IF4E1_SOYBN
ID IF4E1_SOYBN Reviewed; 237 AA.
AC C6ZJZ3; A0A6H1NPQ5; A0A6H1NPQ6;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Eukaryotic translation initiation factor 4E-1 {ECO:0000303|PubMed:31860775};
DE Short=eIF4E-1 {ECO:0000303|PubMed:31860775};
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:31860775};
GN ORFNames=GLYMA_13G222400 {ECO:0000312|EMBL:KRH21134.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Williams;
RA Li W., Zhang Y., Han Y.;
RT "Cloning and analysis of gene encoding eukaryotic translation initiation
RT factor 4E, eIF4E.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, FUNCTION (MICROBIAL INFECTION),
RP DISRUPTION PHENOTYPE (MICROBIAL INFECTION), VARIANTS ASN-170 AND LYS-180,
RP INTERACTION WITH VIRAL VPG; NIA-PRO AND NIB (MICROBIAL INFECTION),
RP SUBCELLULAR LOCATION, SUBCELLULAR LOCATION (MICROBIAL INFECTION), TISSUE
RP SPECIFICITY, AND INDUCTION BY POTYVIRUS (MICROBIAL INFECTION).
RC STRAIN=cv. Kefeng 1, cv. Liao 04M05-3, cv. Nannong 1138-2, cv. Tianlong 1,
RC cv. Zhongzuo 06-06, and cv. Zhongzuo J8035;
RX PubMed=31860775; DOI=10.1111/mpp.12897;
RA Gao L., Luo J., Ding X., Wang T., Hu T., Song P., Zhai R., Zhang H.,
RA Zhang K., Li K., Zhi H.;
RT "Soybean RNA interference lines silenced for eIF4E show broad potyvirus
RT resistance.";
RL Mol. Plant Pathol. 21:303-317(2020).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82; TISSUE=Callus;
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [4]
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 (e.g. soybean mosaic virus (SMV), bean common
CC mosaic virus (BCMV) and watermelon mosaic virus (WMV), but not bean pod
CC mottle virus (BPMV)) (PubMed:31860775). {ECO:0000250|UniProtKB:P29557,
CC ECO:0000269|PubMed:31860775}.
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:31860775}.
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) in the nucleus; this interaction is possible in
CC susceptible hosts but is impaired in resistant plants
CC (PubMed:31860775). Binds to soybean mosaic virus (SMV) VPg in the
CC nucleus (PubMed:31860775). Interacts with SMV nuclear inclusion protein
CC A (NIa-Pro) and nuclear inclusion protein B (NIb) in the cytoplasm
CC (PubMed:31860775). {ECO:0000269|PubMed:31860775}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31860775}. Cytoplasm
CC {ECO:0000269|PubMed:31860775}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31860775}. Cytoplasm
CC {ECO:0000269|PubMed:31860775}. Note=(Microbial infection) Binds to
CC potyvirus viral genome-linked protein (VPg) in the nucleus and with
CC potyvirus nuclear inclusion protein A (NIa-Pro) and nuclear inclusion
CC protein B (NIb) in the cytoplasm. {ECO:0000269|PubMed:31860775}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots, flowers, immature pods
CC and mature seeds, and, to a lower extent, in stems and leaves.
CC {ECO:0000269|PubMed:31860775}.
CC -!- INDUCTION: (Microbial infection) Induced upon infection by soybean
CC mosaic virus (SMV) in susceptible plants (e.g. cv. Tianlong 1) but not
CC in resistant plants (e.g. cv. Kefeng 1). {ECO:0000269|PubMed:31860775}.
CC -!- PTM: According to the redox status, the Cys-135-Cys-173 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: (Microbial infection) Increased resistance to
CC potyvirus such as soybean mosaic virus (SMV), bean common mosaic virus
CC (BCMV) and watermelon mosaic virus (WMV), but susceptible to bean pod
CC mottle virus (BPMV). {ECO:0000269|PubMed:31860775}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC {ECO:0000305}.
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DR EMBL; EU912426; ACM45958.1; -; mRNA.
DR EMBL; MN369710; QIZ03080.1; -; mRNA.
DR EMBL; MN369711; QIZ03081.1; -; mRNA.
DR EMBL; MN369712; QIZ03082.1; -; mRNA.
DR EMBL; MN369713; QIZ03083.1; -; mRNA.
DR EMBL; MN369715; QIZ03085.1; -; mRNA.
DR EMBL; CM000846; KRH21134.1; -; Genomic_DNA.
DR RefSeq; NP_001237528.1; NM_001250599.1.
DR AlphaFoldDB; C6ZJZ3; -.
DR SMR; C6ZJZ3; -.
DR STRING; 3847.GLYMA13G29420.1; -.
DR EnsemblPlants; KRH21134; KRH21134; GLYMA_13G222400.
DR GeneID; 100499636; -.
DR Gramene; KRH21134; KRH21134; GLYMA_13G222400.
DR KEGG; gmx:100499636; -.
DR eggNOG; KOG1670; Eukaryota.
DR HOGENOM; CLU_043552_2_1_1; -.
DR InParanoid; C6ZJZ3; -.
DR OMA; NKFGGRW; -.
DR OrthoDB; 1394271at2759; -.
DR Proteomes; UP000008827; Chromosome 13.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA: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; IMP:UniProtKB.
DR GO; GO:0009615; P:response to virus; IEP: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..237
FT /note="Eukaryotic translation initiation factor 4E-1"
FT /id="PRO_0000454064"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..65
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT REGION 72..108
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT REGION 156..165
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..41
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 80..85
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 112
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 130..131
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 180..185
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 225..229
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 135..173
FT /evidence="ECO:0000250|UniProtKB:P29557"
FT VARIANT 170
FT /note="D -> N (in strain: Zhongzuo 06-06)"
FT /evidence="ECO:0000269|PubMed:31860775"
FT VARIANT 180
FT /note="R -> K (in strain: Liao 04M05-3 and Zhongzuo J8035)"
FT /evidence="ECO:0000269|PubMed:31860775"
SQ SEQUENCE 237 AA; 26762 MW; 9F6995D76AFA03D4 CRC64;
MVVEDTQKSV ITEDQYPSRV VSDNNNDDDD DDLEEGEIPV DGEDSGATAT TKPPAALARN
PHPLENSWTF WFDNPSSKSK QAAWGSSIRP IYTFATVEEF WSIYNNIHHP SKLGLGADFH
CFKHKIEPKW EDPICANGGK WTMTFPRGKS DTSWLYTLLA MIGEQFDHGD EICGAVVNVR
SRQDKIAIWT KNASNEAAQV SIGKQWKEFL DYNDTIGFIF HEDAKKLDRG AKNKYVV
