IF4E1_PRUDO
ID IF4E1_PRUDO Reviewed; 233 AA.
AC M1JJT8;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=Eukaryotic translation initiation factor 4E-1 {ECO:0000303|PubMed:23382802};
DE Short=eIF-4E-1 {ECO:0000303|PubMed:23382802};
DE Short=eIF4E-1 {ECO:0000303|PubMed:23382802};
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|PubMed:23382802};
OS Prunus domestica (Garden plum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=3758;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION (MICROBIAL INFECTION), DISRUPTION
RP PHENOTYPE (MICROBIAL INFECTION), TISSUE SPECIFICITY, AND SUBUNIT (MICROBIAL
RP INFECTION).
RX PubMed=23382802; DOI=10.1371/journal.pone.0050627;
RA Wang X., Kohalmi S.E., Svircev A., Wang A., Sanfacon H., Tian L.;
RT "Silencing of the host factor eIF(iso)4E gene confers plum pox virus
RT resistance in plum.";
RL PLoS ONE 8:e50627-e50627(2013).
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).
CC {ECO:0000250|UniProtKB:A0A075QQ08}.
CC -!- FUNCTION: (Microbial infection) Not involved in the plum pox virus
CC (PPV) strain D infection process. {ECO:0000269|PubMed:23382802}.
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) Does not interact with the VPg of Plum
CC pox virus (PPV) strain D. {ECO:0000269|PubMed:23382802}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C6ZJZ3}. Cytoplasm
CC {ECO:0000250|UniProtKB:C6ZJZ3}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in leaves, flower buds, leaf buds
CC and anthers, to a lower extent in roots, stems and green immature
CC fruit, and, at low levels, in petals. {ECO:0000269|PubMed:23382802}.
CC -!- PTM: According to the redox status, the Cys-131-Cys-169 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) Not observable resistance
CC to Plum pox virus (PPV) strain D. {ECO:0000269|PubMed:23382802}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC {ECO:0000305}.
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DR EMBL; JX137116; AGE81987.1; -; mRNA.
DR SMR; M1JJT8; -.
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:0051607; P:defense 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..233
FT /note="Eukaryotic translation initiation factor 4E-1"
FT /id="PRO_0000454054"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..58
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT REGION 65..104
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT REGION 152..161
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT BINDING 76..81
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
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 126..127
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 176..181
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 221..225
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 131..169
FT /evidence="ECO:0000250|UniProtKB:P29557"
SQ SEQUENCE 233 AA; 26429 MW; 049FE5134F7FAC25 CRC64;
MVVEDALKTS ASEDQAKTET NPKPREEDDE PEEGEIVGDE ESASKPSKGI APESHALEHS
WTFWFDSPAA KSAKTKQEDW GSSIRPIYTF STVEEFWSIY NNIRHPSKLA IGTDFHCFKY
KIEPKWEDPV CANGGKWTVT LPKGKSDTSW LYTLLGMIGE QFDHGDEICG AVVNVRNRQE
KISIWTKNAI NEAAQLSIGK QWKGLLDYNE TIGFIFHEDA MRHERSAKNK YVV
