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IFI4E_ARAHY
ID   IFI4E_ARAHY             Reviewed;         203 AA.
AC   A0A445AGS0; W8GH57;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   08-MAY-2019, sequence version 1.
DT   03-AUG-2022, entry version 9.
DE   RecName: Full=Eukaryotic translation initiation factor isoform 4E {ECO:0000303|Ref.1};
DE            Short=PeaeIF(iso)4E {ECO:0000303|Ref.1};
DE            Short=eIF(iso)-4E {ECO:0000303|Ref.1};
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=eIF(iso)4E {ECO:0000303|Ref.1};
GN   OrderedLocusNames=Ahy_B02g059482 {ECO:0000312|EMBL:RYR25631.1};
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   Chi Y., Xie H., Yang J.;
RL   Submitted (DEC-2013) 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, INTERACTION
RP   WITH POTYVIRUS HC-PRO AND VPG (MICROBIAL INFECTION), TISSUE SPECIFICITY,
RP   SUBCELLULAR LOCATION, AND SUBCELLULAR LOCATION (MICROBIAL INFECTION).
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:Q66WU1,
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:O04663}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with the potyvirus peanut
CC       stripe virus (PStV) helper component proteinase (HC-Pro) in the
CC       cytoplasm and with PStV viral genome-linked protein (VPg) in the
CC       nucleus; these interactions are possible in susceptible hosts but
CC       impaired in resistant plants. {ECO:0000269|PubMed:28344571}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28344571}. Nucleus
CC       {ECO:0000269|PubMed:28344571}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28344571}. Nucleus
CC       {ECO:0000269|PubMed:28344571}. Note=(Microbial infection) Binds to
CC       potyvirus viral genome-linked protein (VPg) in the nucleus and with
CC       viral helper component proteinase (HC-Pro) in the 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-102-Cys-141 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}.
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DR   EMBL; KF956378; AHK23094.1; -; mRNA.
DR   EMBL; SDMP01000012; RYR25631.1; -; Genomic_DNA.
DR   STRING; 3818.A0A445AGS0; -.
DR   Proteomes; UP000289738; Chromosome b02.
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..203
FT                   /note="Eukaryotic translation initiation factor isoform 4E"
FT                   /id="PRO_0000454073"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         47..52
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         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         97..98
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         148..153
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   DISULFID        102..141
FT                   /evidence="ECO:0000250|UniProtKB:P29557"
FT   CONFLICT        166..167
FT                   /note="AQ -> TH (in Ref. 1; AHK23094)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   203 AA;  22953 MW;  DE845006A15ED89B CRC64;
     MATETAGAVV ESSSAATVPS PAPEAGSKHK LERKWTFWFD NQSKPKQGAA WGTSLREVYT
     FDTVEEFWCL YDQVFKPSKL PGNADFHLFK TGIEPKWEDP ECAKGGKWTV TSNRKANLDN
     MWLETMMALI GEQFDDAEDI CGVVASVRQR QDKLSLWTKT AANEAAQMGI GRKWKEIIDV
     TDKIIYNFHD DSRTRSSKSR YSV
 
 
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