ID EF1A1_BOVIN Reviewed; 462 AA.
AC P68103; A5PK01; P04719; P04720; Q2KJJ3;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 24-JAN-2024, entry version 155.
DE RecName: Full=Elongation factor 1-alpha 1;
DE Short=EF-1-alpha-1;
DE EC=3.6.5.- {ECO:0000250|UniProtKB:P68104};
DE AltName: Full=Elongation factor Tu;
DE Short=EF-Tu;
DE AltName: Full=Eukaryotic elongation factor 1 A-1;
DE Short=eEF1A-1;
GN Name=EEF1A1; Synonyms=EEF1A, EF1A;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Perez D.R., Johnson C.M., Donis R.O.;
RT "BVDV NS5A interacts with eEF1a.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Japanese black; TISSUE=Endometrium;
RA Kojima T., Oshima K., Watanabe H., Komatsu M.;
RT "cDNA of bovine elongation factor 1 alpha from endometrium.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus, and Hereford; TISSUE=Ileum, and Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Translation elongation factor that catalyzes the GTP-
CC dependent binding of aminoacyl-tRNA (aa-tRNA) to the A-site of
CC ribosomes during the elongation phase of protein synthesis. Base
CC pairing between the mRNA codon and the aa-tRNA anticodon promotes GTP
CC hydrolysis, releasing the aa-tRNA from EEF1A1 and allowing its
CC accommodation into the ribosome. The growing protein chain is
CC subsequently transferred from the P-site peptidyl tRNA to the A-site
CC aa-tRNA, extending it by one amino acid through ribosome-catalyzed
CC peptide bond formation. Also plays a role in the positive regulation of
CC IFNG transcription in T-helper 1 cells as part of an IFNG promoter-
CC binding complex with TXK and PARP1. {ECO:0000250|UniProtKB:P68104}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000250|UniProtKB:P68104};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P68104};
CC -!- SUBUNIT: Found in a nuclear export complex with XPO5, EEF1A1, Ran and
CC aminoacylated tRNA. Interacts with PARP1 and TXK. Interacts with KARS1.
CC May interact with ERGIC2. Interacts with IFIT1 (via TPR repeats 4-7)
CC (By similarity). Interacts with DLC1, facilitating distribution to the
CC membrane periphery and ruffles upon growth factor stimulation.
CC Interacts with ZPR1; the interaction occurs in a epidermal growth
CC factor (EGF)-dependent manner (By similarity). Interacts with PPP1R16B
CC (By similarity). Interacts with SPHK1 and SPHK2; both interactions
CC increase SPHK1 and SPHK2 kinase activity (By similarity).
CC {ECO:0000250|UniProtKB:P68104}.
CC -!- INTERACTION:
CC P68103; PRO_0000038035 [P19711]; Xeno; NbExp=6; IntAct=EBI-352178, EBI-9350549;
CC P68103; PRO_0000038022 [Q96662]; Xeno; NbExp=2; IntAct=EBI-352178, EBI-9350684;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P68104}. Nucleus
CC {ECO:0000250|UniProtKB:P68104}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P68104}. Cell membrane
CC {ECO:0000250|UniProtKB:P68104}. Note=Colocalizes with DLC1 at actin-
CC rich regions in the cell periphery. Translocates together with ZPR1
CC from the cytoplasm to the nucleus and nucleolus after treatment with
CC mitogens. Localization at the cell membrane depends on EEF1A1
CC phosphorylation status and the presence of PPP1R16B.
CC {ECO:0000250|UniProtKB:P68104}.
CC -!- PTM: ISGylated. {ECO:0000250|UniProtKB:P68104}.
CC -!- PTM: Phosphorylated by TXK. Phosphorylation by PASK increases
CC translation efficiency. Phosphorylated by ROCK2. Phosphorylation by
CC TGFBR1 inhibits translation elongation. {ECO:0000250|UniProtKB:P68104}.
CC -!- PTM: Trimethylated at Lys-79 by EEF1AKMT1. Methylated at Lys-165 by
CC EEF1AKMT3, methylation by EEF1AKMT3 is dynamic as well as inducible by
CC stress conditions, such as ER-stress, and plays a regulatory role on
CC mRNA translation. Trimethylated at Lys-318 by EEF1AKMT2. Mono-, di-,
CC and trimethylated at Lys-36 by EEF1AKMT4; trimethylated form is
CC predominant. Methylation by EEF1AKMT4 contributes to the fine-tuning of
CC translation rates for a subset of tRNAs. Trimethylated at Gly-2 by
CC METTL13. Mono- and dimethylated at Lys-55 by METTL13; dimethylated form
CC is predominant. {ECO:0000250|UniProtKB:P68104}.
CC -!- PTM: Ubiquitinated at Lys-385 by RNF14 in response to ribosome
CC collisions (ribosome stalling), leading to its degradation by the
CC proteasome and rescue of stalled ribosomes.
CC {ECO:0000250|UniProtKB:P68104}.
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; AJ238405; CAB88863.1; -; mRNA.
DR EMBL; AB060107; BAB60846.1; -; mRNA.
DR EMBL; BC105315; AAI05316.1; -; mRNA.
DR EMBL; BC142302; AAI42303.1; -; mRNA.
DR RefSeq; NP_776960.1; NM_174535.2.
DR AlphaFoldDB; P68103; -.
DR SMR; P68103; -.
DR BioGRID; 159494; 2.
DR IntAct; P68103; 3.
DR STRING; 9913.ENSBTAP00000061151; -.
DR PaxDb; 9913-ENSBTAP00000019318; -.
DR PeptideAtlas; P68103; -.
DR Ensembl; ENSBTAT00000019318.6; ENSBTAP00000019318.5; ENSBTAG00000014534.6.
DR Ensembl; ENSBTAT00000087016.1; ENSBTAP00000061151.1; ENSBTAG00000014534.6.
DR GeneID; 282220; -.
DR KEGG; bta:282220; -.
DR CTD; 1915; -.
DR VEuPathDB; HostDB:ENSBTAG00000014534; -.
DR VGNC; VGNC:56362; EEF1A1.
DR eggNOG; KOG0052; Eukaryota.
DR GeneTree; ENSGT00950000183029; -.
DR HOGENOM; CLU_007265_3_5_1; -.
DR InParanoid; P68103; -.
DR OMA; VACTFES; -.
DR OrthoDB; 5477300at2759; -.
DR TreeFam; TF300304; -.
DR Reactome; R-BTA-156842; Eukaryotic Translation Elongation.
DR Reactome; R-BTA-3371511; HSF1 activation.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR Reactome; R-BTA-8876725; Protein methylation.
DR Proteomes; UP000009136; Chromosome 9.
DR Bgee; ENSBTAG00000014534; Expressed in myometrium and 105 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0003746; F:translation elongation factor activity; ISS:UniProtKB.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
DR GO; GO:1900022; P:regulation of D-erythro-sphingosine kinase activity; ISS:UniProtKB.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; ISS:UniProtKB.
DR CDD; cd01883; EF1_alpha; 1.
DR CDD; cd03693; EF1_alpha_II; 1.
DR CDD; cd03705; EF1_alpha_III; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
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 NCBIfam; TIGR00483; EF-1_alpha; 1.
DR PANTHER; PTHR23115:SF222; ELONGATION FACTOR 1-ALPHA 1-RELATED; 1.
DR PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
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; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cytoplasm; Elongation factor; GTP-binding;
KW Hydrolase; Isopeptide bond; Membrane; Methylation; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Protein biosynthesis; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT CHAIN 2..462
FT /note="Elongation factor 1-alpha 1"
FT /id="PRO_0000090882"
FT DOMAIN 5..242
FT /note="tr-type G"
FT REGION 14..21
FT /note="G1"
FT /evidence="ECO:0000255"
FT REGION 70..74
FT /note="G2"
FT /evidence="ECO:0000255"
FT REGION 91..94
FT /note="G3"
FT /evidence="ECO:0000255"
FT REGION 153..156
FT /note="G4"
FT /evidence="ECO:0000255"
FT REGION 194..196
FT /note="G5"
FT /evidence="ECO:0000255"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P68105"
FT BINDING 153..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P68105"
FT BINDING 194..196
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P68105"
FT MOD_RES 2
FT /note="N,N,N-trimethylglycine"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT MOD_RES 36
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT MOD_RES 36
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT MOD_RES 36
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT MOD_RES 55
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT MOD_RES 79
FT /note="N6,N6,N6-trimethyllysine; by EEF1AKMT1"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT MOD_RES 165
FT /note="N6,N6,N6-trimethyllysine; alternate; by EEF1AKMT3"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT MOD_RES 165
FT /note="N6,N6-dimethyllysine; alternate; by EEF1AKMT3"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT MOD_RES 165
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10126"
FT MOD_RES 165
FT /note="N6-methyllysine; alternate; by EEF1AKMT3"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT MOD_RES 172
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10126"
FT MOD_RES 273
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10126"
FT MOD_RES 300
FT /note="Phosphoserine; by TGFBR1"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT MOD_RES 301
FT /note="5-glutamyl glycerylphosphorylethanolamine"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT MOD_RES 318
FT /note="N6,N6,N6-trimethyllysine; by EEF1AKMT2"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT MOD_RES 374
FT /note="5-glutamyl glycerylphosphorylethanolamine"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT MOD_RES 392
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10126"
FT MOD_RES 392
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10126"
FT MOD_RES 432
FT /note="Phosphothreonine; by PASK"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT MOD_RES 439
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10126"
FT CROSSLNK 385
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT CONFLICT 232
FT /note="L -> M (in Ref. 3; AAI05316)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 50141 MW; D465615545AF686A CRC64;
MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL
DKLKAERERG ITIDISLWKF ETSKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV
GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP PYSQKRYEEI VKEVSTYIKK
IGYNPDTVAF VPISGWNGDN MLEPSANMPW FKGWKVTRKD GNASGTTLLE ALDCILPPTR
PTDKPLRLPL QDVYKIGGIG TVPVGRVETG VLKPGMVVTF APVNVTTEVK SVEMHHEALS
EALPGDNVGF NVKNVSVKDV RRGNVAGDSK NDPPMEAAGF TAQVIILNHP GQISAGYAPV
LDCHTAHIAC KFAELKEKID RRSGKKLEDG PKFLKSGDAA IVDMVPGKPM CVESFSDYPP
LGRFAVRDMR QTVAVGVIKA VDKKAAGAGK VTKSAQKAQK AK
//
