ID   IF4G2_WHEAT             Reviewed;         787 AA.
AC   Q41583;
DT   09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Eukaryotic translation initiation factor isoform 4G-2;
DE            Short=eIF(iso)-4G-2;
DE            Short=eIF(iso)4G-2;
DE   AltName: Full=Eukaryotic initiation factor iso-4F subunit p82-16;
DE            Short=eIF-(iso)4F p82-16 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].
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).
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
CC       {ECO:0000305}.
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DR   EMBL; M95746; AAA74724.1; -; mRNA.
DR   AlphaFoldDB; Q41583; -.
DR   SMR; Q41583; -.
DR   MINT; Q41583; -.
DR   STRING; 4565.Traes_2AL_57DF7CC48.1; -.
DR   PRIDE; Q41583; -.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; Q41583; 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   2: Evidence at transcript level;
KW   Initiation factor; Protein biosynthesis; Reference proteome;
KW   Translation regulation.
FT   CHAIN           1..787
FT                   /note="Eukaryotic translation initiation factor isoform 4G-
FT                   2"
FT                   /id="PRO_0000420548"
FT   DOMAIN          210..435
FT                   /note="MIF4G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT   DOMAIN          621..743
FT                   /note="MI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          112..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          514..607
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..155
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..183
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..551
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        572..600
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   787 AA;  86580 MW;  C3FA312F17E8AF73 CRC64;
     MTTDQPVISL RPGGGGGGPR GGRLFAPAFA VAASGSGDFL RPHGGGAFRA LQDWCLHLSH
     ERVRYSRDQL LDLRKITDVT EQILRLQQEI EAELHGDDQS WVRNDSNVQL QTQTQTQVQA
     QNRFTETDNR DWRARTEKPP APAVPEEKSW DNIREVKEQY NASGRQQEQF NRQDQSSSQK
     AQVGPPPALI KADVPWSARR GNLSEKDRVL KTVKGILNKL TPEKFDLLKG ELLDSGITTA
     DILKDVISLI FEKAVFEPTF CPMYAQLCSE LNDNLPKFPS EEPGGKEITF KRVLLNNCQE
     AFEGADSLRV EIASLTGPDQ EMEKRDKERI FKLRTLGNIR LIGELLKQKM VPEKIVHHIV
     KELLGSDKKA CPDEEHVEAI CQFFNTIGKQ LDENPKSRRI NDTYFVHLRE LVANPQLTPR
     SKFMVRDLID LRSNNWVPRR AEIKAKTISE IHTEAEKNLG LRPGATANMR NGRNAPGGPL
     SPGGFSVNRP GTGGMMPGMP GSRKMPGMPG LDNDNWEVQR SRSMPRGDPL RNQGSLINKV
     SSINKPSPIN PRLLPQGTGA LIGKSALLGT GGPPSRPSSI TASPTPLPAQ TTASPKPSSA
     TPASVPIPDK AASSAKVIPA GLEKKTASLL EEYFGIRILD EAQQCIEELQ SPDYHPEIVK
     EAINLALDKG ASFVDPLVKL LEHLYTKKTF KTEDLENGCL LYGSLLEDIG IDLPKAPTQF
     GEVIARLILS CGLRFEAVEG ILKAMEDTFF RKAIFTSVTK TLEADPAGQA ILSSHAAVVD
     ACNSLSI