IF2B_ARATH
ID IF2B_ARATH Reviewed; 268 AA.
AC Q41969; F4K6W6; Q8L7Q3; Q9C5N7;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 3.
DT 25-MAY-2022, entry version 164.
DE RecName: Full=Eukaryotic translation initiation factor 2 subunit beta {ECO:0000305};
DE Short=eIF2-beta {ECO:0000305};
DE AltName: Full=Protein EMBRYO DEFECTIVE 1401 {ECO:0000305};
GN Name=EIF2B {ECO:0000305}; Synonyms=EMB1401 {ECO:0000305};
GN OrderedLocusNames=At5g20920; ORFNames=F22D1.90;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Browning K.S., Chen R.;
RT "Arabidopsis thaliana protein synthesis initiation factor eIF2 beta mRNA.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-252.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=8281187; DOI=10.1046/j.1365-313x.1993.04061051.x;
RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D.,
RA Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M.,
RA Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C.,
RA Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.;
RT "An inventory of 1152 expressed sequence tags obtained by partial
RT sequencing of cDNAs from Arabidopsis thaliana.";
RL Plant J. 4:1051-1061(1993).
RN [8]
RP PHOSPHORYLATION AT SER-42; SER-80 AND SER-112.
RX PubMed=19509420; DOI=10.1074/jbc.m109.007658;
RA Dennis M.D., Person M.D., Browning K.S.;
RT "Phosphorylation of plant translation initiation factors by CK2 enhances
RT the in vitro interaction of multifactor complex components.";
RL J. Biol. Chem. 284:20615-20628(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: eIF-2 functions in the early steps of protein synthesis by
CC forming a ternary complex with GTP and initiator tRNA. This complex
CC binds to a 40S ribosomal subunit, followed by mRNA binding to form a
CC 43S pre-initiation complex. Junction of the 60S ribosomal subunit to
CC form the 80S initiation complex is preceded by hydrolysis of the GTP
CC bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for
CC eIF-2 to recycle and catalyze another round of initiation, the GDP
CC bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by
CC eIF-2B (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma chain.
CC -!- INTERACTION:
CC Q41969; O23160: MYB73; NbExp=3; IntAct=EBI-2130789, EBI-25506855;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q41969-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q41969-2; Sequence=VSP_058490;
CC -!- PTM: Phosphorylated at Ser-42, Ser-80 and Ser-112 by CK2.
CC {ECO:0000269|PubMed:19509420}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family. {ECO:0000305}.
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DR EMBL; AF353095; AAK29672.1; -; mRNA.
DR EMBL; AF296834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92904.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92905.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92906.1; -; Genomic_DNA.
DR EMBL; AY128324; AAM91527.1; -; mRNA.
DR EMBL; BT000056; AAN15375.1; -; mRNA.
DR EMBL; BX829594; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY087810; AAM65346.1; -; mRNA.
DR EMBL; Z18133; CAA79110.1; -; mRNA.
DR RefSeq; NP_001078610.1; NM_001085141.1. [Q41969-1]
DR RefSeq; NP_197592.1; NM_122100.4. [Q41969-1]
DR RefSeq; NP_974817.1; NM_203088.2. [Q41969-2]
DR AlphaFoldDB; Q41969; -.
DR SMR; Q41969; -.
DR BioGRID; 17491; 41.
DR IntAct; Q41969; 33.
DR STRING; 3702.AT5G20920.3; -.
DR iPTMnet; Q41969; -.
DR MetOSite; Q41969; -.
DR PaxDb; Q41969; -.
DR PRIDE; Q41969; -.
DR ProteomicsDB; 228815; -. [Q41969-1]
DR EnsemblPlants; AT5G20920.1; AT5G20920.1; AT5G20920. [Q41969-1]
DR EnsemblPlants; AT5G20920.2; AT5G20920.2; AT5G20920. [Q41969-2]
DR EnsemblPlants; AT5G20920.3; AT5G20920.3; AT5G20920. [Q41969-1]
DR GeneID; 832216; -.
DR Gramene; AT5G20920.1; AT5G20920.1; AT5G20920. [Q41969-1]
DR Gramene; AT5G20920.2; AT5G20920.2; AT5G20920. [Q41969-2]
DR Gramene; AT5G20920.3; AT5G20920.3; AT5G20920. [Q41969-1]
DR KEGG; ath:AT5G20920; -.
DR Araport; AT5G20920; -.
DR TAIR; locus:2147162; AT5G20920.
DR eggNOG; KOG2768; Eukaryota.
DR InParanoid; Q41969; -.
DR OMA; PKHILAF; -.
DR OrthoDB; 1178655at2759; -.
DR PhylomeDB; Q41969; -.
DR PRO; PR:Q41969; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q41969; baseline and differential.
DR Genevisible; Q41969; AT.
DR GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0031369; F:translation initiation factor binding; IBA:GO_Central.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IBA:GO_Central.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
DR InterPro; IPR045196; IF2/IF5.
DR InterPro; IPR002735; Transl_init_fac_IF2/IF5_dom.
DR InterPro; IPR016189; Transl_init_fac_IF2/IF5_N.
DR InterPro; IPR016190; Transl_init_fac_IF2/IF5_Zn-bd.
DR PANTHER; PTHR23001; PTHR23001; 1.
DR Pfam; PF01873; eIF-5_eIF-2B; 1.
DR SMART; SM00653; eIF2B_5; 1.
DR SUPFAM; SSF100966; SSF100966; 1.
DR SUPFAM; SSF75689; SSF75689; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Initiation factor; Metal-binding;
KW Phosphoprotein; Protein biosynthesis; Reference proteome; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..268
FT /note="Eukaryotic translation initiation factor 2 subunit
FT beta"
FT /id="PRO_0000137411"
FT ZN_FING 222..246
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 42
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:19509420"
FT MOD_RES 80
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:19509420"
FT MOD_RES 112
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:19509420"
FT VAR_SEQ 14
FT /note="Missing (in isoform 2)"
FT /id="VSP_058490"
FT CONFLICT 71
FT /note="T -> A (in Ref. 1; AAK29672 and 6; AAM65346)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 268 AA; 30663 MW; E1C17373472F4DEB CRC64;
MADEINEIRE EQEQLAPFDP SKKKKKKKVV IQEPVEDLAE SSQTEKSDSL PVNDGLESSF
TGMKKKKKKP TESSLLNNES VDAGEDLDEI ANDEQEGEEG IVLQQRYPWE GSERDYIYDE
LLGRVFNILR ENNPELAGDR RRTVMRPPQV LREGTKKTVF VNFMDLCKTM HRQPDHVMQY
LLAELGTSGS LDGQQRLVVK GRFAPKNFEG ILRRYITDYV ICLGCKSPDT ILSKENRLFF
LRCEKCGSQR SVAPIKTGFV ARVSRRKT
