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EF1A1_FELCA
ID   EF1A1_FELCA             Reviewed;         462 AA.
AC   Q66RN5;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 123.
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   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Pathak S., Kapil S.;
RL   Submitted (AUG-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; AY712790; AAU10465.1; -; mRNA.
DR   RefSeq; NP_001009326.1; NM_001009326.1.
DR   RefSeq; XP_006931902.1; XM_006931840.3.
DR   RefSeq; XP_019685628.1; XM_019830069.1.
DR   AlphaFoldDB; Q66RN5; -.
DR   SMR; Q66RN5; -.
DR   STRING; 9685.ENSFCAP00000024974; -.
DR   Ensembl; ENSFCAT00000031196; ENSFCAP00000024974; ENSFCAG00000030977.
DR   GeneID; 493922; -.
DR   KEGG; fca:493922; -.
DR   CTD; 1915; -.
DR   eggNOG; KOG0052; Eukaryota.
DR   GeneTree; ENSGT00950000183029; -.
DR   HOGENOM; CLU_007265_3_5_1; -.
DR   InParanoid; Q66RN5; -.
DR   OMA; EMHHKSV; -.
DR   OrthoDB; 1150082at2759; -.
DR   Proteomes; UP000011712; Chromosome B2.
DR   Bgee; ENSFCAG00000030977; Expressed in embryo and 11 other tissues.
DR   GO; GO:0030864; C:cortical actin cytoskeleton; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
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:0032587; C:ruffle membrane; IEA:Ensembl.
DR   GO; GO:0005516; F:calmodulin binding; IEA:Ensembl.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR   GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IEA:Ensembl.
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; 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   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_0000090884"
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"
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
 
 
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