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IF4E1_LACSA
ID   IF4E1_LACSA             Reviewed;         235 AA.
AC   A0A2J6L8Y7; Q7XJB1;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2018, sequence version 1.
DT   03-AUG-2022, entry version 17.
DE   RecName: Full=Eukaryotic translation initiation factor 4E-1 {ECO:0000303|PubMed:12857809};
DE            Short=Ls-eIF4E-1 {ECO:0000303|PubMed:12857809};
DE            Short=eIF-4E-1 {ECO:0000303|PubMed:12857809};
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:12857809};
GN   Name=eIF4E {ECO:0000303|PubMed:12857809};
GN   ORFNames=LSAT_4X27581 {ECO:0000312|EMBL:PLY83747.1};
OS   Lactuca sativa (Garden lettuce).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Cichorioideae; Cichorieae;
OC   Lactucinae; Lactuca.
OX   NCBI_TaxID=4236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, FUNCTION (MICROBIAL INFECTION),
RP   VARIANTS PRO-75; 113-GLN--ALA-115 DELINS HIS AND SER-191, SUBUNIT
RP   (MICROBIAL INFECTION), AND POLYMORPHISM.
RC   STRAIN=cv. 87-20M, cv. Floribibb, cv. Malika, cv. Mantilia, cv. Salinas,
RC   cv. Salinas 88, cv. Vanguard, and cv. Vanguard 75;
RX   PubMed=12857809; DOI=10.1104/pp.102.017855;
RA   Nicaise V., German-Retana S., Sanjuan R., Dubrana M.-P., Mazier M.,
RA   Maisonneuve B., Candresse T., Caranta C., LeGall O.;
RT   "The eukaryotic translation initiation factor 4E controls lettuce
RT   susceptibility to the Potyvirus Lettuce mosaic virus.";
RL   Plant Physiol. 132:1272-1282(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Salinas;
RX   PubMed=28401891; DOI=10.1038/ncomms14953;
RA   Reyes-Chin-Wo S., Wang Z., Yang X., Kozik A., Arikit S., Song C., Xia L.,
RA   Froenicke L., Lavelle D.O., Truco M.J., Xia R., Zhu S., Xu C., Xu H.,
RA   Xu X., Cox K., Korf I., Meyers B.C., Michelmore R.W.;
RT   "Genome assembly with in vitro proximity ligation data and whole-genome
RT   triplication in lettuce.";
RL   Nat. Commun. 8:14953-14953(2017).
RN   [3]
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 (PubMed:12857809).
CC       {ECO:0000250|UniProtKB:P29557, ECO:0000269|PubMed:12857809}.
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:12857809}.
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:12857809}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C6ZJZ3}. Cytoplasm
CC       {ECO:0000250|UniProtKB:C6ZJZ3}.
CC   -!- PTM: According to the redox status, the Cys-133-Cys-171 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 strains cv. Autumn Gold, cv.
CC       Desert Storm, cv. Salinas 88 and cv. Vanguard 75, alleles mo1(2) and
CC       Ls-eIF4E(2), confers an increased resistance to lettuce mosaic virus
CC       (LMV). {ECO:0000269|PubMed:12857809}.
CC   -!- POLYMORPHISM: Variant present in the strains cv. Alize, cv. Classic,
CC       cv. Floribibb, cv. Malika, cv. Mantilia, cv. Oriana and cv. Presidio,
CC       alleles mo1(1) and Ls-eIF4E(1), confers an increased resistance to
CC       lettuce mosaic virus (LMV). {ECO:0000269|PubMed:12857809}.
CC   -!- MISCELLANEOUS: Displayed sequence is from cv. Salinas, cv. Fiona, cv.
CC       Girelle, cv. Jessy, cv. Vanguard, cv. Mariska, cv. Trocadero and cv.
CC       87-20M, allele Ls-eIF4E(0), and is associated with susceptibility to
CC       lettuce mosaic virus (LMV). {ECO:0000269|PubMed:12857809}.
CC   -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC       {ECO:0000305}.
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DR   EMBL; AF530162; AAP86602.1; -; mRNA.
DR   EMBL; NBSK01004716; PLY83747.1; -; Genomic_DNA.
DR   STRING; 4236.A0A2J6L8Y7; -.
DR   EnsemblPlants; rna-gnl|WGS:NBSK|LSAT_4X27581_mrna; cds-PLY83747.1; gene-LSAT_4X27581.
DR   Gramene; rna-gnl|WGS:NBSK|LSAT_4X27581_mrna; cds-PLY83747.1; gene-LSAT_4X27581.
DR   OrthoDB; 1394271at2759; -.
DR   Proteomes; UP000235145; Unassembled WGS sequence.
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..235
FT                   /note="Eukaryotic translation initiation factor 4E-1"
FT                   /id="PRO_0000454070"
FT   REGION          16..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          60..63
FT                   /note="EIF4G-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT   REGION          70..106
FT                   /note="EIF4G-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT   REGION          154..163
FT                   /note="EIF4G-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT   COMPBIAS        42..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         78..83
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         110
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         128..129
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         178..183
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         223..227
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        133..171
FT                   /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT   VARIANT         75
FT                   /note="A -> P (in strain: Autumn Gold, Desert Storm,
FT                   Salinas 88 and Vanguard 75, alleles mo1(2) and Ls-
FT                   eIF4E(2))"
FT                   /evidence="ECO:0000269|PubMed:12857809"
FT   VARIANT         113..115
FT                   /note="QGA -> H (in strain: Alize, Classic, Floribibb,
FT                   Malika, Mantilia, Oriana and Presidio, alleles mo1(1) and
FT                   Ls-eIF4E(1))"
FT                   /evidence="ECO:0000269|PubMed:12857809"
FT   VARIANT         191
FT                   /note="A -> S (in strain: Alize, Classic, Floribibb,
FT                   Malika, Mantilia, Oriana and Presidio, alleles mo1(1) and
FT                   Ls-eIF4E(1))"
FT                   /evidence="ECO:0000269|PubMed:12857809"
FT   CONFLICT        1
FT                   /note="M -> G (in Ref. 1; AAP86602)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   235 AA;  26678 MW;  D444A2B03451ABE0 CRC64;
     MVEEIMKSEE QKLIDVNKHR GVRSDGEEDE QLEEGEIVGG DADTLSSSSS SRPGTAIAQH
     PLEHSWTFWF DTPSAKSKQV AWGSSMRPIY TFSSVEEFWS LYNNIHRPSK LAQGADFYCF
     KNKIEPKWED PVCANGGKWT MTFTKAKSDT CWLYTLLAMI GEQFDHGDDI CGAVVNVRAR
     QEKIALWTKN AANESAQLSI GKQWKEFIDY NDTIGFIFHE DAKTLDRSAK NKYTV
 
 
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