EF1A4_ARATH
ID EF1A4_ARATH Reviewed; 449 AA.
AC Q8GTY0; P13905; Q0WSD5; Q39093; Q9C5L4;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Elongation factor 1-alpha 4 {ECO:0000303|PubMed:2101309};
DE Short=EF-1-alpha 4 {ECO:0000303|PubMed:2101309};
DE AltName: Full=eEF-1A4 {ECO:0000303|PubMed:2101309};
GN Name=A4 {ECO:0000303|PubMed:2101309};
GN Synonyms=EF1A {ECO:0000303|PubMed:21245040};
GN OrderedLocusNames=At5g60390 {ECO:0000312|Araport:AT5G60390};
GN ORFNames=MUF9.4 {ECO:0000312|EMBL:BAB08224.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [8]
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).
RN [9]
RP INTERACTION WITH ATX1, SUBCELLULAR LOCATION, AND METHYLATION AT LYS-55;
RP LYS-79; LYS-187; LYS-261; LYS-306 AND LYS-396.
RC STRAIN=cv. Wassilewskija-2;
RX PubMed=21245040; DOI=10.1093/nar/gkq1300;
RA Ndamukong I., Lapko H., Cerny R.L., Avramova Z.;
RT "A cytoplasm-specific activity encoded by the Trithorax-like ATX1 gene.";
RL Nucleic Acids Res. 39:4709-4718(2011).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC -!- SUBUNIT: Interacts with ATX1 isoform 3 in the cytoplasm on the nuclear
CC periphery. {ECO:0000269|PubMed:21245040}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21245040}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:21245040}.
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=Q8GTY0-1; Sequence=Displayed;
CC -!- PTM: Trimethylated on Lys-396 by ATX1 isoform 3.
CC {ECO:0000269|PubMed:21245040}.
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}.
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DR EMBL; X16432; CAA34456.1; -; Genomic_DNA.
DR EMBL; AB011483; BAB08224.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97318.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97319.2; -; Genomic_DNA.
DR EMBL; CP002688; AED97320.1; -; Genomic_DNA.
DR EMBL; AF360167; AAK25877.1; -; mRNA.
DR EMBL; AF419586; AAL31918.1; -; mRNA.
DR EMBL; AY059904; AAL24386.1; -; mRNA.
DR EMBL; AY060564; AAL31193.1; -; mRNA.
DR EMBL; AY128802; AAM91202.1; -; mRNA.
DR EMBL; AY133532; AAM91362.1; -; mRNA.
DR EMBL; AY140095; AAM98236.1; -; mRNA.
DR EMBL; AY140099; AAM98240.1; -; mRNA.
DR EMBL; BT000688; AAN31833.1; -; mRNA.
DR EMBL; BT002510; AAO00870.1; -; mRNA.
DR EMBL; BT006369; AAP21177.1; -; mRNA.
DR EMBL; AK226349; BAE98497.1; -; mRNA.
DR EMBL; AK226639; BAE98750.1; -; mRNA.
DR PIR; S08534; S08534.
DR RefSeq; NP_001030993.1; NM_001035916.3. [Q8GTY0-1]
DR RefSeq; NP_001119464.1; NM_001125992.1. [Q8GTY0-1]
DR RefSeq; NP_001318848.1; NM_001345413.1. [Q8GTY0-1]
DR RefSeq; NP_001320767.1; NM_001331743.1. [Q8GTY0-1]
DR RefSeq; NP_001320768.1; NM_001331742.1. [Q8GTY0-1]
DR RefSeq; NP_200847.1; NM_125432.4. [Q8GTY0-1]
DR RefSeq; NP_563799.1; NM_100666.4. [Q8GTY0-1]
DR RefSeq; NP_563800.1; NM_100667.4. [Q8GTY0-1]
DR RefSeq; NP_563801.1; NM_100668.3. [Q8GTY0-1]
DR AlphaFoldDB; Q8GTY0; -.
DR SMR; Q8GTY0; -.
DR BioGRID; 21405; 3.
DR BioGRID; 22548; 10.
DR BioGRID; 22549; 3.
DR BioGRID; 22550; 2.
DR IntAct; Q8GTY0; 1.
DR MINT; Q8GTY0; -.
DR iPTMnet; Q8GTY0; -.
DR EnsemblPlants; AT1G07920.1; AT1G07920.1; AT1G07920.
DR EnsemblPlants; AT1G07930.1; AT1G07930.1; AT1G07930.
DR EnsemblPlants; AT1G07940.1; AT1G07940.1; AT1G07940.
DR EnsemblPlants; AT1G07940.2; AT1G07940.2; AT1G07940.
DR EnsemblPlants; AT1G07940.3; AT1G07940.3; AT1G07940.
DR EnsemblPlants; AT1G07940.4; AT1G07940.4; AT1G07940.
DR EnsemblPlants; AT5G60390.1; AT5G60390.1; AT5G60390.
DR EnsemblPlants; AT5G60390.2; AT5G60390.2; AT5G60390.
DR EnsemblPlants; AT5G60390.3; AT5G60390.3; AT5G60390.
DR GeneID; 836161; -.
DR GeneID; 837307; -.
DR GeneID; 837308; -.
DR GeneID; 837309; -.
DR Gramene; AT1G07920.1; AT1G07920.1; AT1G07920.
DR Gramene; AT1G07930.1; AT1G07930.1; AT1G07930.
DR Gramene; AT1G07940.1; AT1G07940.1; AT1G07940.
DR Gramene; AT1G07940.2; AT1G07940.2; AT1G07940.
DR Gramene; AT1G07940.3; AT1G07940.3; AT1G07940.
DR Gramene; AT1G07940.4; AT1G07940.4; AT1G07940.
DR Gramene; AT5G60390.1; AT5G60390.1; AT5G60390.
DR Gramene; AT5G60390.2; AT5G60390.2; AT5G60390.
DR Gramene; AT5G60390.3; AT5G60390.3; AT5G60390.
DR KEGG; ath:AT1G07920; -.
DR KEGG; ath:AT1G07930; -.
DR KEGG; ath:AT1G07940; -.
DR KEGG; ath:AT5G60390; -.
DR Araport; AT5G60390; -.
DR TAIR; locus:2175118; AT5G60390.
DR HOGENOM; CLU_007265_3_5_1; -.
DR InParanoid; Q8GTY0; -.
DR OMA; DIMVRKL; -.
DR PhylomeDB; Q8GTY0; -.
DR BRENDA; 3.6.5.3; 399.
DR PRO; PR:Q8GTY0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8GTY0; baseline and differential.
DR Genevisible; Q8GTY0; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; 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 4"
FT /id="PRO_0000415911"
FT DOMAIN 5..230
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 14..21
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 70..74
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 91..94
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 153..156
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 194..196
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q5SHN6"
FT BINDING 91..95
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q5SHN6"
FT BINDING 153..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q5SHN6"
FT MOD_RES 55
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000269|PubMed:21245040"
FT MOD_RES 79
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:21245040"
FT MOD_RES 187
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:21245040"
FT MOD_RES 261
FT /note="N6-methyllysine"
FT /evidence="ECO:0000269|PubMed:21245040"
FT MOD_RES 306
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:21245040"
FT MOD_RES 396
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:21245040"
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 68
FT /note="E -> D (in Ref. 1; CAA34456)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="L -> F (in Ref. 4; AAK25877)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="V -> F (in Ref. 4; AAN31833)"
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
