PLP1_ARATH
ID PLP1_ARATH Reviewed; 414 AA.
AC O23179; F4JR94; O23148; Q8LBT5;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Patatin-like protein 1;
DE Short=AtPLP1;
DE EC=3.1.1.-;
DE AltName: Full=Patatin-related phospholipase A IIgamma;
DE Short=pPLAIIg;
DE AltName: Full=Phospholipase A IVA;
DE Short=AtPLAIVA;
GN Name=PLP1; OrderedLocusNames=At4g37070; ORFNames=AP22.83, C7A10.290;
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-414 (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=10094464; DOI=10.1016/s0014-5793(99)00097-6;
RA Terryn N., Heijnen L., De Keyser A., Van Asseldonck M., De Clercq R.,
RA Verbakel H., Gielen J., Zabeau M., Villarroel R., Jesse T., Neyt P.,
RA Hogers R., Van Den Daele H., Ardiles W., Schueller C., Mayer K.F.X.,
RA Dehais P., Rombauts S., Van Montagu M., Rouze P., Vos P.;
RT "Evidence for an ancient chromosomal duplication in Arabidopsis thaliana by
RT sequencing and analyzing a 400-kb contig at the APETALA2 locus on
RT chromosome 4.";
RL FEBS Lett. 445:237-245(1999).
RN [7]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
RP 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 [8]
RP FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-399, AND DISRUPTION
RP 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:12226489,
CC ECO:0000269|PubMed:20053799}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:12226489};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12226489}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O23179-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O23179-2; Sequence=VSP_053856;
CC -!- TISSUE SPECIFICITY: Expressed specifically in roots and root hairs.
CC {ECO:0000269|PubMed:12226489, 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 -!- PTM: Phosphorylated at Ser-399 by CPK3. Phosphorylation enhances PLP1
CC activity towards phosphatidylcholine. {ECO:0000269|PubMed:20053799}.
CC -!- DISRUPTION PHENOTYPE: Decreased number of lateral roots.
CC {ECO:0000269|PubMed:20053799}.
CC -!- SIMILARITY: Belongs to the patatin family. {ECO:0000305}.
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DR EMBL; Z99707; CAB16787.1; -; Genomic_DNA.
DR EMBL; AL161590; CAB80373.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86744.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86745.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86746.1; -; Genomic_DNA.
DR EMBL; BT029750; ABM06020.1; -; mRNA.
DR EMBL; AY087005; AAM64566.1; -; mRNA.
DR EMBL; AJ002596; CAA05628.1; -; mRNA.
DR PIR; H85437; H85437.
DR PIR; T52294; T52294.
DR RefSeq; NP_568015.1; NM_119870.2. [O23179-2]
DR RefSeq; NP_849511.1; NM_179180.3. [O23179-1]
DR RefSeq; NP_849512.3; NM_179181.3. [O23179-2]
DR AlphaFoldDB; O23179; -.
DR SMR; O23179; -.
DR BioGRID; 15142; 3.
DR STRING; 3702.AT4G37070.2; -.
DR iPTMnet; O23179; -.
DR PaxDb; O23179; -.
DR PRIDE; O23179; -.
DR ProteomicsDB; 234674; -. [O23179-1]
DR EnsemblPlants; AT4G37070.1; AT4G37070.1; AT4G37070. [O23179-2]
DR EnsemblPlants; AT4G37070.2; AT4G37070.2; AT4G37070. [O23179-1]
DR EnsemblPlants; AT4G37070.3; AT4G37070.3; AT4G37070. [O23179-2]
DR GeneID; 829861; -.
DR Gramene; AT4G37070.1; AT4G37070.1; AT4G37070. [O23179-2]
DR Gramene; AT4G37070.2; AT4G37070.2; AT4G37070. [O23179-1]
DR Gramene; AT4G37070.3; AT4G37070.3; AT4G37070. [O23179-2]
DR KEGG; ath:AT4G37070; -.
DR Araport; AT4G37070; -.
DR TAIR; locus:2114995; AT4G37070.
DR eggNOG; KOG0513; Eukaryota.
DR InParanoid; O23179; -.
DR OMA; FDKFLVI; -.
DR PhylomeDB; O23179; -.
DR BRENDA; 3.1.1.23; 399.
DR PRO; PR:O23179; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23179; baseline and differential.
DR Genevisible; O23179; 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:0010311; P:lateral root formation; IMP:TAIR.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Hydrolase; Lipid degradation;
KW Lipid metabolism; Phosphoprotein; Plant defense; Reference proteome.
FT CHAIN 1..414
FT /note="Patatin-like protein 1"
FT /id="PRO_0000425813"
FT DOMAIN 22..228
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 26..31
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 64..68
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 215..217
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 66
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 215
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20053799"
FT VAR_SEQ 384..414
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_053856"
FT CONFLICT 359
FT /note="M -> V (in Ref. 5; AAM64566)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 414 AA; 45824 MW; 078E35777043AF43 CRC64;
MENKSPSKKN KPPSCGSLVT ILSLDGGGVR GIIAGVILAF LEKQLQELDG EEARLADYFD
VIAGTSTGGL VTAMLTVPDE TGRPHFAAKD IVPFYLEHCP KIFPQPTGVL ALLPKLPKLL
SGPKYSGKYL RNLLSKLLGE TRLHQTLTNI VIPTFDIKKL QPTIFSSYQL LVDPSLDVKV
SDICIGTSAA PTFFPPHYFS NEDSQGNKTE FNLVDGAVTA NNPTLVAMTA VSKQIVKNNP
DMGKLKPLGF DRFLVISIGT GSTKREEKYS AKKAAKWGII SWLYDDGSTP ILDITMESSR
DMIHYHSSVV FKALQSEDKY LRIDDDTLEG DVSTMDLATK SNLENLQKIG EKMLTNRVMQ
MNIDTGVYEP VAENITNDEQ LKRYAKILSD ERKLRRLRSD TMIKDSSNES QEIK
