PLAT1_ARATH
ID PLAT1_ARATH Reviewed; 181 AA.
AC O65660; Q93ZG8;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=PLAT domain-containing protein 1 {ECO:0000305};
DE Short=AtPLAT1 {ECO:0000303|PubMed:25396746};
DE Short=PLAT domain protein 1 {ECO:0000303|PubMed:25396746};
DE Flags: Precursor;
GN Name=PLAT1 {ECO:0000303|PubMed:25396746};
GN OrderedLocusNames=At4g39730 {ECO:0000312|Araport:AT4G39730};
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=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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14760647; DOI=10.1002/elps.200305677;
RA Lee K., Lee J., Kim Y., Bae D., Kang K.Y., Yoon S.C., Lim D.;
RT "Defining the plant disulfide proteome.";
RL Electrophoresis 25:532-541(2004).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-15, CLEAVAGE OF SIGNAL PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER LEU-14, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=22274653; DOI=10.1104/pp.111.193144;
RA Lundquist P.K., Poliakov A., Bhuiyan N.H., Zybailov B., Sun Q.,
RA van Wijk K.J.;
RT "The functional network of the Arabidopsis plastoglobule proteome based on
RT quantitative proteomics and genome-wide coexpression analysis.";
RL Plant Physiol. 158:1172-1192(2012).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=25396746; DOI=10.1371/journal.pone.0112946;
RA Hyun T.K., van der Graaff E., Albacete A., Eom S.H., Grosskinsky D.K.,
RA Boehm H., Janschek U., Rim Y., Ali W.W., Kim S.Y., Roitsch T.;
RT "The Arabidopsis PLAT domain protein1 is critically involved in abiotic
RT stress tolerance.";
RL PLoS ONE 9:E112946-E112946(2014).
CC -!- FUNCTION: Positive regulator of abiotic stress tolerance involved in
CC the regulation of plant growth. May be a downstream target of the
CC abscisic acid (ABA) signaling pathway. {ECO:0000269|PubMed:25396746}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:25396746}. Plastid, chloroplast, plastoglobule
CC {ECO:0000269|PubMed:22274653}. Note=Localizes to rod shaped ER
CC structures that resemble ER bodies. {ECO:0000269|PubMed:25396746}.
CC -!- TISSUE SPECIFICITY: Expressed in root tips, pericycle cells, lateral
CC root primordia, stomata, leaf vasculature, hydathodes and floral
CC organs. {ECO:0000269|PubMed:25396746}.
CC -!- INDUCTION: By salt and cold stresses, and abscisic acid.
CC {ECO:0000269|PubMed:25396746}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plant have enhanced sensitivity to salt, drought
CC and cold stresses. {ECO:0000269|PubMed:25396746}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL09786.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL022605; CAA18759.1; -; Genomic_DNA.
DR EMBL; AL161595; CAB80636.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE87110.1; -; Genomic_DNA.
DR EMBL; AY057547; AAL09786.1; ALT_FRAME; mRNA.
DR EMBL; AY079024; AAL84978.1; -; mRNA.
DR EMBL; AY093757; AAM10381.1; -; mRNA.
DR EMBL; AY088352; AAM65891.1; -; mRNA.
DR PIR; T05010; T05010.
DR RefSeq; NP_195683.1; NM_120134.3.
DR AlphaFoldDB; O65660; -.
DR SMR; O65660; -.
DR STRING; 3702.AT4G39730.1; -.
DR iPTMnet; O65660; -.
DR PaxDb; O65660; -.
DR PRIDE; O65660; -.
DR ProteomicsDB; 236745; -.
DR EnsemblPlants; AT4G39730.1; AT4G39730.1; AT4G39730.
DR GeneID; 830128; -.
DR Gramene; AT4G39730.1; AT4G39730.1; AT4G39730.
DR KEGG; ath:AT4G39730; -.
DR Araport; AT4G39730; -.
DR TAIR; locus:2135217; AT4G39730.
DR eggNOG; ENOG502RZE1; Eukaryota.
DR HOGENOM; CLU_092946_1_0_1; -.
DR InParanoid; O65660; -.
DR OMA; TGAHKQC; -.
DR OrthoDB; 1307023at2759; -.
DR PhylomeDB; O65660; -.
DR PRO; PR:O65660; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O65660; baseline and differential.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0010287; C:plastoglobule; IEA:UniProtKB-SubCell.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0009409; P:response to cold; IMP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IMP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IMP:UniProtKB.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR Pfam; PF01477; PLAT; 1.
DR SUPFAM; SSF49723; SSF49723; 1.
DR PROSITE; PS50095; PLAT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chloroplast; Endoplasmic reticulum; Growth regulation;
KW Plastid; Reference proteome; Signal; Stress response.
FT SIGNAL 1..14
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 15..181
FT /note="PLAT domain-containing protein 1"
FT /id="PRO_5006739242"
FT DOMAIN 29..156
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT MOD_RES 15
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 181 AA; 20136 MW; 58839B336840CD33 CRC64;
MARRDVLLPF LLLLATVSAV AFAEDDPDCV YTFYLRTGSI WKAGTDSIIS ARIYDKDGDY
IGIKNLQAWA GLMGPDYNYF ERGNLDIFSG RAPCLPSPIC ALNLTSDGSG DHHGWYVNYV
EITTAGVHAQ CSTQDFEIEQ WLATDTSPYE LTAVRNNCPV KLRDSVSRVG SEIRKKLSWV
V
