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 27-MAR-2024, entry version 171. 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: Component of the eIF2 complex that functions in the early CC steps of protein synthesis by forming a ternary complex with GTP and CC initiator tRNA. This complex binds to a 40S ribosomal subunit, followed CC by mRNA binding to form a 43S pre-initiation complex (43S PIC). CC Junction of the 60S ribosomal subunit to form the 80S initiation CC complex is preceded by hydrolysis of the GTP bound to eIF2 and release CC of an eIF2-GDP binary complex. In order for eIF2 to recycle and CC catalyze another round of initiation, the GDP bound to eIF2 must CC exchange with GTP by way of a reaction catalyzed by eIF2B (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: Eukaryotic translation initiation factor 2 eIF2 is a CC heterotrimeric complex composed of an alpha, a beta and a gamma CC subunit. {ECO:0000250|UniProtKB:P09064}. CC -!- INTERACTION: CC Q41969; O23160: MYB73; NbExp=3; IntAct=EBI-2130789, EBI-25506855; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:P56329}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.Q41969; -. DR iPTMnet; Q41969; -. DR MetOSite; Q41969; -. DR PaxDb; 3702-AT5G20920-3; -. 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; AT5G20920; EIF2 BETA. DR eggNOG; KOG2768; Eukaryota. DR InParanoid; Q41969; -. DR OMA; VINEMQQ; -. DR OrthoDB; 5480877at2759; -. DR PhylomeDB; Q41969; -. DR PRO; PR:Q41969; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; Q41969; baseline and differential. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; ISS:UniProtKB. DR GO; GO:0009536; C:plastid; HDA:TAIR. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW. DR GO; GO:0002183; P:cytoplasmic translational initiation; ISS:UniProtKB. DR Gene3D; 3.30.30.170; -; 1. 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; EUKARYOTIC TRANSLATION INITIATION FACTOR; 1. DR PANTHER; PTHR23001:SF3; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 2; 1. DR Pfam; PF01873; eIF-5_eIF-2B; 1. DR SMART; SM00653; eIF2B_5; 1. DR SUPFAM; SSF100966; Translation initiation factor 2 beta, aIF2beta, N-terminal domain; 1. DR SUPFAM; SSF75689; Zinc-binding domain of translation initiation factor 2 beta; 1. DR Genevisible; Q41969; AT. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Cytoplasm; Initiation factor; KW Metal-binding; Phosphoprotein; Protein biosynthesis; Reference proteome; KW Zinc; 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 //