NPC5_ARATH
ID NPC5_ARATH Reviewed; 521 AA.
AC Q9S816;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Non-specific phospholipase C5;
DE EC=3.1.4.3;
GN Name=NPC5; OrderedLocusNames=At3g03540; ORFNames=T12J13.18, T21P5.4;
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 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 FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY PHOSPHATE DEPRIVATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=18564386; DOI=10.1111/j.1365-313x.2008.03582.x;
RA Gaude N., Nakamura Y., Scheible W.R., Ohta H., Doermann P.;
RT "Phospholipase C5 (NPC5) is involved in galactolipid accumulation during
RT phosphate limitation in leaves of Arabidopsis.";
RL Plant J. 56:28-39(2008).
RN [5]
RP TISSUE SPECIFICITY.
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: Non-specific phospholipase C (PLC) which assumes minor PLC
CC activity during inorganic phosphate starvation. Can hydrolyze both
CC phosphatidylcholine (PC) and phosphatidylethanolamine (PE). Required
CC for normal accumulation of digalactosyldiacylglycerol (DGDG) during
CC phosphate limitation and may contribute to the conversion of
CC phospholipids to diacylglycerol, the substrate for galactolipid
CC synthesis. {ECO:0000269|PubMed:18564386}.
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 -!- INTERACTION:
CC Q9S816; Q9C9P3: F9E10.24; NbExp=3; IntAct=EBI-25513162, EBI-4427281;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18564386}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in flowers.
CC {ECO:0000269|PubMed:20507939}.
CC -!- INDUCTION: Slightly induced by inorganic phosphate deprivation.
CC {ECO:0000269|PubMed:15618226, ECO:0000269|PubMed:18564386}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants accumulates reduced levels of
CC digalactosyldiacylglycerol (DGDG) during phosphate limitation.
CC {ECO:0000269|PubMed:18564386}.
CC -!- SIMILARITY: Belongs to the bacterial phospholipase C family.
CC {ECO:0000305}.
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DR EMBL; AB084294; BAC22509.1; -; mRNA.
DR EMBL; AC009327; AAF03477.1; -; Genomic_DNA.
DR EMBL; AC009895; AAF01581.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73955.1; -; Genomic_DNA.
DR RefSeq; NP_566207.1; NM_111225.2.
DR AlphaFoldDB; Q9S816; -.
DR SMR; Q9S816; -.
DR BioGRID; 6574; 1.
DR IntAct; Q9S816; 1.
DR STRING; 3702.AT3G03540.1; -.
DR PaxDb; Q9S816; -.
DR PRIDE; Q9S816; -.
DR ProteomicsDB; 248935; -.
DR EnsemblPlants; AT3G03540.1; AT3G03540.1; AT3G03540.
DR GeneID; 821241; -.
DR Gramene; AT3G03540.1; AT3G03540.1; AT3G03540.
DR KEGG; ath:AT3G03540; -.
DR Araport; AT3G03540; -.
DR TAIR; locus:2096384; AT3G03540.
DR eggNOG; ENOG502QPJ0; Eukaryota.
DR HOGENOM; CLU_029943_1_0_1; -.
DR InParanoid; Q9S816; -.
DR OMA; EIVVCET; -.
DR OrthoDB; 430314at2759; -.
DR PhylomeDB; Q9S816; -.
DR BioCyc; ARA:AT3G03540-MON; -.
DR BioCyc; MetaCyc:AT3G03540-MON; -.
DR BRENDA; 3.1.4.3; 399.
DR PRO; PR:Q9S816; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9S816; baseline and differential.
DR Genevisible; Q9S816; AT.
DR GO; GO:0005829; C:cytosol; 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:0016036; P:cellular response to phosphate starvation; IMP:TAIR.
DR GO; GO:0009247; P:glycolipid biosynthetic process; IMP:TAIR.
DR GO; GO:0009395; P:phospholipid catabolic process; IMP: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 Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1..521
FT /note="Non-specific phospholipase C5"
FT /id="PRO_0000424787"
FT REGION 478..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 521 AA; 59071 MW; 1A39ACEF6807B8EF CRC64;
MAETKKGSES YPIKTIVVLV QENRSFDHTL GWFKELNREI DGVMKSDQKF NPGFSSDLNS
HNVVFGDQSQ YVDPNPGHSI RDIYEQVFGK PWDSGHPDPN PGPATMSGFA QNAERKMKGM
SSAVMNGFKP DALPVYKELV QNFAICDRWF ASVPGATQPN RLFIHSATSH GTTNNERKLL
IEGFPQKTIF ESLDEAGFTF GIYYQCFPTT LFYRNLRKLK YLTRFHDYGL QFKKDCKEGN
LPNYVVVEQR WYDLLLNPAN DDHPSHDVSE GQKLVKEVYE ALRSSPQWNE ILFIITYDEH
GGFYDHVPTP LDGVPNPDGI LGPPPYNFEF NRLGVRVPTF FISPWIEPGT VLHGSNGPYL
MSQYEHSSIP ATVKKIFKLK DFLTKRDSWA GTFESVITRN SPRQDCPETL SNPVKMRGTV
AKENAELSDF QEELVIVAAG LKGDYKNEEL LYKLCKKTCV SDASKYVTKA FDKFVEESKK
ARERGGDEND IVFCVDDDDD HNVVKPPPSQ SEPSHATPWS N
