ID   MCA3_CRIGR              Reviewed;         174 AA.
AC   P70102;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Eukaryotic translation elongation factor 1 epsilon-1;
DE   AltName: Full=Elongation factor p18;
DE   AltName: Full=Multisynthase complex auxiliary component p18;
GN   Name=EEF1E1;
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8849690; DOI=10.1016/0014-5793(96)01005-8;
RA   Quevillon S., Mirande M.;
RT   "The p18 component of the multisynthetase complex shares a protein motif
RT   with the beta and gamma subunits of eukaryotic elongation factor 1.";
RL   FEBS Lett. 395:63-67(1996).
CC   -!- FUNCTION: Positive modulator of ATM response to DNA damage.
CC       {ECO:0000250|UniProtKB:Q9D1M4}.
CC   -!- SUBUNIT: Part of a multisubunit complex that groups tRNA ligases for
CC       Arg (RARS1), Asp (DARS1), Gln (QARS1), Ile (IARS1), Leu (LARS1), Lys
CC       (KARS1), Met (MARS1) the bifunctional ligase for Glu and Pro (EPRS1)
CC       and the auxiliary subunits AIMP1/p43, AIMP2/p38 and EEF1E1/p18. Can
CC       interact simultaneously with MARS1 and EPRS1. Forms a linear complex
CC       that contains MARS1, EEF1E1, EPRS1 and AIMP2 that is at the core of the
CC       multisubunit complex. Interacts with ATM and ATR. The interaction with
CC       ATM, which takes place independently of TP53, is induced by DNA damage
CC       that may occur during genotoxic stress or cell growth. The interaction
CC       with ATR is enhanced by UV irradiation. {ECO:0000250|UniProtKB:O43324}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9D1M4}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9D1M4}. Note=Cytoplasmic under growth arrest
CC       conditions. Translocated into the nucleus when growth resumes at S
CC       phase and following DNA damage. {ECO:0000250|UniProtKB:Q9D1M4}.
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DR   EMBL; U67146; AAB18625.1; -; mRNA.
DR   PIR; S74241; S74241.
DR   RefSeq; NP_001233672.1; NM_001246743.1.
DR   AlphaFoldDB; P70102; -.
DR   SMR; P70102; -.
DR   STRING; 10029.NP_001233672.1; -.
DR   Ensembl; ENSCGRT00001021048; ENSCGRP00001016804; ENSCGRG00001017026.
DR   GeneID; 100689310; -.
DR   KEGG; cge:100689310; -.
DR   CTD; 9521; -.
DR   eggNOG; KOG0867; Eukaryota.
DR   GeneTree; ENSGT00390000016974; -.
DR   OMA; FIVDLTF; -.
DR   OrthoDB; 1422931at2759; -.
DR   GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0043517; P:positive regulation of DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR   InterPro; IPR042450; EEF1E1.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR004046; GST_C.
DR   PANTHER; PTHR44490; PTHR44490; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Coiled coil; Cytoplasm; Nucleus; Protein biosynthesis.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O43324"
FT   CHAIN           2..174
FT                   /note="Eukaryotic translation elongation factor 1 epsilon-
FT                   1"
FT                   /id="PRO_0000221131"
FT   DOMAIN          50..173
FT                   /note="GST C-terminal"
FT   REGION          2..56
FT                   /note="N-terminal"
FT                   /evidence="ECO:0000250"
FT   REGION          57..63
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          64..152
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          153..169
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O43324"
FT   MOD_RES         138
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O43324"
SQ   SEQUENCE   174 AA;  19818 MW;  9A5FC3B1ACAE4C46 CRC64;
     MAAAAELKLL EKSLGLRPGN KYSAQGERQI PVLQTNNGPS LTGLATIATH LVKQASKEHL
     LGSTAEEKAL VQQWLEYRIT QVDGHSSKED THTLLKDLNS YLEDKVYLAG YNITLADILL
     YYGLHRFIVD LTVQEKEKYL NVSRWFCHIQ HYPDIRQHLS SVVFIKNRLY ANSH