IFI4E_CAPAN
ID IFI4E_CAPAN Reviewed; 202 AA.
AC A0A1U8F5V2; I2FKT8; I2FKU5; I2FKV3; Q4PZB3;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Eukaryotic translation initiation factor isoform 4E {ECO:0000303|PubMed:16760413, ECO:0000303|PubMed:21073716};
DE Short=eIF(iso)-4E {ECO:0000303|PubMed:16760413, ECO:0000303|PubMed:21073716};
DE Short=eIF(iso)4E {ECO:0000303|PubMed:16760413, ECO:0000303|PubMed:21073716};
DE AltName: Full=eIF-(iso)4F 25 kDa subunit {ECO:0000305};
DE AltName: Full=eIF-(iso)4F p28 subunit {ECO:0000305};
DE AltName: Full=mRNA cap-binding protein {ECO:0000305};
GN Name=eIFiso4E {ECO:0000303|PubMed:16760413, ECO:0000303|PubMed:21073716};
GN ORFNames=LOC107853558 {ECO:0000312|Proteomes:UP000189700};
OS Capsicum annuum (Capsicum pepper).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX NCBI_TaxID=4072;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, FUNCTION (MICROBIAL INFECTION),
RP DISRUPTION PHENOTYPE (MICROBIAL INFECTION), AND SUBUNIT (MICROBIAL
RP INFECTION).
RC STRAIN=cv. Florida VR2, cv. Yolo Wonder, and cv. Yolo Y;
RX PubMed=16760413; DOI=10.1099/vir.0.81817-0;
RA Ruffel S., Gallois J.-L., Moury B., Robaglia C., Palloix A., Caranta C.;
RT "Simultaneous mutations in translation initiation factors eIF4E and
RT eIF(iso)4E are required to prevent pepper veinal mottle virus infection of
RT pepper.";
RL J. Gen. Virol. 87:2089-2098(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Zunla-1;
RX PubMed=24591624; DOI=10.1073/pnas.1400975111;
RA Qin C., Yu C., Shen Y., Fang X., Chen L., Min J., Cheng J., Zhao S., Xu M.,
RA Luo Y., Yang Y., Wu Z., Mao L., Wu H., Ling-Hu C., Zhou H., Lin H.,
RA Gonzalez-Morales S., Trejo-Saavedra D.L., Tian H., Tang X., Zhao M.,
RA Huang Z., Zhou A., Yao X., Cui J., Li W., Chen Z., Feng Y., Niu Y., Bi S.,
RA Yang X., Li W., Cai H., Luo X., Montes-Hernandez S., Leyva-Gonzalez M.A.,
RA Xiong Z., He X., Bai L., Tan S., Tang X., Liu D., Liu J., Zhang S.,
RA Chen M., Zhang L., Zhang L., Zhang Y., Liao W., Zhang Y., Wang M., Lv X.,
RA Wen B., Liu H., Luan H., Zhang Y., Yang S., Wang X., Xu J., Li X., Li S.,
RA Wang J., Palloix A., Bosland P.W., Li Y., Krogh A., Rivera-Bustamante R.F.,
RA Herrera-Estrella L., Yin Y., Yu J., Hu K., Zhang Z.;
RT "Whole-genome sequencing of cultivated and wild peppers provides insights
RT into Capsicum domestication and specialization.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:5135-5140(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-202, FUNCTION, FUNCTION (MICROBIAL
RP INFECTION), VARIANTS THR-15; THR-16; GLU-20; THR-20; ALA-24; GLU-24;
RP SER-24; SER-27; ASN-56; ILE-63; THR-90; PRO-115 AND ILE-119, AND SUBUNIT
RP (MICROBIAL INFECTION).
RC STRAIN=cv. CDP01246, cv. CDP06433, and cv. CDP09688; TISSUE=Leaf;
RX PubMed=21073716; DOI=10.1186/1471-2164-11-631;
RA Ibiza V.P., Canizares J., Nuez F.;
RT "EcoTILLING in Capsicum species: searching for new virus resistances.";
RL BMC Genomics 11:631-631(2010).
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 (PubMed:16760413, PubMed:21073716).
CC {ECO:0000250|UniProtKB:O04663, ECO:0000250|UniProtKB:P29557,
CC ECO:0000269|PubMed:16760413, ECO:0000269|PubMed:21073716}.
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:16760413, ECO:0000269|PubMed:21073716}.
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:O04663}.
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:16760413,
CC ECO:0000305|PubMed:21073716}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0A445AGS0}.
CC Nucleus {ECO:0000250|UniProtKB:A0A445AGS0}.
CC -!- PTM: According to the redox status, the Cys-101-Cys-140 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) Truncated protein
CC associated with pvr6 resistance allele, correlates with resistance to
CC pepper veinal mottle virus (PVMV), especially when associated with the
CC pvr2(2) allele of eIF4E. {ECO:0000269|PubMed:16760413}.
CC -!- MISCELLANEOUS: Displayed sequence is from cv. Florida VR2, cv. Yolo Y
CC and cv. Yolo Wonder, cv. CDP06433, cv. CDP09688 and cv. Zunla-1, with
CC allele pvr6(+) (haplotype C1), and correlates with susceptibility to
CC pepper veinal mottle virus (PVMV). {ECO:0000305|PubMed:16760413,
CC ECO:0000305|PubMed:21073716}.
CC -!- MISCELLANEOUS: Plants harboring specific haplotypes couples for
CC eIF4E/eIF(iso)4E are resistant or tolerant to potyvirus such as potato
CC virus Y (PVY). {ECO:0000269|PubMed:21073716}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC {ECO:0000305}.
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DR EMBL; DQ022080; AAY62607.1; -; mRNA.
DR EMBL; DQ022081; AAY62608.1; -; mRNA.
DR EMBL; DQ022082; AAY62609.1; -; mRNA.
DR EMBL; FN824349; CBL94685.1; -; mRNA.
DR EMBL; FN824356; CBL94692.1; -; mRNA.
DR EMBL; FN824364; CBL94700.1; -; mRNA.
DR RefSeq; NP_001311631.1; NM_001324702.1.
DR RefSeq; XP_016554036.1; XM_016698550.1.
DR SMR; A0A1U8F5V2; -.
DR GeneID; 107853558; -.
DR KEGG; cann:107853558; -.
DR OrthoDB; 1394271at2759; -.
DR Proteomes; UP000189700; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0009615; P:response to virus; IEA:UniProt.
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; Initiation factor; Nucleus;
KW Protein biosynthesis; RNA-binding; Translation regulation.
FT CHAIN 1..202
FT /note="Eukaryotic translation initiation factor isoform 4E"
FT /id="PRO_0000454077"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 46..51
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 78
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 96..97
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 147..152
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 191..194
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 101..140
FT /evidence="ECO:0000250|UniProtKB:P29557"
FT VARIANT 15
FT /note="P -> T (in haplotype K1, allele pvr6(8))"
FT /evidence="ECO:0000269|PubMed:21073716"
FT VARIANT 16
FT /note="P -> T (in haplotype F1, allele pvr6(6))"
FT /evidence="ECO:0000269|PubMed:21073716"
FT VARIANT 20
FT /note="A -> E (in haplotypes G1 and G2, allele pvr6(9). In
FT haplotype E1, allele pvr6(5). In haplotype H1, allele
FT pvr6(7). In haplotype Ih1)"
FT /evidence="ECO:0000269|PubMed:21073716"
FT VARIANT 20
FT /note="A -> T (in haplotype A1, allele pvr6(2))"
FT /evidence="ECO:0000269|PubMed:21073716"
FT VARIANT 24
FT /note="V -> A (in haplotypes G1 and G2, allele pvr6(9). In
FT haplotype H1, allele pvr6(7))"
FT /evidence="ECO:0000269|PubMed:21073716"
FT VARIANT 24
FT /note="V -> E (in haplotype K1, allele pvr6(8))"
FT /evidence="ECO:0000269|PubMed:21073716"
FT VARIANT 24
FT /note="V -> S (in haplotype Ih1)"
FT /evidence="ECO:0000269|PubMed:21073716"
FT VARIANT 27
FT /note="P -> S (in haplotype B1, allele pvr6(3))"
FT /evidence="ECO:0000269|PubMed:21073716"
FT VARIANT 56
FT /note="K -> N (in haplotype K1, allele pvr6(8))"
FT /evidence="ECO:0000269|PubMed:21073716"
FT VARIANT 63
FT /note="V -> I (in haplotype H1, allele pvr6(7). In
FT haplotype Ih1)"
FT /evidence="ECO:0000269|PubMed:21073716"
FT VARIANT 90
FT /note="A -> T (in strain: cv. CDP01246; haplotype D1,
FT allele pvr6(4). In haplotype B1, allele pvr6(3))"
FT /evidence="ECO:0000269|PubMed:21073716"
FT VARIANT 115
FT /note="A -> P (in haplotype K1, allele pvr6(8))"
FT /evidence="ECO:0000269|PubMed:21073716"
FT VARIANT 119
FT /note="T -> I (in haplotype E1, allele pvr6(5))"
FT /evidence="ECO:0000269|PubMed:21073716"
SQ SEQUENCE 202 AA; 23037 MW; 25ED566C8A424B4C CRC64;
MATEAPPPVD TTEVPPFTAA ETAVKQPHKL ERKWTFWFDN QSKPKQGAAW GSSLKKAYTF
DTVEEFWSLY DQIFKPSKLT VNADFHLFKA GIEPKWEDPE CANGGKWTVT SSRKANLETM
WLETLMALVG EQFDDSEDIC GVVASVRRSQ DKLSLWTKTA TNEAAQMGIG RKWKEIIDTE
KISYSFHDDS KRERSAKSRY TV
