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   02-SEP-2026, entry version 165.
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 (By similarity). Also plays a role
CC       in cytoskeleton organization by promoting actin bundling (By
CC       similarity). {ECO:0000250|UniProtKB:P68104,
CC       ECO:0000250|UniProtKB:P68105}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + phosphate + H(+); 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). Interacts
CC       with guanyl-nucleotide exchange factor EEF1B2 (By similarity).
CC       Interacts (via middle-region) with HTATIP2 (via N-terminus); the
CC       interaction is direct and competes with EEF1A1 binding to guanyl-
CC       nucleotide exchange factor EEF1B2, thereby inhibiting GDP for GTP
CC       exchange and reactivation of EEF1A1 (By similarity). Interacts with
CC       tRNA (By similarity). Interacts with CEP112 (By similarity).
CC       {ECO:0000250|UniProtKB:P62630, 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   FunCoup; P68103; 2332.
DR   IntAct; P68103; 3.
DR   STRING; 9913.ENSBTAP00000061151; -.
DR   PaxDb; 9913-ENSBTAP00000061151; -.
DR   PeptideAtlas; P68103; -.
DR   Ensembl; ENSBTAT00000087016.1; ENSBTAP00000061151.1; ENSBTAG00000014534.7.
DR   Ensembl; ENSBTAT00085047524; ENSBTAP00085043939; ENSBTAG00085016873.
DR   Ensembl; ENSBTAT00085078206; ENSBTAP00085041455; ENSBTAG00085034623.
DR   Ensembl; ENSBTAT00090032113; ENSBTAP00090016382; ENSBTAG00090016186.
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; FAPQNIT; -.
DR   OrthoDB; 9857985at2759; -.
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   CD-CODE; D7FE2080; Nucleolus.
DR   PRO; PR:P68103; -.
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:InterPro.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0019209; F:kinase activator 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: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   FunFam; 2.40.30.10:FF:000005; Elongation factor 1-alpha; 1.
DR   FunFam; 3.40.50.300:FF:000090; Elongation factor 1-alpha; 1.
DR   FunFam; 2.40.30.10:FF:000168; Elongation factor 1-alpha 2; 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; IPR054696; GTP-eEF1A_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR050100; TRAFAC_GTPase_members.
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   NCBIfam; TIGR00483; EF-1_alpha; 1.
DR   NCBIfam; NF008969; PRK12317.1; 1.
DR   PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
DR   Pfam; PF22594; GTP-eEF1A_C; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 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
//