IF4B1_WHEAT
ID IF4B1_WHEAT Reviewed; 527 AA.
AC Q9AUJ7; Q9M7E9; Q9M7F1;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Eukaryotic translation initiation factor 4B1 {ECO:0000303|PubMed:10600500};
DE Short=TaTif4B1 {ECO:0000303|PubMed:10600500};
DE Short=eIF4B {ECO:0000303|PubMed:10600500};
GN Name=EIF4B {ECO:0000303|PubMed:10600500};
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 {ECO:0000312|EMBL:AAC28254.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, HOMODIMERIZATION, GENE
RP FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Chinese Spring;
RX PubMed=10600500; DOI=10.1006/bbrc.1999.1814;
RA Metz A.M., Wong K.C., Malmstrom S.A., Browning K.S.;
RT "Eukaryotic initiation factor 4B from wheat and Arabidopsis thaliana is a
RT member of a multigene family.";
RL Biochem. Biophys. Res. Commun. 266:314-321(1999).
RN [2]
RP FUNCTION, AND SUBUNIT.
RX PubMed=19493973; DOI=10.1104/pp.109.138438;
RA Mayberry L.K., Allen M.L., Dennis M.D., Browning K.S.;
RT "Evidence for variation in the optimal translation initiation complex:
RT plant eIF4B, eIF4F, and eIF(iso)4F differentially promote translation of
RT mRNAs.";
RL Plant Physiol. 150:1844-1854(2009).
CC -!- FUNCTION: Promotes the eIF4F and eIF4A RNA-dependent ATP-hydrolysis
CC activity with different efficiency depending on mRNAs, thus providing
CC mRNA discrimination during initiation of translation.
CC {ECO:0000269|PubMed:10600500, ECO:0000269|PubMed:19493973}.
CC -!- SUBUNIT: Homodimer (PubMed:10600500, PubMed:19493973). Nonspherical
CC monomer. mRNA-discriminating component of initiation complexes (By
CC similarity) (PubMed:19493973). {ECO:0000250|UniProtKB:Q9LIN5,
CC ECO:0000269|PubMed:10600500, ECO:0000269|PubMed:19493973}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:10600500}.
CC -!- SIMILARITY: Belongs to the eIF-4 subunit B family. {ECO:0000305}.
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DR EMBL; AF021243; AAC28254.1; -; Genomic_DNA.
DR EMBL; AF136004; AAF27284.1; -; mRNA.
DR EMBL; AF136006; AAF27286.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9AUJ7; -.
DR SMR; Q9AUJ7; -.
DR MINT; Q9AUJ7; -.
DR STRING; 4565.Traes_2BL_89B629D3F.2; -.
DR PRIDE; Q9AUJ7; -.
DR EnsemblPlants; TraesCAD_scaffold_012277_01G000100.1; TraesCAD_scaffold_012277_01G000100.1; TraesCAD_scaffold_012277_01G000100.
DR EnsemblPlants; TraesCS2D02G337300.1; TraesCS2D02G337300.1; TraesCS2D02G337300.
DR EnsemblPlants; TraesWEE_scaffold_004053_01G000100.1; TraesWEE_scaffold_004053_01G000100.1; TraesWEE_scaffold_004053_01G000100.
DR Gramene; TraesCAD_scaffold_012277_01G000100.1; TraesCAD_scaffold_012277_01G000100.1; TraesCAD_scaffold_012277_01G000100.
DR Gramene; TraesCS2D02G337300.1; TraesCS2D02G337300.1; TraesCS2D02G337300.
DR Gramene; TraesWEE_scaffold_004053_01G000100.1; TraesWEE_scaffold_004053_01G000100.1; TraesWEE_scaffold_004053_01G000100.
DR eggNOG; ENOG502QVPR; Eukaryota.
DR OMA; TPEEMMM; -.
DR Proteomes; UP000019116; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR InterPro; IPR010433; EIF-4B_pln.
DR PANTHER; PTHR32091; PTHR32091; 2.
DR Pfam; PF06273; eIF-4B; 2.
PE 1: Evidence at protein level;
KW Initiation factor; Nucleus; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..527
FT /note="Eukaryotic translation initiation factor 4B1"
FT /id="PRO_0000434273"
FT REGION 1..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 196..203
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 13..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 424
FT /note="E -> D (in Ref. 1; AAF27286)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="S -> A (in Ref. 1; AAF27286)"
FT /evidence="ECO:0000305"
FT CONFLICT 454..458
FT /note="GQRPS -> AQRPI (in Ref. 1; AAF27286)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 527 AA; 56828 MW; 2D9FAE7D4A78E2A8 CRC64;
MAKPWGGVGA WALDAEREDE EREHAAAFPA PDPPAAAGGA ASFPSLKEAV VAGGGKQKKK
KGTTLSLSEF TTYGAAGAPR RVAPAEPKGL TPQEMMMLPT GPRERSEDEL DRSRGFRSYG
GDREPRGGGF DDDRRSSRDS DLDMPSRADE SDNWGKNKSF SPAPTDSGRR DRLSGPSPLG
RSDDIDNWSR DKKPLPSRYP SLGTGGGFRE SSGGGFRESS GGGFRESSGG GFRDSPGPSD
SDRWVRGAVP APMTNNGDRP RLNLNPPKRD PSATPVPAAE VARSRPSPFG AAKPREEVLA
EKGLDWRKME GEIEKKTSRP TSSHSSRPNS AHSSRPGSPG SQVSAVGSEG APRARPKVNP
FGDAKPREVV LQEKGKDWRK IDLELEHRAV NRPESEEEKN LKEEINLLKV DLKEIEAIAG
DGSEQAKEVS EKISQMEKQL DLLTVELDDK IRFGQRPSSG AGRAAAFPPA SEEPHVAVAH
MDRPRSRGGV ETYPKPVEER WGFHGSRERG SFGGGGSSDR SSTRQGW
