPRARDI
DIGTQEEDED LTDFQIELIQ AAAVLKGDHI KDIYPFKLAD KMKVLDAARY VEEAFTRFHG
ESKKAKEEGR DEHEIVDLSK GSTRHSTPKS FVQKLFSCLI CDN
