EF1B2_ARATH
ID EF1B2_ARATH Reviewed; 224 AA.
AC Q9SCX3;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 144.
DE RecName: Full=Elongation factor 1-beta 2;
DE Short=EF-1-beta 2;
DE AltName: Full=Elongation factor 1-beta' 2;
DE Short=EF-1-beta' 2;
DE AltName: Full=Elongation factor 1B-alpha 2;
DE AltName: Full=eEF-1B alpha 2;
GN OrderedLocusNames=At5g19510; ORFNames=T20D1.30;
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], AND FUNCTION.
RX PubMed=10618495; DOI=10.1016/s0014-5793(99)01694-4;
RA Hericourt F., Jupin I.;
RT "Molecular cloning and characterization of the Arabidopsis thaliana alpha-
RT subunit of elongation factor 1B.";
RL FEBS Lett. 464:148-152(1999).
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].
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
RN [6]
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: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound
CC to EF-1-alpha to GTP. {ECO:0000269|PubMed:10618495}.
CC -!- SUBUNIT: EF-1 is composed of 4 subunits: alpha, beta (1B-alpha=beta'),
CC delta (1B-beta), and gamma (1B-gamma). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family. {ECO:0000305}.
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DR EMBL; AJ249597; CAB64730.1; -; mRNA.
DR EMBL; AF296830; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92719.1; -; Genomic_DNA.
DR EMBL; AF360304; AAK26014.1; -; mRNA.
DR EMBL; AY056354; AAL07240.1; -; mRNA.
DR PIR; PA0110; PA0110.
DR PIR; T52558; T52558.
DR RefSeq; NP_568375.2; NM_121956.3.
DR AlphaFoldDB; Q9SCX3; -.
DR SMR; Q9SCX3; -.
DR BioGRID; 17347; 5.
DR STRING; 3702.AT5G19510.1; -.
DR iPTMnet; Q9SCX3; -.
DR MetOSite; Q9SCX3; -.
DR PaxDb; Q9SCX3; -.
DR PRIDE; Q9SCX3; -.
DR ProteomicsDB; 221915; -.
DR EnsemblPlants; AT5G19510.1; AT5G19510.1; AT5G19510.
DR GeneID; 832071; -.
DR Gramene; AT5G19510.1; AT5G19510.1; AT5G19510.
DR KEGG; ath:AT5G19510; -.
DR Araport; AT5G19510; -.
DR TAIR; locus:2180806; AT5G19510.
DR eggNOG; KOG1668; Eukaryota.
DR HOGENOM; CLU_050172_3_0_1; -.
DR InParanoid; Q9SCX3; -.
DR OMA; FEVKPWD; -.
DR OrthoDB; 1464823at2759; -.
DR PhylomeDB; Q9SCX3; -.
DR PRO; PR:Q9SCX3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9SCX3; baseline and differential.
DR Genevisible; Q9SCX3; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:InterPro.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR CDD; cd00292; EF1B; 1.
DR Gene3D; 3.30.70.60; -; 1.
DR InterPro; IPR036219; eEF-1beta-like_sf.
DR InterPro; IPR014038; EF1B_bsu/dsu_GNE.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR014717; Transl_elong_EF1B/ribosomal_S6.
DR InterPro; IPR001326; Transl_elong_EF1B_B/D_CS.
DR Pfam; PF00736; EF1_GNE; 1.
DR SMART; SM00888; EF1_GNE; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF54984; SSF54984; 1.
DR PROSITE; PS00824; EF1BD_1; 1.
DR PROSITE; PS00825; EF1BD_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Elongation factor; Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..224
FT /note="Elongation factor 1-beta 2"
FT /id="PRO_0000155032"
FT DOMAIN 14..65
FT /note="GST C-terminal"
FT REGION 89..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..108
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..139
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"
SQ SEQUENCE 224 AA; 24201 MW; F9BF9178A60CB3B4 CRC64;
MAVTFSDLHT EEGVKSVEEH LAGKTYISGD QLSVDDVKVY AAVPVKPSDA FPNASKWYES
VASQLAKSFP GKAVGVQFGG SAAAAPAVEA EAPAAAADDD DDMDLFGDET EEEKKAAEER
EAAKKDTKKP KESGKSSVLM DVKPWDDETD MKKLEEAVRG VEMPGLFWGA SKLVPVGYGI
KKLTIMFTIV DDLVSPDNLI EDFLTSEPNN EYIQSCDIVA FNKI
