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 27-MAR-2024, entry version 103.
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 PaxDb; 10029-NP_001233672-1; -.
DR Ensembl; ENSCGRT00000024577; ENSCGRP00000024247; ENSCGRG00000017575.
DR Ensembl; ENSCGRT00001021048.1; ENSCGRP00001016804.1; ENSCGRG00001017026.1.
DR GeneID; 100689310; -.
DR KEGG; cge:100689310; -.
DR CTD; 9521; -.
DR eggNOG; KOG0867; Eukaryota.
DR GeneTree; ENSGT00390000016974; -.
DR OMA; NWATGTH; -.
DR OrthoDB; 2950728at2759; -.
DR Proteomes; UP000694386; Unplaced.
DR Proteomes; UP001108280; Chromosome 3.
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 CDD; cd10305; GST_C_AIMP3; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.90; -; 1.
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; EUKARYOTIC TRANSLATION ELONGATION FACTOR 1 EPSILON-1; 1.
DR PANTHER; PTHR44490:SF1; EUKARYOTIC TRANSLATION ELONGATION FACTOR 1 EPSILON-1; 1.
DR Pfam; PF00043; GST_C; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 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
//
