IF4G1_WHEAT
ID IF4G1_WHEAT Reviewed; 788 AA.
AC Q03387;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Eukaryotic translation initiation factor isoform 4G-1;
DE Short=eIF(iso)-4G-1;
DE Short=eIF(iso)4G-1;
DE AltName: Full=Eukaryotic initiation factor iso-4F subunit p82-34;
DE Short=eIF-(iso)4F p82-34 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 [MRNA], AND PROTEIN SEQUENCE OF 193-200; 255-284;
RP 411-419; 448-458 AND 681-688.
RC TISSUE=Root tip;
RX PubMed=1385417; DOI=10.1016/s0021-9258(18)50081-8;
RA Allen M.L., Metz A.M., Timmer R.T., Rhoads R.E., Browning K.S.;
RT "Isolation and sequence of the cDNAs encoding the subunits of the isozyme
RT form of wheat protein synthesis initiation factor 4F.";
RL J. Biol. Chem. 267:23232-23236(1992).
RN [2]
RP SEQUENCE REVISION.
RA Metz A.M.;
RL Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases.
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. Two forms of p82 have been
CC identified, p82-34 and p82-16.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
CC {ECO:0000305}.
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DR EMBL; M95747; AAA16209.1; -; mRNA.
DR PIR; A44452; A44452.
DR AlphaFoldDB; Q03387; -.
DR SMR; Q03387; -.
DR ELM; Q03387; -.
DR PRIDE; Q03387; -.
DR EnsemblPlants; TraesCAD_scaffold_026722_01G000100.1; TraesCAD_scaffold_026722_01G000100.1; TraesCAD_scaffold_026722_01G000100.
DR EnsemblPlants; TraesCLE_scaffold_010819_01G000100.1; TraesCLE_scaffold_010819_01G000100.1; TraesCLE_scaffold_010819_01G000100.
DR EnsemblPlants; TraesCS2D02G353600.1; TraesCS2D02G353600.1; TraesCS2D02G353600.
DR EnsemblPlants; TraesROB_scaffold_010397_01G000400.1; TraesROB_scaffold_010397_01G000400.1; TraesROB_scaffold_010397_01G000400.
DR EnsemblPlants; TraesWEE_scaffold_021246_01G000100.1; TraesWEE_scaffold_021246_01G000100.1; TraesWEE_scaffold_021246_01G000100.
DR Gramene; TraesCAD_scaffold_026722_01G000100.1; TraesCAD_scaffold_026722_01G000100.1; TraesCAD_scaffold_026722_01G000100.
DR Gramene; TraesCLE_scaffold_010819_01G000100.1; TraesCLE_scaffold_010819_01G000100.1; TraesCLE_scaffold_010819_01G000100.
DR Gramene; TraesCS2D02G353600.1; TraesCS2D02G353600.1; TraesCS2D02G353600.
DR Gramene; TraesROB_scaffold_010397_01G000400.1; TraesROB_scaffold_010397_01G000400.1; TraesROB_scaffold_010397_01G000400.
DR Gramene; TraesWEE_scaffold_021246_01G000100.1; TraesWEE_scaffold_021246_01G000100.1; TraesWEE_scaffold_021246_01G000100.
DR eggNOG; KOG0401; Eukaryota.
DR OMA; MEKDHQP; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; Q03387; baseline and differential.
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; 1.
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 Direct protein sequencing; Initiation factor; Protein biosynthesis;
KW Reference proteome; Translation regulation.
FT CHAIN 1..788
FT /note="Eukaryotic translation initiation factor isoform 4G-
FT 1"
FT /id="PRO_0000213334"
FT DOMAIN 211..436
FT /note="MIF4G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT DOMAIN 622..744
FT /note="MI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 788 AA; 86295 MW; 476DE9EE9DEE4715 CRC64;
MTTDQPVISL RPGGGGGGPR GGRLFAPAFA VAASGSGDFL RPHGGGASGV SRIGDLHSES
RERVRYSRDQ LLDLRKITDV TEQILRLQQE IEAELNGDDQ SWVRNDSNVQ LQTQAQPQVQ
AQNRFTETDN RDWRARTEKP PAPAVQEEKS WDNIREVKEQ YNASGRQQEQ FNRQDQSSSQ
KAQVGPPPAL IKADVPWSAR RGNLSEKDRV LKTVKGILNK LTPEKFDLLK GQLLDSGITT
ADILKDVISL IFEKAVFEPT FCPMYAQLCS ELNDNLPTFP SEEPGGKEIT FKRVLLNNCQ
EAFEGADSLR VEIASLTGPD QEMEKRDKER IFKLRTLGNI RLIGELLKQK MVPEKIVHHI
VKELLGSDKK ACPDEEHVEA ICQFFNTIGK QLDENPKSRR INDTYFVQIR ELVANPQLTP
RSKFMVRDLI DLRSNNWVPR RAEIKAKTIS EIHTEAEKNL GLRPGATANM RNGRNAPGGP
LSPGGFSVNR PGTGGMMPGM PGSRKMPGMP GLDNDNWEVQ RSRSMPRGDP LRNQGPLINK
VPSINKPSPI NPRLLPQGTG ALIGKSALLG TGGPPSRPSS LTASPTPLPA QTTASPKPSS
ATPASVPIPD KAASSAKVIP AGLQKKTASL LEEYFGIRIL DEAQQCIEEL QSPDYHPEIV
KEAINLALDK GASFVDPLVK LLEHLYTKKT FKTEDLENGC LLYGSLLEDI GIDLPKAPTQ
FGEVVARLIL SCGLRFEAAE GILKAMEDTF FRKAIFTSVT KTLGADPAGQ AILSSHAAVV
DACNSLSI
