IF4B2_ARATH
ID IF4B2_ARATH Reviewed; 549 AA.
AC Q9SAD7; Q0WMZ1; Q9LD20; Q9M7E8;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Eukaryotic translation initiation factor 4B2 {ECO:0000303|PubMed:10600500};
DE Short=AtTif4B2 {ECO:0000303|PubMed:10600500};
DE Short=eIF4B2 {ECO:0000305};
DE AltName: Full=Protein SPONTANEOUS NECROTIC SPOTS {ECO:0000303|PubMed:22639576};
GN Name=EIF4B2 {ECO:0000303|PubMed:10600500};
GN Synonyms=SNS {ECO:0000303|PubMed:22639576};
GN OrderedLocusNames=At1g13020 {ECO:0000312|EMBL:AEE28960.1};
GN ORFNames=F3F19.4 {ECO:0000312|EMBL:AAD31055.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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).
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).
RN [7]
RP MISCELLANEOUS ON PCD.
RC STRAIN=cv. C24;
RX PubMed=22639576; DOI=10.3389/fpls.2011.00009;
RA Gaussand G.M.D.J.-M., Jia Q., van der Graaff E., Lamers G.E.M.,
RA Fransz P.F., Hooykaas P.J.J., de Pater S.;
RT "Programmed cell death in the leaves of the Arabidopsis spontaneous
RT necrotic spots (sns-D) mutant correlates with increased expression of the
RT eukaryotic translation initiation factor eIF4B2.";
RL Front. Plant Sci. 2:9-9(2011).
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 -!- MISCELLANEOUS: Over-expression in sns-D leads to programmed cell death
CC (PCD) in the leaves characterized by spontaneous necrotic spots on the
CC rosette leaves under aseptic conditions. Embryo lethal when homozygote.
CC {ECO:0000269|PubMed:22639576}.
CC -!- SIMILARITY: Belongs to the eIF-4 subunit B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF27293.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF136007; AAF27287.1; -; Genomic_DNA.
DR EMBL; AF145231; AAF27293.1; ALT_FRAME; mRNA.
DR EMBL; AC007357; AAD31055.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28960.1; -; Genomic_DNA.
DR EMBL; AK229665; BAF01509.1; -; mRNA.
DR PIR; B86264; B86264.
DR RefSeq; NP_172761.1; NM_101172.3.
DR AlphaFoldDB; Q9SAD7; -.
DR SMR; Q9SAD7; -.
DR STRING; 3702.AT1G13020.1; -.
DR iPTMnet; Q9SAD7; -.
DR MetOSite; Q9SAD7; -.
DR PaxDb; Q9SAD7; -.
DR PRIDE; Q9SAD7; -.
DR ProteomicsDB; 250677; -.
DR EnsemblPlants; AT1G13020.1; AT1G13020.1; AT1G13020.
DR GeneID; 837859; -.
DR Gramene; AT1G13020.1; AT1G13020.1; AT1G13020.
DR KEGG; ath:AT1G13020; -.
DR Araport; AT1G13020; -.
DR TAIR; locus:2031795; AT1G13020.
DR eggNOG; ENOG502QVPR; Eukaryota.
DR HOGENOM; CLU_028368_1_0_1; -.
DR InParanoid; Q9SAD7; -.
DR OMA; MPMPSRY; -.
DR OrthoDB; 1227687at2759; -.
DR PhylomeDB; Q9SAD7; -.
DR PRO; PR:Q9SAD7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SAD7; baseline and differential.
DR Genevisible; Q9SAD7; AT.
DR GO; GO:0005576; C:extracellular region; 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 Initiation factor; Nucleus; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..549
FT /note="Eukaryotic translation initiation factor 4B2"
FT /id="PRO_0000434275"
FT REGION 1..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 169..176
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 234..241
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 27..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 68
FT /note="S -> G (in Ref. 1; AAF27287)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="D -> G (in Ref. 4; BAF01509)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 549 AA; 59324 MW; E2E6E8B844218D7A CRC64;
MSKPWGGIGA WADEAERADE EQAAEATATA ADSQSFPSLK EAATAKSSKK KKKMTLSEFT
KGAYTAPSSA GLTREQMLQL PTGPRQRSED EMQPGRLGGG FSSYGGGRSS GPPGRMSRDR
EDSDGSWGGG GGGRRSYGGF DDDQRGSNSR VSDFPQVSRA DEDDDWGKGK KSLPSFDQGR
QGSRYGGGGG SFGGGGGGGA GSYGGGGAGA GSGGGGGFSK ADEVDNWAAG KAKSSTFGSG
FRESGPEPDR WARGVLPSGG GVQEERRRLV FEPRKADTEV SETPTAVKTS KPSPFGAARP
REQVLAEKGL DWKKLDSDIE AKKGQTSRPS SAQSSRPSSA QSNRSESSAL NNVENVVKPR
PKVNPFGDAK PREVLLEEQG KDWRKIDSEL EHRRVDRPET EGERMLKEEI EELRKKLEKE
AAIAPESKES QQESDSNHQN LPDLIREKEK NLDLLIRELD DKVRFRPRAV ERPGSSASRG
GSYSERPHSR AGSIDESRSV ESMERPRSHG TGDNWPRPVD DRRNFQGSKE RGFFNNRNFD
RSSSAREGW
