EF1A1_PONAB
ID EF1A1_PONAB Reviewed; 462 AA.
AC Q5R4R8; Q5NVF3;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Elongation factor 1-alpha 1;
DE Short=EF-1-alpha-1;
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;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis. Plays a
CC role in the positive regulation of IFNG transcription in T-helper 1
CC cells as part of an IFNG promoter-binding complex with TXK and PARP1.
CC {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). May interact with ERGIC2. Interacts with IFIT1 (via
CC TPR repeats 4-7) (By similarity). Interacts with DLC1, facilitating
CC distribution to the membrane periphery and ruffles upon growth factor
CC stimulation. Interacts with ZPR1; the interaction occurs in a epidermal
CC growth factor (EGF)-dependent manner (By similarity). Interacts with
CC PPP1R16B (By similarity). Interacts with SPHK1 and SPHK2; both
CC interactions increase SPHK1 and SPHK2 kinase activity (By similarity).
CC {ECO:0000250|UniProtKB:P68104}.
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.
CC {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 -!- 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; CR861176; CAH93248.1; -; mRNA.
DR EMBL; CR926083; CAI29710.1; -; mRNA.
DR RefSeq; NP_001126911.1; NM_001133439.1.
DR RefSeq; XP_009240283.1; XM_009242008.1.
DR RefSeq; XP_009240413.1; XM_009242138.1.
DR AlphaFoldDB; Q5R4R8; -.
DR SMR; Q5R4R8; -.
DR STRING; 9601.ENSPPYP00000018935; -.
DR Ensembl; ENSPPYT00000019520; ENSPPYP00000018778; ENSPPYG00000016777.
DR GeneID; 100173928; -.
DR GeneID; 100455760; -.
DR KEGG; pon:100173928; -.
DR KEGG; pon:100455760; -.
DR CTD; 1915; -.
DR eggNOG; KOG0052; Eukaryota.
DR GeneTree; ENSGT00950000183029; -.
DR HOGENOM; CLU_007265_3_5_1; -.
DR InParanoid; Q5R4R8; -.
DR OMA; EMHHKSV; -.
DR OrthoDB; 1150082at2759; -.
DR TreeFam; TF300304; -.
DR Proteomes; UP000001595; Chromosome 6.
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; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
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 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 2: Evidence at transcript level;
KW Acetylation; Cell membrane; Cytoplasm; Elongation factor; GTP-binding;
KW Membrane; Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; 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_0000090888"
FT DOMAIN 5..242
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 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 CONFLICT 253
FT /note="V -> A (in Ref. 1; CAI29710)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="M -> V (in Ref. 1; CAH93248)"
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
