EF1A2_ARATH
ID EF1A2_ARATH Reviewed; 449 AA.
AC Q8W4H7; B9DGN1; P13905; Q8VZE8; Q94AD0; Q9ASU9; Q9LN13;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Elongation factor 1-alpha 2;
DE Short=EF-1-alpha 2;
DE AltName: Full=eEF-1A2;
GN Name=A2; OrderedLocusNames=At1g07930; ORFNames=T6D22.31;
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=2101309; DOI=10.1007/bf00015660;
RA Liboz T., Bardet C., le van Thai A., Axelos M., Lescure B.;
RT "The four members of the gene family encoding the Arabidopsis thaliana
RT translation elongation factor EF-1 alpha are actively transcribed.";
RL Plant Mol. Biol. 14:107-110(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Tremousaygue D., Bardet C., Dabos P., Regad F., Pelese F., Lescure B.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [9]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-438 AND LYS-441, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19292762; DOI=10.1111/j.1365-313x.2009.03862.x;
RA Saracco S.A., Hansson M., Scalf M., Walker J.M., Smith L.M., Vierstra R.D.;
RT "Tandem affinity purification and mass spectrometric analysis of
RT ubiquitylated proteins in Arabidopsis.";
RL Plant J. 59:344-358(2009).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8W4H7-1; Sequence=Displayed;
CC -!- MISCELLANEOUS: There are four genes for EF-1-alpha in Arabidopsis
CC thaliana. The sequence of genes 1, 2, and 3 are identical.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79822.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X16431; CAA34454.1; -; Genomic_DNA.
DR EMBL; U63815; AAB07883.1; -; Genomic_DNA.
DR EMBL; AC026875; AAF79822.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28213.1; -; Genomic_DNA.
DR EMBL; AF361822; AAK32834.1; -; mRNA.
DR EMBL; AY048275; AAK82537.1; -; mRNA.
DR EMBL; AY059160; AAL15385.1; -; mRNA.
DR EMBL; AY062553; AAL32631.1; -; mRNA.
DR EMBL; AY065008; AAL57653.1; -; mRNA.
DR EMBL; AY080660; AAL86336.1; -; mRNA.
DR EMBL; AY114651; AAM47970.1; -; mRNA.
DR EMBL; AY123029; AAM67562.1; -; mRNA.
DR EMBL; BT003325; AAO29944.1; -; mRNA.
DR EMBL; AK317216; BAH19898.1; -; mRNA.
DR PIR; F86214; F86214.
DR PIR; S06724; S06724.
DR RefSeq; NP_001030993.1; NM_001035916.3. [Q8W4H7-1]
DR RefSeq; NP_001119464.1; NM_001125992.1. [Q8W4H7-1]
DR RefSeq; NP_001318848.1; NM_001345413.1. [Q8W4H7-1]
DR RefSeq; NP_001320767.1; NM_001331743.1. [Q8W4H7-1]
DR RefSeq; NP_001320768.1; NM_001331742.1. [Q8W4H7-1]
DR RefSeq; NP_200847.1; NM_125432.4. [Q8W4H7-1]
DR RefSeq; NP_563799.1; NM_100666.4. [Q8W4H7-1]
DR RefSeq; NP_563800.1; NM_100667.4. [Q8W4H7-1]
DR RefSeq; NP_563801.1; NM_100668.3. [Q8W4H7-1]
DR AlphaFoldDB; Q8W4H7; -.
DR SMR; Q8W4H7; -.
DR BioGRID; 21405; 3.
DR BioGRID; 22548; 10.
DR BioGRID; 22549; 3.
DR BioGRID; 22550; 2.
DR IntAct; Q8W4H7; 2.
DR iPTMnet; Q8W4H7; -.
DR ProMEX; Q8W4H7; -.
DR EnsemblPlants; AT1G07920.1; AT1G07920.1; AT1G07920. [Q8W4H7-1]
DR EnsemblPlants; AT1G07930.1; AT1G07930.1; AT1G07930. [Q8W4H7-1]
DR EnsemblPlants; AT1G07940.1; AT1G07940.1; AT1G07940. [Q8W4H7-1]
DR EnsemblPlants; AT1G07940.2; AT1G07940.2; AT1G07940. [Q8W4H7-1]
DR EnsemblPlants; AT1G07940.3; AT1G07940.3; AT1G07940. [Q8W4H7-1]
DR EnsemblPlants; AT1G07940.4; AT1G07940.4; AT1G07940. [Q8W4H7-1]
DR EnsemblPlants; AT5G60390.1; AT5G60390.1; AT5G60390. [Q8W4H7-1]
DR EnsemblPlants; AT5G60390.2; AT5G60390.2; AT5G60390. [Q8W4H7-1]
DR EnsemblPlants; AT5G60390.3; AT5G60390.3; AT5G60390. [Q8W4H7-1]
DR GeneID; 836161; -.
DR GeneID; 837307; -.
DR GeneID; 837308; -.
DR GeneID; 837309; -.
DR Gramene; AT1G07920.1; AT1G07920.1; AT1G07920. [Q8W4H7-1]
DR Gramene; AT1G07930.1; AT1G07930.1; AT1G07930. [Q8W4H7-1]
DR Gramene; AT1G07940.1; AT1G07940.1; AT1G07940. [Q8W4H7-1]
DR Gramene; AT1G07940.2; AT1G07940.2; AT1G07940. [Q8W4H7-1]
DR Gramene; AT1G07940.3; AT1G07940.3; AT1G07940. [Q8W4H7-1]
DR Gramene; AT1G07940.4; AT1G07940.4; AT1G07940. [Q8W4H7-1]
DR Gramene; AT5G60390.1; AT5G60390.1; AT5G60390. [Q8W4H7-1]
DR Gramene; AT5G60390.2; AT5G60390.2; AT5G60390. [Q8W4H7-1]
DR Gramene; AT5G60390.3; AT5G60390.3; AT5G60390. [Q8W4H7-1]
DR KEGG; ath:AT1G07920; -.
DR KEGG; ath:AT1G07930; -.
DR KEGG; ath:AT1G07940; -.
DR KEGG; ath:AT5G60390; -.
DR Araport; AT1G07930; -.
DR TAIR; locus:2205105; AT1G07930.
DR HOGENOM; CLU_007265_3_5_1; -.
DR InParanoid; Q8W4H7; -.
DR OMA; DIMVRKL; -.
DR PhylomeDB; Q8W4H7; -.
DR BRENDA; 3.6.5.3; 399.
DR PRO; PR:Q8W4H7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8W4H7; baseline and differential.
DR Genevisible; Q8W4H7; AT.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00118_A; EF_Tu_A; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00483; EF-1_alpha; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Elongation factor; GTP-binding;
KW Isopeptide bond; Methylation; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..449
FT /note="Elongation factor 1-alpha 2"
FT /id="PRO_0000415909"
FT DOMAIN 5..230
FT /note="tr-type G"
FT REGION 14..21
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 70..74
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 91..94
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 153..156
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 194..196
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 91..95
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 153..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 55
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8GTY0"
FT MOD_RES 79
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8GTY0"
FT MOD_RES 187
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8GTY0"
FT MOD_RES 261
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8GTY0"
FT MOD_RES 306
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8GTY0"
FT MOD_RES 396
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8GTY0"
FT CROSSLNK 438
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:19292762"
FT CROSSLNK 441
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:19292762"
FT CONFLICT 38
FT /note="V -> L (in Ref. 5; AAL15385/AAK32834)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="E -> Q (in Ref. 5; AAK82537)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="F -> I (in Ref. 5; AAK82537)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="V -> G (in Ref. 5; AAK82537)"
FT /evidence="ECO:0000305"
FT CONFLICT 154..155
FT /note="KM -> NI (in Ref. 5; AAL57653)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="S -> L (in Ref. 5; AAK82537)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="K -> M (in Ref. 6; BAH19898)"
FT /evidence="ECO:0000305"
FT CONFLICT 422..424
FT /note="AVG -> TVS (in Ref. 5; AAM47970/AAL32631)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 449 AA; 49502 MW; 12FFA6C537DFCEE9 CRC64;
MGKEKFHINI VVIGHVDSGK STTTGHLIYK LGGIDKRVIE RFEKEAAEMN KRSFKYAWVL
DKLKAERERG ITIDIALWKF ETTKYYCTVI DAPGHRDFIK NMITGTSQAD CAVLIIDSTT
GGFEAGISKD GQTREHALLA FTLGVKQMIC CCNKMDATTP KYSKARYDEI IKEVSSYLKK
VGYNPDKIPF VPISGFEGDN MIERSTNLDW YKGPTLLEAL DQINEPKRPS DKPLRLPLQD
VYKIGGIGTV PVGRVETGMI KPGMVVTFAP TGLTTEVKSV EMHHESLLEA LPGDNVGFNV
KNVAVKDLKR GYVASNSKDD PAKGAANFTS QVIIMNHPGQ IGNGYAPVLD CHTSHIAVKF
SEILTKIDRR SGKEIEKEPK FLKNGDAGMV KMTPTKPMVV ETFSEYPPLG RFAVRDMRQT
VAVGVIKSVD KKDPTGAKVT KAAVKKGAK
