IF4E1_ARAHY
ID IF4E1_ARAHY Reviewed; 231 AA.
AC K0P2S0; A0A444WX02;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=Eukaryotic translation initiation factor 4E-1 {ECO:0000303|Ref.1};
DE Short=PeaeIF4E {ECO:0000303|Ref.1};
DE Short=eIF-4E-1 {ECO:0000303|Ref.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=eIF4E {ECO:0000303|Ref.1};
GN OrderedLocusNames=Ahy_B10g100505 {ECO:0000312|EMBL:RYQ81914.1};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Manlin X.;
RT "The function of eIF4E between peanut peanut stripe virus interaction.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Fuhuasheng; TISSUE=Leaf;
RX PubMed=31043757; DOI=10.1038/s41588-019-0402-2;
RA Zhuang W., Chen H., Yang M., Wang J., Pandey M.K., Zhang C., Chang W.C.,
RA Zhang L., Zhang X., Tang R., Garg V., Wang X., Tang H., Chow C.N., Wang J.,
RA Deng Y., Wang D., Khan A.W., Yang Q., Cai T., Bajaj P., Wu K., Guo B.,
RA Zhang X., Li J., Liang F., Hu J., Liao B., Liu S., Chitikineni A., Yan H.,
RA Zheng Y., Shan S., Liu Q., Xie D., Wang Z., Khan S.A., Ali N., Zhao C.,
RA Li X., Luo Z., Zhang S., Zhuang R., Peng Z., Wang S., Mamadou G.,
RA Zhuang Y., Zhao Z., Yu W., Xiong F., Quan W., Yuan M., Li Y., Zou H.,
RA Xia H., Zha L., Fan J., Yu J., Xie W., Yuan J., Chen K., Zhao S., Chu W.,
RA Chen Y., Sun P., Meng F., Zhuo T., Zhao Y., Li C., He G., Zhao Y., Wang C.,
RA Kavikishor P.B., Pan R.L., Paterson A.H., Wang X., Ming R., Varshney R.K.;
RT "The genome of cultivated peanut provides insight into legume karyotypes,
RT polyploid evolution and crop domestication.";
RL Nat. Genet. 51:865-876(2019).
RN [3]
RP FUNCTION, FUNCTION (MICROBIAL INFECTION), DISRUPTION PHENOTYPE (MICROBIAL
RP INFECTION), INTERACTION WITH POTYVIRUS HC-PRO AND VPG (MICROBIAL
RP INFECTION), TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Huayu 20;
RX PubMed=28344571; DOI=10.3389/fmicb.2017.00338;
RA Xu M., Xie H., Wu J., Xie L., Yang J., Chi Y.;
RT "Translation Initiation Factor eIF4E and eIFiso4E are both required for
RT peanut stripe virus infection in peanut (Arachis hypogaea L.).";
RL Front. Microbiol. 8:338-338(2017).
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 such as peanut stripe virus (PStV)
CC (PubMed:28344571). {ECO:0000250|UniProtKB:A0A075QQ08,
CC ECO:0000269|PubMed:28344571}.
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:28344571}.
CC -!- SUBUNIT: EIF4F is a multi-subunit complex, the composition of which
CC varies with external and internal environmental conditions (By
CC similarity). It is composed of at least EIF4A, EIF4E and EIF4G (By
CC similarity). EIF4E is also known to interact with other partners (By
CC similarity). In higher plants two isoforms of EIF4F have been
CC identified, named isoform EIF4F and isoform EIF(iso)4F (By similarity).
CC Isoform EIF4F has subunits p220 and p26, whereas isoform EIF(iso)4F has
CC subunits p82 and p28 (By similarity). {ECO:0000250|UniProtKB:P29557}.
CC -!- SUBUNIT: (Microbial infection) Interacts with potyvirus peanut stripe
CC virus (PStV) helper component proteinase (HC-Pro) in the cytoplasm and
CC with PStV viral genome-linked protein (VPg) in the nucleus; these
CC interactions are possible in susceptible hosts but impaired in
CC resistant plants. {ECO:0000269|PubMed:28344571}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28344571}. Cytoplasm
CC {ECO:0000269|PubMed:28344571}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously with highest levels in young
CC leaves and roots, and lowest levels in flowers.
CC {ECO:0000269|PubMed:28344571}.
CC -!- PTM: According to the redox status, the Cys-129-Cys-167 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) No significant resistance
CC against peanut stripe virus (PStV) (PubMed:28344571). Plants lacking
CC both eIF4E and eIF(iso)4E exhibit an increased resistance against PStV
CC (PubMed:28344571). {ECO:0000269|PubMed:28344571}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=RYQ81915.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; HE985069; CCM43797.1; -; mRNA.
DR EMBL; SDMP01000020; RYQ81914.1; -; Genomic_DNA.
DR EMBL; SDMP01000020; RYQ81915.1; ALT_SEQ; Genomic_DNA.
DR STRING; 3818.K0P2S0; -.
DR Proteomes; UP000289738; Chromosome b10.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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:0051607; P:defense response to virus; IMP: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..231
FT /note="Eukaryotic translation initiation factor 4E-1"
FT /id="PRO_0000454053"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..59
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT REGION 66..102
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT REGION 150..159
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 74..79
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 106
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 124..125
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 174..179
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 219..223
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 129..167
FT /evidence="ECO:0000250|UniProtKB:P29557"
SQ SEQUENCE 231 AA; 26138 MW; 06807AC9C93FC132 CRC64;
MVVEDTQKSS ITDDQITANP NNENEDLEEG EILDDDDSSA TSRPPSSSGA LARNPHPLEN
SWTFWFDNPS AKSKQAAWGS SIRPIYTFAT VEEFWSIYNN IHHPSKLAVG ADFHCFKHKI
EPKWEDPICA NGGKWTMTFP RGKSDTSWLY TLLGMIGEQF DHGDEICGAV VNVRNRQEKI
ALWTKNAANE AAQVSIGKQW KEFLDYNDTI GFIFHEDAKK HDRAAKNKYV I
