IF4B1_ARATH
ID IF4B1_ARATH Reviewed; 532 AA.
AC Q9LIN5; Q8L6Y0; Q9LD19; Q9M7F0; Q9SQK7;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Eukaryotic translation initiation factor 4B1 {ECO:0000303|PubMed:10600500};
DE Short=AtTif4B1 {ECO:0000303|PubMed:10600500};
DE Short=eIF4B1 {ECO:0000305};
GN Name=EIF4B1 {ECO:0000303|PubMed:10600500};
GN OrderedLocusNames=At3g26400 {ECO:0000312|EMBL:AEE77153.1};
GN ORFNames=F20C19.13 {ECO:0000312|EMBL:BAB02201.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 216-532.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, PROTEIN SEQUENCE OF 293-307, 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).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(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:19493973}.
CC -!- SUBUNIT: Homodimer (By similarity). Nonspherical monomer. mRNA-
CC discriminating component of initiation complexes (PubMed:19493973).
CC {ECO:0000250|UniProtKB:Q9AUJ7, ECO:0000269|PubMed:19493973}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q9AUJ7}.
CC -!- SIMILARITY: Belongs to the eIF-4 subunit B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM98238.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF021805; AAF05869.1; -; Genomic_DNA.
DR EMBL; AF136005; AAF27285.1; -; mRNA.
DR EMBL; AF145232; AAF27294.1; -; mRNA.
DR EMBL; AP001298; BAB02201.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77153.1; -; Genomic_DNA.
DR EMBL; AY140097; AAM98238.1; ALT_INIT; mRNA.
DR EMBL; BT006541; AAP21349.1; -; mRNA.
DR RefSeq; NP_189271.1; NM_113547.2.
DR AlphaFoldDB; Q9LIN5; -.
DR SMR; Q9LIN5; -.
DR STRING; 3702.AT3G26400.1; -.
DR iPTMnet; Q9LIN5; -.
DR PaxDb; Q9LIN5; -.
DR PRIDE; Q9LIN5; -.
DR ProteomicsDB; 228874; -.
DR EnsemblPlants; AT3G26400.1; AT3G26400.1; AT3G26400.
DR GeneID; 822244; -.
DR Gramene; AT3G26400.1; AT3G26400.1; AT3G26400.
DR KEGG; ath:AT3G26400; -.
DR Araport; AT3G26400; -.
DR TAIR; locus:2079246; AT3G26400.
DR eggNOG; ENOG502QVPR; Eukaryota.
DR HOGENOM; CLU_028368_1_0_1; -.
DR InParanoid; Q9LIN5; -.
DR OMA; TPEEMMM; -.
DR OrthoDB; 1227687at2759; -.
DR PhylomeDB; Q9LIN5; -.
DR PRO; PR:Q9LIN5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LIN5; baseline and differential.
DR Genevisible; Q9LIN5; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:TAIR.
DR InterPro; IPR010433; EIF-4B_pln.
DR PANTHER; PTHR32091; PTHR32091; 1.
DR Pfam; PF06273; eIF-4B; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Initiation factor; Nucleus; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..532
FT /note="Eukaryotic translation initiation factor 4B1"
FT /id="PRO_0000434274"
FT REGION 16..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 177..184
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 237..244
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 29..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 37
FT /note="S -> R (in Ref. 1; AAF05869)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="F -> L (in Ref. 1; AAF05869)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="D -> G (in Ref. 1; AAF05869)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="Missing (in Ref. 1; AAF05869)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="E -> D (in Ref. 1; AAF05869)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="V -> I (in Ref. 1; AAF05869)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="L -> V (in Ref. 1; AAF05869)"
FT /evidence="ECO:0000305"
FT CONFLICT 507
FT /note="N -> D (in Ref. 1; AAF05869)"
FT /evidence="ECO:0000305"
FT CONFLICT 516
FT /note="T -> S (in Ref. 1; AAF05869)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 532 AA; 57720 MW; E3EDE5C04DFC7D50 CRC64;
MSKAWGGIGI GAWADEAERA DEEQAAEATA ATADTQSFPS LREAAAATAT SGKSRKMKKM
SLSEFTTGAY TAPGGRNSVG LTQQEILQLP TGPRQRSEEE MQPGRLGGGF SSYGGRSGGR
IGRDRDDSDG SWSGGGGGGG RRPYGGGFDD DRRGNQSRVS DFPQPSRADE VDDWGKEKKP
LPSFDQGRQG RYSGDGGGFG GGGSGFGGGG GGGGGGLSRA DDVDNWGAGK RQAPVRSSTF
GSSFGDSGQE ERRRLVLEPR KVESGGSETP PVVEKTSKPN PFGAARPRED VLAEKGLDWK
KIDSEIEAKK GSSQTSRPTS AHSSRPSSAQ SNRSESSGLN NVVKPRPKVN PFGDAKPREV
LLEEQGKDWR KMDLELEHRR VDRPETEEEK MLKEEIEELR KKLEKESVAP EIKESDQEPG
SNNNHNDLPE IIRGKEKDLE ILTRELDDKV RFRQKPVERP GSGAGRTGTY SERTHSRAGS
IDETRSFEST ERPRSRGAVD AWVRPANEQR RNFQGTKERG FFSNRSSSRE GW
