LFG1_ARATH
ID LFG1_ARATH Reviewed; 235 AA.
AC F4JIE8; O23329;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Protein LIFEGUARD 1 {ECO:0000303|PubMed:23888068};
DE Short=AtLFG1 {ECO:0000303|PubMed:23888068};
GN Name=LFG1 {ECO:0000303|PubMed:23888068};
GN OrderedLocusNames=At4g14730 {ECO:0000312|Araport:AT4G14730};
GN ORFNames=Dl3405W {ECO:0000312|EMBL:CAB10252.1},
GN FCAALL.300 {ECO:0000312|EMBL:CAB78515.1};
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 2).
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY.
RX PubMed=19202280; DOI=10.1271/bbb.80752;
RA Yamagami A., Nakazawa M., Matsui M., Tujimoto M., Sakuta M., Asami T.,
RA Nakano T.;
RT "Chemical genetics reveal the novel transmembrane protein BIL4, which
RT mediates plant cell elongation in brassinosteroid signaling.";
RL Biosci. Biotechnol. Biochem. 73:415-421(2009).
RN [6]
RP FUNCTION (MICROBIAL INFECTION), DISRUPTION PHENOTYPE, TISSUE SPECIFICITY,
RP GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=23888068; DOI=10.1093/jxb/ert217;
RA Weis C., Hueckelhoven R., Eichmann R.;
RT "LIFEGUARD proteins support plant colonization by biotrophic powdery mildew
RT fungi.";
RL J. Exp. Bot. 64:3855-3867(2013).
CC -!- FUNCTION: (Microbial infection) Facilitates the development of the
CC powdery mildew fungus E.cruciferarum. {ECO:0000269|PubMed:23888068}.
CC -!- FUNCTION: (Microbial infection) May prevent cell death upon A.alternata
CC f.sp. lycopersici (AAL) toxin treatment. {ECO:0000269|PubMed:23888068}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4JIE8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4JIE8-2; Sequence=VSP_059076, VSP_059077;
CC -!- TISSUE SPECIFICITY: Expressed at very low in leaves.
CC {ECO:0000269|PubMed:23888068}.
CC -!- DISRUPTION PHENOTYPE: Delayed development of the powdery mildew fungus
CC E.cruciferarum. Increased cell death upon A.alternata f.sp. lycopersici
CC (AAL) toxin treatment. {ECO:0000269|PubMed:23888068}.
CC -!- SIMILARITY: Belongs to the BI1 family. {ECO:0000305}.
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DR EMBL; Z97337; CAB10252.1; -; Genomic_DNA.
DR EMBL; AL161539; CAB78515.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83489.1; -; Genomic_DNA.
DR EMBL; BT010801; AAR24168.1; -; mRNA.
DR EMBL; BT011269; AAR92305.1; -; mRNA.
DR PIR; B71410; B71410.
DR RefSeq; NP_193209.2; NM_117558.3. [F4JIE8-1]
DR AlphaFoldDB; F4JIE8; -.
DR SMR; F4JIE8; -.
DR IntAct; F4JIE8; 4.
DR STRING; 3702.AT4G14730.1; -.
DR iPTMnet; F4JIE8; -.
DR PaxDb; F4JIE8; -.
DR PRIDE; F4JIE8; -.
DR ProteomicsDB; 238464; -. [F4JIE8-1]
DR EnsemblPlants; AT4G14730.1; AT4G14730.1; AT4G14730. [F4JIE8-1]
DR GeneID; 827126; -.
DR Gramene; AT4G14730.1; AT4G14730.1; AT4G14730. [F4JIE8-1]
DR KEGG; ath:AT4G14730; -.
DR Araport; AT4G14730; -.
DR TAIR; locus:2130170; AT4G14730.
DR eggNOG; KOG2322; Eukaryota.
DR HOGENOM; CLU_058671_0_1_1; -.
DR InParanoid; F4JIE8; -.
DR OMA; KHPINLI; -.
DR OrthoDB; 1290306at2759; -.
DR PRO; PR:F4JIE8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JIE8; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0034620; P:cellular response to unfolded protein; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:UniProtKB.
DR InterPro; IPR006214; Bax_inhibitor_1-related.
DR PANTHER; PTHR23291; PTHR23291; 1.
DR Pfam; PF01027; Bax1-I; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Membrane; Plant defense; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..235
FT /note="Protein LIFEGUARD 1"
FT /id="PRO_0000441629"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 80..100
FT /note="LLWPLLAFEKKHPINCIVLSI -> RYVSFHILLFIHSFLGSIIVA (in
FT isoform 2)"
FT /id="VSP_059076"
FT VAR_SEQ 101..235
FT /note="Missing (in isoform 2)"
FT /id="VSP_059077"
SQ SEQUENCE 235 AA; 26272 MW; FB4556314C4B3015 CRC64;
MAKSDIETGG GNELYPGMKE SSELRWAFIR KLYSILSLQL LVTVGVSAVV YFVRPIPEFI
TETHRGLAVF FVILLLPLLL LWPLLAFEKK HPINCIVLSI FTLSISFSVG ICCSLSQGRI
VLEAAILTAV MVFGLTIYTF WAVKRGHDFS FLGPFLFGAL LIILVFTLLQ IFHPLGKLSS
MIFSGIASIV FCGYIIFDTN QLIKKLNYDE YITAAIRLYL DVMNLFLSLL GIISN
