PLP5_ARATH
ID PLP5_ARATH Reviewed; 414 AA.
AC O23180;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Patatin-like protein 5;
DE Short=AtPLP5;
DE EC=3.1.1.-;
DE AltName: Full=Patatin-related phospholipase A IIdelta;
DE Short=pPLAIId;
DE AltName: Full=Phospholipase A IVB;
DE Short=AtPLAIVB;
GN Name=PLP5; OrderedLocusNames=At4g37060; ORFNames=AP22.93, C7A10.300;
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 FUNCTION, TISSUE SPECIFICITY, INDUCTION BY AUXIN, PHOSPHORYLATION AT
RP SER-399, 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O23180-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, cotyledons and leaves.
CC {ECO:0000269|PubMed:20053799}.
CC -!- INDUCTION: By auxin. {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 PLP5
CC activity towards phosphatidylcholine. {ECO:0000269|PubMed:20053799}.
CC -!- DISRUPTION PHENOTYPE: Slight decrease in 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; CAB16788.1; -; Genomic_DNA.
DR EMBL; AL161590; CAB80372.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86742.1; -; Genomic_DNA.
DR PIR; G85437; G85437.
DR RefSeq; NP_195423.1; NM_119869.2. [O23180-1]
DR AlphaFoldDB; O23180; -.
DR SMR; O23180; -.
DR STRING; 3702.AT4G37060.2; -.
DR iPTMnet; O23180; -.
DR ProteomicsDB; 234970; -. [O23180-1]
DR EnsemblPlants; AT4G37060.1; AT4G37060.1; AT4G37060. [O23180-1]
DR GeneID; 829860; -.
DR Gramene; AT4G37060.1; AT4G37060.1; AT4G37060. [O23180-1]
DR KEGG; ath:AT4G37060; -.
DR Araport; AT4G37060; -.
DR eggNOG; KOG0513; Eukaryota.
DR PhylomeDB; O23180; -.
DR BRENDA; 3.1.1.23; 399.
DR PRO; PR:O23180; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23180; baseline and differential.
DR Genevisible; O23180; AT.
DR GO; GO:0047372; F:acylglycerol lipase activity; IDA:UniProtKB.
DR GO; GO:0004620; F:phospholipase activity; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0010311; P:lateral root formation; IMP:UniProtKB.
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; Hydrolase; Lipid degradation; Lipid metabolism;
KW Phosphoprotein; Plant defense; Reference proteome.
FT CHAIN 1..414
FT /note="Patatin-like protein 5"
FT /id="PRO_0000425817"
FT DOMAIN 22..228
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 393..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 COMPBIAS 393..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ SEQUENCE 414 AA; 45642 MW; 0A537879893A4A1F CRC64;
MENESPSKKN MPPSCGTLVT ILSLDGGGVR GIIAGVILAY LEKQLQELDG EHVRVADYFD
VIAGTSTGGL VTAMLTAPDE NGRPRFAAKE IVPFYLEHCP KIFPQPTGVL ALLPKLPKLL
SGPKYSGNYL RTTLGKLLGE TKLRQTLTNV VIPTFDIKTL QPTIFSSYQA LTDPSLDVKV
SDICIGTSAA PTYFPPYYFS NEDSQGKTRH FNLVDGGVTA NNPTLVAMTA VTKQIVNNNP
DMGTLNPLGY DQFLVISIGT GSAKKEERYS AKKAAKWGII SWLYEDGTTP ILDITFESSR
DIVHYHSSVV FKALQSEDKY LRIDDDTLEG DASTLDLSTK SNLENLIKLG EKMLTNRVMQ
MNIDTGTYEP AAENINNDEQ LKRFAKILSE ERKLRRKRSD KMTKDSSIGS QEIK
