IF4E1_HORVV
ID IF4E1_HORVV Reviewed; 215 AA.
AC Q4QXS7; A0A0M5NBZ4; B8Y450; D8LAQ6; D8LAQ7; D8LAQ8; D8LAQ9; D8LAR0; D8LAR1;
AC D8LAR2;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Eukaryotic translation initiation factor 4E-1 {ECO:0000303|PubMed:15634196, ECO:0000303|PubMed:21806691, ECO:0000303|Ref.3};
DE Short=Hv-eIF4E-1 {ECO:0000303|PubMed:15634196, ECO:0000303|PubMed:21806691, ECO:0000303|Ref.3};
DE Short=eIF-4E-1 {ECO:0000303|PubMed:15634196, ECO:0000303|PubMed:21806691, ECO:0000303|Ref.3};
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:0000303|PubMed:15634196, ECO:0000303|PubMed:21806691, ECO:0000303|Ref.3};
GN Name=eIF4E {ECO:0000303|PubMed:15634196, ECO:0000303|PubMed:21806691,
GN ECO:0000303|Ref.3};
OS Hordeum vulgare subsp. vulgare (Domesticated barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=112509;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Morex;
RX PubMed=15634196; DOI=10.1111/j.1365-313x.2004.02285.x;
RA Wicker T., Zimmermann W., Perovic D., Paterson A.H., Ganal M., Graner A.,
RA Stein N.;
RT "A detailed look at 7 million years of genome evolution in a 439 kb
RT contiguous sequence at the barley Hv-eIF4E locus: recombination,
RT rearrangements and repeats.";
RL Plant J. 41:184-194(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANTS SER-53; PHE-57; ILE-118; THR-118;
RP 160-ASN-GLN-161 DELINS LYS-GLU; HIS-161; ILE-175; VAL-195; GLY-206; ALA-208
RP AND GLY-209, FUNCTION, FUNCTION (MICROBIAL INFECTION), AND SUBUNIT
RP (MICROBIAL INFECTION).
RC STRAIN=cv. Miho Golden; TISSUE=Leaf;
RX PubMed=21806691; DOI=10.1111/j.1365-294x.2011.05201.x;
RA Hofinger B.J., Russell J.R., Bass C.G., Baldwin T., dos Reis M.,
RA Hedley P.E., Li Y., Macaulay M., Waugh R., Hammond-Kosack K.E., Kanyuka K.;
RT "An exceptionally high nucleotide and haplotype diversity and a signature
RT of positive selection for the eIF4E resistance gene in barley are revealed
RT by allele mining and phylogenetic analyses of natural populations.";
RL Mol. Ecol. 20:3653-3668(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-120; ASP-160 AND
RP 161-LYS.
RC STRAIN=cv. Mikamo Golden, and cv. Sukai Golden;
RA Nagamine T.;
RT "Classification of Japanese barley cultivars with rym5 allelic barley
RT yellow mosaic virus (BaYMV)-resistant genotypes using a CAPS marker for the
RT eIF4E gene.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS SER-53 AND
RP HIS-161.
RC STRAIN=cv. Haruna Nijo;
RX PubMed=19011002; DOI=10.1104/pp.108.129734;
RA Wicker T., Krattinger S.G., Lagudah E.S., Komatsuda T., Pourkheirandish M.,
RA Matsumoto T., Cloutier S., Reiser L., Kanamori H., Sato K., Perovic D.,
RA Stein N., Keller B.;
RT "Analysis of intraspecies diversity in wheat and barley genomes identifies
RT breakpoints of ancient haplotypes and provides insight into the structure
RT of diploid and hexaploid triticeae gene pools.";
RL Plant Physiol. 149:258-270(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Morex;
RX PubMed=23075845; DOI=10.1038/nature11543;
RG International Barley Genome Sequencing Consortium;
RA Mayer K.F., Waugh R., Brown J.W., Schulman A., Langridge P., Platzer M.,
RA Fincher G.B., Muehlbauer G.J., Sato K., Close T.J., Wise R.P., Stein N.;
RT "A physical, genetic and functional sequence assembly of the barley
RT genome.";
RL Nature 491:711-716(2012).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-53 AND HIS-161.
RC STRAIN=cv. Haruna Nijo; TISSUE=Root, and Shoot;
RX PubMed=21415278; DOI=10.1104/pp.110.171579;
RA Matsumoto T., Tanaka T., Sakai H., Amano N., Kanamori H., Kurita K.,
RA Kikuta A., Kamiya K., Yamamoto M., Ikawa H., Fujii N., Hori K., Itoh T.,
RA Sato K.;
RT "Comprehensive sequence analysis of 24,783 barley full-length cDNAs derived
RT from 12 clone libraries.";
RL Plant Physiol. 156:20-28(2011).
RN [7]
RP FUNCTION, FUNCTION (MICROBIAL INFECTION), VARIANTS SER-53; PHE-57; ILE-118;
RP THR-118; SER-120; ASP-160; LYS-161; PHE-205; GLY-206; ALA-208 AND SER-208,
RP SUBUNIT (MICROBIAL INFECTION), AND POLYMORPHISM.
RX PubMed=15941403; DOI=10.1111/j.1365-313x.2005.02424.x;
RA Stein N., Perovic D., Kumlehn J., Pellio B., Stracke S., Streng S.,
RA Ordon F., Graner A.;
RT "The eukaryotic translation initiation factor 4E confers multiallelic
RT recessive Bymovirus resistance in Hordeum vulgare (L.).";
RL Plant J. 42:912-922(2005).
RN [8]
RP GENE FAMILY, AND REVIEW.
RX PubMed=24309680; DOI=10.1016/j.meegid.2013.11.024;
RA Moury B., Charron C., Janzac B., Simon V., Gallois J.L., Palloix A.,
RA Caranta C.;
RT "Evolution of plant eukaryotic initiation factor 4E (eIF4E) and potyvirus
RT genome-linked protein (VPg): a game of mirrors impacting resistance
RT spectrum and durability.";
RL Infect. Genet. Evol. 27:472-480(2014).
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 (By
CC similarity). Recognizes and binds the 7-methylguanosine-containing mRNA
CC cap during an early step in the initiation of protein synthesis and
CC facilitates ribosome binding by inducing the unwinding of the mRNAs
CC secondary structures (By similarity). Key component of recessive
CC resistance to potyviruses and bymoviruses, including barley yellow
CC mosaic virus and barley mild mosaic virus (PubMed:21806691,
CC PubMed:15941403). {ECO:0000250|UniProtKB:P29557,
CC ECO:0000269|PubMed:15941403, ECO:0000269|PubMed:21806691}.
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:0000269|PubMed:15941403, ECO:0000269|PubMed:21806691}.
CC -!- SUBUNIT: EIF4F is a multi-subunit complex, the composition of which
CC varies with external and internal environmental conditions. It is
CC composed of at least EIF4A, EIF4E and EIF4G. EIF4E is also known to
CC interact with other partners. In higher plants two isoforms of EIF4F
CC have been identified, named isoform EIF4F and isoform EIF(iso)4F.
CC Isoform EIF4F has subunits p220 and p26, whereas isoform EIF(iso)4F has
CC subunits p82 and p28. {ECO:0000250|UniProtKB:P29557}.
CC -!- SUBUNIT: (Microbial infection) Interacts with potyvirus viral genome-
CC linked protein (VPg); this interaction is possible in susceptible hosts
CC but impaired in resistant plants. {ECO:0000305|PubMed:15941403,
CC ECO:0000305|PubMed:21806691}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C6ZJZ3}. Cytoplasm
CC {ECO:0000250|UniProtKB:C6ZJZ3}.
CC -!- PTM: According to the redox status, the Cys-113-Cys-151 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 -!- POLYMORPHISM: Variant present in the allele rym4, confers an increased
CC resistance to barley yellow mosaic (BaYMV) and barley mild mosaic virus
CC (BaMMV). {ECO:0000269|PubMed:15941403}.
CC -!- POLYMORPHISM: Variant present in the allele rym5, confers an increased
CC resistance to barley yellow mosaic (BaYMV), barley mild mosaic virus
CC (BaMMV) and BaYMV-2. {ECO:0000269|PubMed:15941403}.
CC -!- MISCELLANEOUS: Displayed sequence is cv. Morex. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC {ECO:0000305}.
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DR EMBL; AY661558; AAV80393.1; -; Genomic_DNA.
DR EMBL; FN600114; CBI68710.1; -; mRNA.
DR EMBL; FN646082; CBI83258.1; -; mRNA.
DR EMBL; FN646083; CBI83259.1; -; mRNA.
DR EMBL; FN646084; CBI83260.1; -; mRNA.
DR EMBL; FN646085; CBI83261.1; -; mRNA.
DR EMBL; FN646086; CBI83262.1; -; mRNA.
DR EMBL; FN646087; CBI83263.1; -; mRNA.
DR EMBL; FN646088; CBI83264.1; -; mRNA.
DR EMBL; FJ477092; ACK99543.1; -; Genomic_DNA.
DR EMBL; LC037203; BAS53705.1; -; Genomic_DNA.
DR EMBL; LC037204; BAS53706.1; -; Genomic_DNA.
DR EMBL; AK365250; BAJ96453.1; -; mRNA.
DR EMBL; AK368452; BAJ99655.1; -; mRNA.
DR EMBL; AK368630; BAJ99833.1; -; mRNA.
DR SMR; Q4QXS7; -.
DR STRING; 112509.Q4QXS7; -.
DR EnsemblPlants; HORVU.MOREX.r2.3HG0272870.1; HORVU.MOREX.r2.3HG0272870.1; HORVU.MOREX.r2.3HG0272870.
DR EnsemblPlants; HORVU.MOREX.r2.3HG0272870.1.mrna1; HORVU.MOREX.r2.3HG0272870.1.mrna1; HORVU.MOREX.r2.3HG0272870.1.
DR EnsemblPlants; HORVU.MOREX.r3.3HG0327270.1; HORVU.MOREX.r3.3HG0327270.1; HORVU.MOREX.r3.3HG0327270.
DR Gramene; HORVU.MOREX.r2.3HG0272870.1; HORVU.MOREX.r2.3HG0272870.1; HORVU.MOREX.r2.3HG0272870.
DR Gramene; HORVU.MOREX.r2.3HG0272870.1.mrna1; HORVU.MOREX.r2.3HG0272870.1.mrna1; HORVU.MOREX.r2.3HG0272870.1.
DR Gramene; HORVU.MOREX.r3.3HG0327270.1; HORVU.MOREX.r3.3HG0327270.1; HORVU.MOREX.r3.3HG0327270.
DR eggNOG; KOG1670; Eukaryota.
DR OMA; NKFGGRW; -.
DR Proteomes; UP000011116; Unassembled WGS sequence.
DR ExpressionAtlas; Q4QXS7; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0006413; P:translational initiation; ISS:UniProtKB.
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..215
FT /note="Eukaryotic translation initiation factor 4E-1"
FT /id="PRO_0000454067"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..43
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT REGION 50..86
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT REGION 134..143
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 58..63
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 90
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 108..109
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 158..163
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 203..207
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 113..151
FT /evidence="ECO:0000250|UniProtKB:P29557"
FT VARIANT 53
FT /note="P -> S (in strain: Miho Golden and Haruna Nijo. In
FT allele rym5)"
FT /evidence="ECO:0000269|PubMed:15941403,
FT ECO:0000269|PubMed:19011002, ECO:0000269|PubMed:21415278,
FT ECO:0000269|PubMed:21806691"
FT VARIANT 57
FT /note="S -> F (in alleles 40 and 44. In allele rym4)"
FT /evidence="ECO:0000269|PubMed:15941403,
FT ECO:0000269|PubMed:21806691"
FT VARIANT 118
FT /note="K -> I (in allele 44. In allele rym4)"
FT /evidence="ECO:0000269|PubMed:15941403,
FT ECO:0000269|PubMed:21806691"
FT VARIANT 118
FT /note="K -> T (in alleles 40 and 43. In allele rym4)"
FT /evidence="ECO:0000269|PubMed:15941403,
FT ECO:0000269|PubMed:21806691"
FT VARIANT 120
FT /note="T -> S (in strain: Sukai Golden and Mikamo Golden.
FT In allele rym5)"
FT /evidence="ECO:0000269|PubMed:15941403, ECO:0000269|Ref.3"
FT VARIANT 160..161
FT /note="NQ -> KE (in alleles 38 and 39)"
FT /evidence="ECO:0000269|PubMed:21806691"
FT VARIANT 160
FT /note="N -> D (in strain: Sukai Golden and Mikamo Golden.
FT In allele rym5)"
FT /evidence="ECO:0000269|PubMed:15941403, ECO:0000269|Ref.3"
FT VARIANT 161
FT /note="Q -> H (in strain: Miho Golden and Haruna Nijo)"
FT /evidence="ECO:0000269|PubMed:19011002,
FT ECO:0000269|PubMed:21415278, ECO:0000269|PubMed:21806691"
FT VARIANT 161
FT /note="Q -> K (in strain: Sukai Golden and Mikamo Golden.
FT In allele rym5)"
FT /evidence="ECO:0000269|PubMed:15941403, ECO:0000269|Ref.3"
FT VARIANT 175
FT /note="T -> I (in allele 41)"
FT /evidence="ECO:0000269|PubMed:21806691"
FT VARIANT 195
FT /note="G -> V (in allele 42)"
FT /evidence="ECO:0000269|PubMed:21806691"
FT VARIANT 205
FT /note="S -> F (in allele rym4)"
FT /evidence="ECO:0000269|PubMed:15941403"
FT VARIANT 206
FT /note="D -> G (in alleles 40, 43 and 44. In allele rym4)"
FT /evidence="ECO:0000269|PubMed:15941403,
FT ECO:0000269|PubMed:21806691"
FT VARIANT 208
FT /note="G -> A (in alleles 40, 43 and 44)"
FT /evidence="ECO:0000269|PubMed:15941403,
FT ECO:0000269|PubMed:21806691"
FT VARIANT 208
FT /note="G -> S (in alleles 40, 43 and 44)"
FT /evidence="ECO:0000269|PubMed:15941403"
FT VARIANT 209
FT /note="A -> G (in allele 39)"
FT /evidence="ECO:0000269|PubMed:21806691"
SQ SEQUENCE 215 AA; 23873 MW; 28CFF4DA0D6E79CF CRC64;
MAEDTETRPA SAGAEEREEG EIADDGDGSA AAAAGRVSAH PLENAWTFWF DNPQGKSRAV
AWGSTIHPIH TFSTVEDFWS LYNNIHHPSK LNVGADFHCF KDKIEPKWED PICANGGKWT
ISCGKGKSDT FWLHTLLALI GEQFDFGDEI CGAVVSVRKN QERVAIWTKN AANETAQISI
GKQWKEFLDY KDSIGFVVHE DAKRSDKGAK NRYTV
