EF1B1_ARATH
ID EF1B1_ARATH Reviewed; 228 AA.
AC Q84WM9; Q9SCX2; Q9SCX4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Elongation factor 1-beta 1;
DE Short=EF-1-beta 1;
DE AltName: Full=Elongation factor 1-beta' 1;
DE Short=EF-1-beta' 1;
DE AltName: Full=Elongation factor 1B-alpha 1;
DE AltName: Full=eEF-1B alpha 1;
GN OrderedLocusNames=At5g12110; ORFNames=MXC9.7;
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=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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 19-228.
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).
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family. {ECO:0000305}.
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DR EMBL; AJ249596; CAB64729.1; -; mRNA.
DR EMBL; AJ249598; CAB64731.1; -; mRNA.
DR EMBL; AB007727; BAB10029.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91764.1; -; Genomic_DNA.
DR EMBL; BT002990; AAO22799.1; -; mRNA.
DR PIR; T52557; T52557.
DR PIR; T52559; T52559.
DR RefSeq; NP_196772.1; NM_121249.5.
DR AlphaFoldDB; Q84WM9; -.
DR SMR; Q84WM9; -.
DR BioGRID; 16362; 4.
DR STRING; 3702.AT5G12110.1; -.
DR PaxDb; Q84WM9; -.
DR PRIDE; Q84WM9; -.
DR ProteomicsDB; 221914; -.
DR EnsemblPlants; AT5G12110.1; AT5G12110.1; AT5G12110.
DR GeneID; 831084; -.
DR Gramene; AT5G12110.1; AT5G12110.1; AT5G12110.
DR KEGG; ath:AT5G12110; -.
DR Araport; AT5G12110; -.
DR TAIR; locus:2177038; AT5G12110.
DR eggNOG; KOG1668; Eukaryota.
DR HOGENOM; CLU_050172_3_0_1; -.
DR InParanoid; Q84WM9; -.
DR OMA; QMPGLTW; -.
DR OrthoDB; 1464823at2759; -.
DR PhylomeDB; Q84WM9; -.
DR PRO; PR:Q84WM9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q84WM9; baseline and differential.
DR Genevisible; Q84WM9; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; 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; PS00825; EF1BD_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell membrane; Elongation factor; Membrane;
KW Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9SCX3"
FT CHAIN 2..228
FT /note="Elongation factor 1-beta 1"
FT /id="PRO_0000155031"
FT DOMAIN 14..65
FT /note="GST C-terminal"
FT REGION 75..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..112
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..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:0000250|UniProtKB:Q9SCX3"
SQ SEQUENCE 228 AA; 24789 MW; 5F1495FF08BC31EF CRC64;
MAVTFSDLHT ERGLKTLEEH LAGKTYISGD QLSVDDVKVY AAVLENPGDG FPNASKWYDS
VASHLAKSFP GKADGVRVGG GVAPPSEAHP HTEEPAADGD GDDDDDIDLF ADETEDEKKA
AEEREAAKKD TKKTKESGKS SVLLEVKPWD DETDMKKLEE AVRSVQMPGL TWGASKLVPV
GYGIKKLTIM MTIVDDLVSV DNLIEDHLTS EPNNEYIQSV DIVAFNKI
