IF4G_WHEAT
ID IF4G_WHEAT Reviewed; 1488 AA.
AC G5CEW6;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Eukaryotic translation initiation factor 4G;
DE Short=eIF-4G;
DE Short=eIF4G;
DE AltName: Full=Eukaryotic initiation factor 4F subunit p220;
DE Short=eIF-4F p220 subunit;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBUNIT.
RX PubMed=21965660; DOI=10.1074/jbc.m111.280099;
RA Mayberry L.K., Allen M.L., Nitka K.R., Campbell L., Murphy P.A.,
RA Browning K.S.;
RT "Plant cap-binding complexes eukaryotic initiation factors eIF4F and
RT eIFiso4F: molecular specificity of subunit binding.";
RL J. Biol. Chem. 286:42566-42574(2011).
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.
CC {ECO:0000250}.
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. In higher plants two
CC isoforms of EIF4F have been identified, named isoform EIF4F and isoform
CC EIF(iso)4F. Isoform EIF4F has subunits p220 and p26, whereas isoform
CC EIF(iso)4F has subunits p82 and p28. {ECO:0000269|PubMed:21965660}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
CC {ECO:0000305}.
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DR EMBL; JN091779; AEQ49596.1; -; Genomic_DNA.
DR AlphaFoldDB; G5CEW6; -.
DR SMR; G5CEW6; -.
DR STRING; 4565.Traes_2BS_80474BB5B.1; -.
DR eggNOG; KOG0401; Eukaryota.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; G5CEW6; baseline.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR045208; IF4G.
DR InterPro; IPR003891; Initiation_fac_eIF4g_MI.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR PANTHER; PTHR23253; PTHR23253; 2.
DR Pfam; PF02847; MA3; 1.
DR Pfam; PF02854; MIF4G; 1.
DR SMART; SM00544; MA3; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR PROSITE; PS51366; MI; 1.
PE 1: Evidence at protein level;
KW Initiation factor; Protein biosynthesis; Reference proteome;
KW Translation regulation.
FT CHAIN 1..1488
FT /note="Eukaryotic translation initiation factor 4G"
FT /id="PRO_0000420547"
FT DOMAIN 883..1106
FT /note="MIF4G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT DOMAIN 1299..1423
FT /note="MI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT REGION 196..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..721
FT /note="EIF4E-binding"
FT REGION 753..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1107..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..679
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..781
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1242..1257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1271..1291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1488 AA; 162229 MW; 4031EFB00C8C8528 CRC64;
MMHQGQTMMY PSVAHPIPPQ LGNVNLNMAS QYPQQQQNKL VAPRKSSNIK ITDPNTNKEV
VLGRPSPNVA AQPQQVSGVA TQPMVYYTNP QQTSYNQSGT YYSGTAGVVP TGSQGRFGYP
ATQAGQSIPF MNPSMSNTVP ASHKDNIAGP APSGQSQLIG KPQGGLHMEK PVPSVKISMP
AGRSDASKFR VADHAVQHRQ KDNEVISGAM VSNKPVSEKE SKAPSIPEKH SKESKAPSAV
EKHPTAVTQP LPIQAAKPET DAATANSPSF LTGADEKKES LPMTDSLKDN KKNATRNDTK
NLPQQPQSAS PAEELKGQTS VKLGDDVVGH METKSFDSEK VDLTSKVSGL TSATSESSIS
PILGKSEADS TSVNAADVPA MVISSAKLSS ASTGEPQAVE SLGVAAVKSK EIEITHQISP
ESSDGKIMSD STENESHDFT VDLAEQASLA TSKPGNSDAT SFVTDPQELP KECTTSVPED
HSLMNTSHNK DTQTLSASVD ASDVSEVNSG TSSESTSQST NDKDIRSSIQ ETGLAVSGIT
PGMLPVNHSV ASEGQVKHAD GAKDESSTEQ SSAVPTGSVR PLSREKPTAE LARTKSTAGR
KKKRKEMLSK ADAAGSSDLY NAYKGPQEQS ESVATSDGAD SSSTVDGTHV LPEESEREVM
CEDDGKKKVE PDDWEDAADM STPKLQSSDS GNQASAVQLP DSDMTEANGR KKYSRDFLLT
FAHQYSSLPV GIRMDTVTST LFKDLAGKSY VIDREPHPSS ARGSDRPTSR GDRRGPAMDD
DKWLKSGVPY SPNRDAHMDL TNGPAINYRG GPGGAHGVLR NPRGALLVGP QSNAPQVPRS
GSDADRWQQK GLIPSPVTPM QVMHKAEKKY VVGKVSDEEQ AKQRQLKAIL NKLTPQNFDK
LFEQVKEVNI DNVSTLTGVI SQIFDKALME PTFCEMYANF CSHLAGALPD FSEDNEKITF
KRLLLNKCQE EFERGEREEA EADKTEEEGE IKQTKEEREE KRVKARRRML GNIRLIGELY
KKRMLTERIM HECIKKLLGN YQNPDEENIE ALCKLMSTIG EMIDHPKAKE HMDAYFDRMR
NLSTSQLISS RVRFLLRDSI DLRKNKWQQR RKVDGPKKID EVHRDAAQER HAQSSRSRGP
VVSSLPRRGA PSMDYGSRGS AAPLVSPGPQ QRGRGFGNQD IRYEQERHQF DRTVPLPQRS
VKDEAITLGP QGGLARGMSL RGQPPVSNSE LPSVVDQRRI LSGPNGYNSV PSTTREDTSS
RIPDRFSGRI ATAAQSASSS HRPASQEGRS GNKSYSEEEL REKSIATIRE YYSAKDEKEV
ALCIEELNAP SFYPSLVSLW VNDSFERKDM ERELLAKLFV GLYNGGYNLL SKPQLIEGLS
SVLASLEDAL SDSPRAAEYL GRLLARFVVE KILVLQDVGK LIEEGGEEPG HLVQEGIAAD
VLGAVLEWIR TEKGDSFLKE AKTSSNLKLE DFRPQHLKRS KLDAFMLT