IF4E1_MAIZE
ID IF4E1_MAIZE Reviewed; 218 AA.
AC O81481; A0A3L6FH01; B4G0T4; B6TBD1; D5KXY1;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Eukaryotic translation initiation factor 4E-1 {ECO:0000303|PubMed:10417723};
DE Short=ZmeIF4E {ECO:0000303|PubMed:23474695};
DE Short=eIF-4E-1 {ECO:0000303|PubMed:10417723};
DE Short=eIF4E-1 {ECO:0000303|PubMed:10417723};
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:10417723};
GN Name=eIF4E1 {ECO:0000303|PubMed:10417723};
GN Synonyms=eif6 {ECO:0000305}, PCO081734 {ECO:0000305};
GN ORFNames=ZEAMMB73_Zm00001d041682 {ECO:0000312|EMBL:ONM33473.1},
GN Zm00014a_030232 {ECO:0000312|EMBL:PWZ32524.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PHOSPHORYLATION.
RC STRAIN=cv. B73 Inbred; TISSUE=Root;
RX PubMed=10417723; DOI=10.1046/j.1365-313x.1999.00489.x;
RA Manjunath S., Williams A.J., Bailey-Serres J.;
RT "Oxygen deprivation stimulates Ca2+-mediated phosphorylation of mRNA cap-
RT binding protein eIF4E in maize roots.";
RL Plant J. 19:21-30(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION BY ETHYLENE; JASMONIC ACID
RP AND SALICYLIC ACID.
RC STRAIN=cv. X178, and cv. Ye478;
RX PubMed=23474695; DOI=10.1007/s00438-013-0737-9;
RA Shi L., Weng J., Liu C., Song X., Miao H., Hao Z., Xie C., Li M., Zhang D.,
RA Bai L., Pan G., Li X., Zhang S.;
RT "Identification of promoter motifs regulating ZmeIF4E expression level
RT involved in maize rough dwarf disease resistance in maize (Zea Mays L.).";
RL Mol. Genet. Genomics 288:89-99(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73; TISSUE=Seedling;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Missouri 17; TISSUE=Seedling;
RX PubMed=30061735; DOI=10.1038/s41588-018-0182-0;
RA Sun S., Zhou Y., Chen J., Shi J., Zhao H., Zhao H., Song W., Zhang M.,
RA Cui Y., Dong X., Liu H., Ma X., Jiao Y., Wang B., Wei X., Stein J.C.,
RA Glaubitz J.C., Lu F., Yu G., Liang C., Fengler K., Li B., Rafalski A.,
RA Schnable P.S., Ware D.H., Buckler E.S., Lai J.;
RT "Extensive intraspecific gene order and gene structural variations between
RT Mo17 and other maize genomes.";
RL Nat. Genet. 50:1289-1295(2018).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA Zhang H., Swaller T.J., Lu Y.-P., Bouck J., Flavell R.B., Feldmann K.A.;
RT "Insights into corn genes derived from large-scale cDNA sequencing.";
RL Plant Mol. Biol. 69:179-194(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. B73;
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
RN [7]
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). {ECO:0000250|UniProtKB:P29557}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C6ZJZ3}. Cytoplasm
CC {ECO:0000250|UniProtKB:C6ZJZ3}.
CC -!- INDUCTION: Induced by ethylene (ETH), jasmonic acid (JA) and salicylic
CC acid (SA), mainly in lines (e.g. cv. Ye478) susceptible to potyvirus
CC such as maize rough dwarf virus (MRDV). {ECO:0000269|PubMed:23474695}.
CC -!- PTM: According to the redox status, the Cys-116-Cys-154 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 -!- PTM: Phosphorylated upon oxygen deprivation.
CC {ECO:0000269|PubMed:10417723}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC {ECO:0000305}.
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DR EMBL; AF076954; AAC27714.1; -; mRNA.
DR EMBL; GU723473; ADE22251.1; -; Genomic_DNA.
DR EMBL; CM007649; ONM33473.1; -; Genomic_DNA.
DR EMBL; NCVQ01000004; PWZ32524.1; -; Genomic_DNA.
DR EMBL; EU962296; ACG34414.1; -; mRNA.
DR EMBL; BT042972; ACF87977.1; -; mRNA.
DR EMBL; BT043330; ACF88335.1; -; mRNA.
DR PIR; T01686; T01686.
DR RefSeq; NP_001105612.1; NM_001112142.1.
DR AlphaFoldDB; O81481; -.
DR SMR; O81481; -.
DR STRING; 4577.GRMZM2G002616_P01; -.
DR PaxDb; O81481; -.
DR EnsemblPlants; Zm00001eb137550_T001; Zm00001eb137550_P001; Zm00001eb137550.
DR GeneID; 542608; -.
DR Gramene; Zm00001eb137550_T001; Zm00001eb137550_P001; Zm00001eb137550.
DR MaizeGDB; 320756; -.
DR eggNOG; KOG1670; Eukaryota.
DR HOGENOM; CLU_043552_2_1_1; -.
DR OMA; WHDLLLC; -.
DR OrthoDB; 1394271at2759; -.
DR Proteomes; UP000007305; Chromosome 3.
DR Proteomes; UP000251960; Chromosome 3.
DR ExpressionAtlas; O81481; baseline and differential.
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:0034059; P:response to anoxia; IDA:AgBase.
DR GO; GO:0009723; P:response to ethylene; IEP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR GO; GO:0009751; P:response to salicylic acid; IEP: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; Initiation factor; Nucleus; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; RNA-binding;
KW Translation regulation.
FT CHAIN 1..218
FT /note="Eukaryotic translation initiation factor 4E-1"
FT /id="PRO_0000193658"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..46
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT REGION 53..89
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT REGION 137..146
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT BINDING 61..66
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 93
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 111..112
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 161..166
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 206..210
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 116..154
FT /evidence="ECO:0000250|UniProtKB:P29557"
FT CONFLICT 13
FT /note="G -> S (in Ref. 5; ACG34414)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="L -> I (in Ref. 5; ACG34414)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="W -> L (in Ref. 2; ADE22251)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="N -> E (in Ref. 1; AAC27714)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 218 AA; 24455 MW; 3E26C118D7131D11 CRC64;
MAEETDTRPA SAGSRGRPAP EDDDREEGEI TDLACAPSPP ATHPLEHSWT FWFDNPQSKS
KQAAWGSSIR PIHTFSTVEE FWGLYNNINH PSKLIVGADF HCFKNKIEPK WEDPICANGG
KWTISCGRGK SDTFWLHTLL AMIGEQFDYG DEICGAVVSV RGKQERIAIW TKNAANEAAQ
VSIGKQWKEL LDYKDSIGFI VHDDAKKMDK GLKNRYTV
