PLP3_ARATH
ID PLP3_ARATH Reviewed; 428 AA.
AC O23181; Q8L3P2;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Patatin-like protein 3;
DE Short=AtPLP3;
DE EC=3.1.1.-;
DE AltName: Full=Patatin-related phospholipase A IIbeta;
DE Short=pPLAIIb;
DE AltName: Full=Phospholipase A IVC;
DE Short=AtPLAIVC;
GN Name=PLP3; OrderedLocusNames=At4g37050; ORFNames=AP22.16, C7A10.310;
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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] OF 9-428 AND 90-428.
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 SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12226489; DOI=10.1104/pp.006288;
RA Holk A., Rietz S., Zahn M., Quader H., Scherer G.F.;
RT "Molecular identification of cytosolic, patatin-related phospholipases A
RT from Arabidopsis with potential functions in plant signal transduction.";
RL Plant Physiol. 130:90-101(2002).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20053799; DOI=10.1093/mp/ssp109;
RA Rietz S., Dermendjiev G., Oppermann E., Tafesse F.G., Effendi Y., Holk A.,
RA Parker J.E., Teige M., Scherer G.F.;
RT "Roles of Arabidopsis patatin-related phospholipases A in root development
RT are related to auxin responses and phosphate deficiency.";
RL Mol. Plant 3:524-538(2010).
CC -!- FUNCTION: Possesses non-specific lipolytic acyl hydrolase (LAH)
CC activity. Catalyzes the hydrolysis of the neutral lipids
CC monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG)
CC and phosphatidylglycerol (PG), and less efficiently the polar lipids
CC phosphatidylcholine (PC) and phosphatidylinositol (PI), but not the
CC storage lipid triacylglycerol (TAG). May play a role in root
CC development. {ECO:0000269|PubMed:20053799}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12226489}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in the stigma, ovary and
CC funiculus of the ovary. {ECO:0000269|PubMed:12226489,
CC ECO:0000269|PubMed:20053799}.
CC -!- INDUCTION: By abscisic acid (ABA) or phosphate deficiency in roots.
CC {ECO:0000269|PubMed:20053799}.
CC -!- DOMAIN: The nitrogen atoms of the two glycine residues in the GGXR
CC motif define the oxyanion hole, and stabilize the oxyanion that forms
CC during the nucleophilic attack by the catalytic serine during substrate
CC cleavage. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants exhibit an impaired response to phosphate
CC deficiency during root development. {ECO:0000269|PubMed:20053799}.
CC -!- SIMILARITY: Belongs to the patatin family. {ECO:0000305}.
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DR EMBL; Z99707; CAB16789.1; -; Genomic_DNA.
DR EMBL; AL161590; CAB80371.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86741.1; -; Genomic_DNA.
DR EMBL; AY099596; AAM20447.1; -; mRNA.
DR EMBL; AY128840; AAM91240.1; -; mRNA.
DR PIR; F85437; F85437.
DR RefSeq; NP_195422.3; NM_119868.3.
DR AlphaFoldDB; O23181; -.
DR SMR; O23181; -.
DR STRING; 3702.AT4G37050.1; -.
DR PaxDb; O23181; -.
DR PRIDE; O23181; -.
DR ProteomicsDB; 234921; -.
DR EnsemblPlants; AT4G37050.1; AT4G37050.1; AT4G37050.
DR GeneID; 829859; -.
DR Gramene; AT4G37050.1; AT4G37050.1; AT4G37050.
DR KEGG; ath:AT4G37050; -.
DR Araport; AT4G37050; -.
DR TAIR; locus:2115065; AT4G37050.
DR eggNOG; KOG0513; Eukaryota.
DR HOGENOM; CLU_000288_144_0_1; -.
DR InParanoid; O23181; -.
DR OMA; HYFENND; -.
DR OrthoDB; 1209603at2759; -.
DR PhylomeDB; O23181; -.
DR BRENDA; 3.1.1.23; 399.
DR PRO; PR:O23181; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23181; baseline and differential.
DR Genevisible; O23181; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0047372; F:acylglycerol lipase activity; IDA:UniProtKB.
DR GO; GO:0004620; F:phospholipase activity; IDA:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009737; P:response to abscisic acid; IDA:TAIR.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002641; PNPLA_dom.
DR Pfam; PF01734; Patatin; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR PROSITE; PS51635; PNPLA; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Lipid degradation; Lipid metabolism; Phosphoprotein;
KW Plant defense; Reference proteome.
FT CHAIN 1..428
FT /note="Patatin-like protein 3"
FT /id="PRO_0000425815"
FT DOMAIN 38..252
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 42..47
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 80..84
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 239..241
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 82
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 239
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O23179"
SQ SEQUENCE 428 AA; 47204 MW; 0EF73611D4940B84 CRC64;
MDTERGSISS SEISRTAHLQ DRTVACLPPS YGQLVTILSI DGGGIRGIIP GTILAYLESQ
LQELDGEEAR LVDYFDVISG TSTGGLIVAM LTAQDQSGGH SRNSNRPLFE AKEIVPFYLK
HSPKIFPQPR GIFCGWGETI VRLVGGPKFN GKYLHDLVEG FLGDTKLTQS LTNVVIPCFD
IKKLQPVIFS SYQAVNNQAM NAKLSDICIS TSAAPTFFPA HRFTNEDSEG IKHEFNLIDG
GIAANNPTLC AIAEVTKQII KKNPVMGDIS PLDFTRFLVI SIGTGSIRNQ EKYNAKMASK
WGLMCWVFES GSTPILDCYS EAIHDMVDYQ SSVVFQALRS EKNYLRIDDD SLKGDLGSVD
ISTEKNMEGL VEVGEALLKK RVSRVNLESG HYQPISENVT NEEALKRFAK VLSEERKLRE
SRSPKLKI
