IF4E1_ARATH
ID IF4E1_ARATH Reviewed; 235 AA.
AC O23252;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Eukaryotic translation initiation factor 4E-1 {ECO:0000303|PubMed:16343979, ECO:0000303|PubMed:9680993};
DE Short=eIF-4E-1 {ECO:0000303|PubMed:16343979, ECO:0000303|PubMed:9680993};
DE Short=eIF4E-1 {ECO:0000303|PubMed:16343979, ECO:0000303|PubMed:9680993};
DE AltName: Full=Protein cucumovirus multiplication 1;
DE AltName: Full=eIF-4F 25 kDa subunit {ECO:0000305};
DE AltName: Full=eIF-4F p26 subunit {ECO:0000305};
DE AltName: Full=mRNA cap-binding protein {ECO:0000305};
GN Name=EIF4E1 {ECO:0000303|PubMed:16343979, ECO:0000303|PubMed:9680993};
GN Synonyms=CUM1; OrderedLocusNames=At4g18040 {ECO:0000312|Araport:AT4G18040};
GN ORFNames=F15J5.10 {ECO:0000312|EMBL:CAB53645.1};
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 [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9680993; DOI=10.1046/j.1365-313x.1998.00047.x;
RA Rodriguez C.M., Freire M.A., Camilleri C., Robaglia C.;
RT "The Arabidopsis thaliana cDNAs coding for eIF4E and eIF(iso)4E are not
RT functionally equivalent for yeast complementation and are differentially
RT expressed during plant development.";
RL Plant J. 13:465-473(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].
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 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 [6]
RP REVIEW, AND SUBUNIT.
RX PubMed=16343979; DOI=10.1016/j.tplants.2005.11.004;
RA Robaglia C., Caranta C.;
RT "Translation initiation factors: a weak link in plant RNA virus
RT infection.";
RL Trends Plant Sci. 11:40-45(2006).
RN [7]
RP INTERACTION WITH EXA1.
RC STRAIN=cv. Columbia;
RX PubMed=28362261; DOI=10.7554/elife.23684;
RA Wu Z., Huang S., Zhang X., Wu D., Xia S., Li X.;
RT "Regulation of plant immune receptor accumulation through translational
RT repression by a glycine-tyrosine-phenylalanine (GYF) domain protein.";
RL Elife 6:0-0(2017).
RN [8]
RP FUNCTION (MICROBIAL INFECTION), DISRUPTION PHENOTYPE, MUTAGENESIS OF
RP TRP-69; THR-80; SER-81; SER-84; GLY-114 AND ASN-176, AND SUBUNIT (MICROBIAL
RP INFECTION).
RC STRAIN=cv. Columbia;
RX PubMed=29504210; DOI=10.1111/pbi.12896;
RA Bastet A., Lederer B., Giovinazzo N., Arnoux X., German-Retana S.,
RA Reinbold C., Brault V., Garcia D., Djennane S., Gersch S., Lemaire O.,
RA Robaglia C., Gallois J.-L.;
RT "Trans-species synthetic gene design allows resistance pyramiding and
RT broad-spectrum engineering of virus resistance in plants.";
RL Plant Biotechnol. J. 16:1569-1581(2018).
RN [9]
RP FUNCTION (MICROBIAL INFECTION), MUTAGENESIS OF TRP-69; THR-80; SER-81;
RP SER-84; GLY-114 AND ASN-176, DISRUPTION PHENOTYPE, AND SUBUNIT (MICROBIAL
RP INFECTION).
RC STRAIN=cv. Columbia;
RX PubMed=30784179; DOI=10.1111/pbi.13096;
RA Bastet A., Zafirov D., Giovinazzo N., Guyon-Debast A., Nogue F.,
RA Robaglia C., Gallois J.-L.;
RT "Mimicking natural polymorphism in eIF4E by CRISPR-Cas9 base editing is
RT associated with resistance to potyviruses.";
RL Plant Biotechnol. J. 17:1736-1750(2019).
CC -!- FUNCTION: Component of the protein complex eIF4F, which is involved in
CC the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal
CC secondary structure and recruitment of mRNA to the ribosome
CC (PubMed:9680993). Recognizes and binds the 7-methylguanosine-containing
CC mRNA cap during an early step in the initiation of protein synthesis
CC and facilitates ribosome binding by inducing the unwinding of the mRNAs
CC secondary structures (By similarity). Key component of recessive
CC resistance to potyviruses (PubMed:29504210, PubMed:30784179).
CC {ECO:0000250|UniProtKB:P48599, ECO:0000269|PubMed:9680993,
CC ECO:0000305|PubMed:29504210, ECO:0000305|PubMed:30784179}.
CC -!- FUNCTION: (Microbial infection) Susceptibility host factor required for
CC viral infection by recruiting viral RNAs to the host ribosomal complex
CC via an interaction with viral genome-linked protein (VPg).
CC {ECO:0000305|PubMed:29504210, ECO:0000305|PubMed:30784179}.
CC -!- SUBUNIT: EIF4F is a multi-subunit complex, the composition of which
CC varies with external and internal environmental conditions
CC (PubMed:16343979). It is composed of at least EIF4A, EIF4E and EIF4G.
CC EIF4E is also known to interact with other partners (PubMed:16343979).
CC In higher plants two isoforms of EIF4F have been identified, named
CC isoform EIF4F and isoform EIF(iso)4F (PubMed:16343979). Isoform EIF4F
CC has subunits p220 and p26, whereas isoform EIF(iso)4F has subunits p82
CC and p28 (PubMed:16343979). Interacts directly with EXA1
CC (PubMed:28362261). {ECO:0000269|PubMed:16343979,
CC ECO:0000269|PubMed:28362261}.
CC -!- SUBUNIT: (Microbial infection) Interacts with viral genome-linked
CC protein (VPg); this interaction is possible in susceptible hosts but
CC impaired in resistant plants. {ECO:0000305|PubMed:29504210,
CC ECO:0000305|PubMed:30784179}.
CC -!- INTERACTION:
CC O23252; O23160: MYB73; NbExp=3; IntAct=EBI-2359499, EBI-25506855;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:K0P2S0}. Cytoplasm
CC {ECO:0000250|UniProtKB:K0P2S0}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues except in the cells of the
CC specialization zone of the roots. {ECO:0000269|PubMed:9680993}.
CC -!- PTM: According to the redox status, the Cys-133-Cys-171 disulfide
CC bridge may have a role in regulating protein function by affecting its
CC ability to bind capped mRNA. {ECO:0000250|UniProtKB:P29557}.
CC -!- DISRUPTION PHENOTYPE: Delayed bolting (PubMed:29504210). Increased
CC resistance to potyviruses such as clover yellow vein virus (ClYVV) and
CC turnip mosaic virus (TuMV) (PubMed:29504210, PubMed:30784179).
CC {ECO:0000269|PubMed:29504210, ECO:0000269|PubMed:30784179}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC {ECO:0000305}.
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DR EMBL; Y10548; CAA71580.1; -; mRNA.
DR EMBL; AL110123; CAB53645.1; -; Genomic_DNA.
DR EMBL; AL161547; CAB78806.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83987.1; -; Genomic_DNA.
DR EMBL; AF389286; AAK63858.1; -; mRNA.
DR EMBL; AY093750; AAM10374.1; -; mRNA.
DR EMBL; AY086496; AAM63497.1; -; mRNA.
DR PIR; T14804; T14804.
DR RefSeq; NP_193538.1; NM_117914.4.
DR AlphaFoldDB; O23252; -.
DR SMR; O23252; -.
DR BioGRID; 12822; 10.
DR IntAct; O23252; 2.
DR STRING; 3702.AT4G18040.1; -.
DR iPTMnet; O23252; -.
DR PaxDb; O23252; -.
DR PRIDE; O23252; -.
DR ProteomicsDB; 232201; -.
DR EnsemblPlants; AT4G18040.1; AT4G18040.1; AT4G18040.
DR GeneID; 827529; -.
DR Gramene; AT4G18040.1; AT4G18040.1; AT4G18040.
DR KEGG; ath:AT4G18040; -.
DR Araport; AT4G18040; -.
DR TAIR; locus:2117647; AT4G18040.
DR eggNOG; KOG1670; Eukaryota.
DR HOGENOM; CLU_043552_2_1_1; -.
DR InParanoid; O23252; -.
DR OMA; NKFGGRW; -.
DR OrthoDB; 1394271at2759; -.
DR PhylomeDB; O23252; -.
DR PRO; PR:O23252; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23252; baseline and differential.
DR Genevisible; O23252; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IBA:GO_Central.
DR GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0000932; C:P-body; IDA:TAIR.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009615; P:response to virus; IMP:TAIR.
DR Gene3D; 3.30.760.10; -; 1.
DR InterPro; IPR023398; TIF_eIF4e-like.
DR InterPro; IPR001040; TIF_eIF_4E.
DR InterPro; IPR019770; TIF_eIF_4E_CS.
DR PANTHER; PTHR11960; PTHR11960; 1.
DR Pfam; PF01652; IF4E; 1.
DR SUPFAM; SSF55418; SSF55418; 1.
DR PROSITE; PS00813; IF4E; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Disulfide bond; Host-virus interaction; Initiation factor;
KW Nucleus; Plant defense; Protein biosynthesis; Reference proteome;
KW RNA-binding; Translation regulation.
FT CHAIN 1..235
FT /note="Eukaryotic translation initiation factor 4E-1"
FT /id="PRO_0000193654"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..63
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT REGION 70..106
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT REGION 154..163
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT BINDING 78..83
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT /ligand_part_id="ChEBI:CHEBI:74429"
FT /ligand_part_note="m7GTP residue in mRNA cap"
FT /evidence="ECO:0000250|UniProtKB:P29557"
FT BINDING 110
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT /ligand_part_id="ChEBI:CHEBI:74429"
FT /ligand_part_note="m7GTP residue in mRNA cap"
FT /evidence="ECO:0000250|UniProtKB:P29557"
FT BINDING 128..129
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT /ligand_part_id="ChEBI:CHEBI:74429"
FT /ligand_part_note="m7GTP residue in mRNA cap"
FT /evidence="ECO:0000250|UniProtKB:P29557"
FT BINDING 178..183
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT /ligand_part_id="ChEBI:CHEBI:74429"
FT /ligand_part_note="m7GTP residue in mRNA cap"
FT /evidence="ECO:0000250|UniProtKB:P29557"
FT BINDING 223..227
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT /ligand_part_id="ChEBI:CHEBI:74429"
FT /ligand_part_note="m7GTP residue in mRNA cap"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT DISULFID 133..171
FT /evidence="ECO:0000250|UniProtKB:P29557"
FT MUTAGEN 69
FT /note="W->L: Normal bolting time and normal susceptibility
FT to potyviruses such as clover yellow vein virus (ClYVV). In
FT eIF4E1(R): Normal bolting time and increased resistance to
FT potyviruses such as ClYVV, watermelon mosaic virus (WMV),
FT turnip mosaic virus (TuMV, including resistance-breaking
FT strains TuMV-E116Q and TuMV-N163Y), lettuce mosaic virus
FT (LMV) and plum pox virus (PPV), and to polerovirus such as
FT beet mild yellowing virus isolate USA (BWYV-USA); when
FT associated with D-80; D-81; A-84; R-114 and K-176."
FT /evidence="ECO:0000269|PubMed:29504210,
FT ECO:0000269|PubMed:30784179"
FT MUTAGEN 80
FT /note="T->D: Normal bolting time and increased resistance
FT to potyviruses such as clover yellow vein virus (ClYVV),
FT watermelon mosaic virus (WMV) and turnip mosaic virus
FT (TuMV, including resistance-breaking strains TuMV-E116Q and
FT TuMV-N163Y); when associated with D-81. In eIF4E1(R);
FT normal bolting time and increased resistance to potyviruses
FT such as ClYVV, WMV, TuMV (including resistance-breaking
FT strains TuMV-E116Q and TuMV-N163Y), lettuce mosaic virus
FT (LMV) and plum pox virus (PPV), and to polerovirus such as
FT beet mild yellowing virus isolate USA (BWYV-USA); when
FT associated with L-69; D-81; A-84; R-114 and K-176."
FT /evidence="ECO:0000269|PubMed:29504210,
FT ECO:0000269|PubMed:30784179"
FT MUTAGEN 81
FT /note="S->D: Normal bolting time and increased resistance
FT to potyviruses such as clover yellow vein virus (ClYVV),
FT watermelon mosaic virus (WMV) and turnip mosaic virus
FT (TuMV, including resistance-breaking strains TuMV-E116Q and
FT TuMV-N163Y); when associated with D-80. In eIF4E1(R);
FT normal bolting time and increased resistance to potyviruses
FT such as ClYVV, WMV, TuMV (including resistance-breaking
FT strains TuMV-E116Q and TuMV-N163Y), lettuce mosaic virus
FT (LMV) and plum pox virus (PPV), and to polerovirus such as
FT beet mild yellowing virus isolate USA (BWYV-USA); when
FT associated with L-69; D-80; A-84; R-114 and K-176."
FT /evidence="ECO:0000269|PubMed:29504210,
FT ECO:0000269|PubMed:30784179"
FT MUTAGEN 84
FT /note="S->A: Normal bolting time and partial resistance to
FT potyviruses such as clover yellow vein virus (ClYVV). In
FT eIF4E1(R); normal bolting time and increased resistance to
FT potyviruses such as ClYVV, watermelon mosaic virus (WMV),
FT turnip mosaic virus (TuMV, including resistance-breaking
FT strains TuMV-E116Q and TuMV-N163Y), lettuce mosaic virus
FT (LMV) and plum pox virus (PPV), and to polerovirus such as
FT beet mild yellowing virus isolate USA (BWYV-USA); when
FT associated with L-69; D-80; D-81; R-114 and K-176."
FT /evidence="ECO:0000269|PubMed:29504210,
FT ECO:0000269|PubMed:30784179"
FT MUTAGEN 114
FT /note="G->R: Normal bolting time and partial resistance to
FT potyviruses such as clover yellow vein virus (ClYVV),
FT watermelon mosaic virus (WMV) and turnip mosaic virus
FT (TuMV). In eIF4E1(R); normal bolting time and increased
FT resistance to potyviruses such as ClYVV, WMV, TuMV
FT (including resistance-breaking strains TuMV-E116Q and TuMV-
FT N163Y), lettuce mosaic virus (LMV) and plum pox virus
FT (PPV), and to polerovirus such as beet mild yellowing virus
FT isolate USA (BWYV-USA); when associated with L-69; D-80; D-
FT 81; A-84 and K-176."
FT /evidence="ECO:0000269|PubMed:29504210,
FT ECO:0000269|PubMed:30784179"
FT MUTAGEN 176
FT /note="N->K: Normal bolting time and increased resistance
FT to potyviruses such as clover yellow vein virus (ClYVV),
FT watermelon mosaic virus (WMV) and turnip mosaic virus
FT (TuMV). In eIF4E1(R); normal bolting time and increased
FT resistance to potyvirus such as ClYVV, TuMV (including
FT resistance-breaking strains TuMV-E116Q and TuMV-N163Y),
FT WMV, lettuce mosaic virus (LMV) and plum pox virus (PPV),
FT and to polerovirus such as beet mild yellowing virus
FT isolate USA (BWYV-USA); when associated with L-69; D-80; D-
FT 81; A-84 and R-114."
FT /evidence="ECO:0000269|PubMed:29504210,
FT ECO:0000269|PubMed:30784179"
SQ SEQUENCE 235 AA; 26519 MW; 0329A375FE19A3C6 CRC64;
MAVEDTPKSV VTEEAKPNSI ENPIDRYHEE GDDAEEGEIA GGEGDGNVDE SSKSGVPESH
PLEHSWTFWF DNPAVKSKQT SWGSSLRPVF TFSTVEEFWS LYNNMKHPSK LAHGADFYCF
KHIIEPKWED PICANGGKWT MTFPKEKSDK SWLYTLLALI GEQFDHGDEI CGAVVNIRGK
QERISIWTKN ASNEAAQVSI GKQWKEFLDY NNSIGFIIHE DAKKLDRNAK NAYTA
