EFTS_RAT
ID EFTS_RAT Reviewed; 324 AA.
AC Q9QYU2;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Elongation factor Ts, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03135};
DE Short=EF-Ts {ECO:0000255|HAMAP-Rule:MF_03135};
DE Short=EF-TsMt {ECO:0000255|HAMAP-Rule:MF_03135};
DE AltName: Full=2A3-2;
DE Flags: Precursor;
GN Name=Tsfm;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10397682; DOI=10.1161/01.atv.19.7.1650;
RA Zibara K., Bourdillon M.C., Chignier E., Covacho C., McGregor J.L.;
RT "Identification and cloning of a new gene (2A3-2), homologous to human
RT translational elongation factor, upregulated in a proliferating rat smooth
RT muscle cell line and in carotid hyperplasia.";
RL Arterioscler. Thromb. Vasc. Biol. 19:1650-1657(1999).
CC -!- FUNCTION: Associates with the EF-Tu.GDP complex and induces the
CC exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-
CC Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
CC {ECO:0000255|HAMAP-Rule:MF_03135}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03135}.
CC -!- SIMILARITY: Belongs to the EF-Ts family. {ECO:0000255|HAMAP-
CC Rule:MF_03135}.
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DR EMBL; AJ005161; CAB56708.1; -; mRNA.
DR AlphaFoldDB; Q9QYU2; -.
DR SMR; Q9QYU2; -.
DR STRING; 10116.ENSRNOP00000064332; -.
DR jPOST; Q9QYU2; -.
DR PaxDb; Q9QYU2; -.
DR PRIDE; Q9QYU2; -.
DR Ensembl; ENSRNOT00000071543; ENSRNOP00000064332; ENSRNOG00000048843.
DR RGD; 1593058; Tsfm.
DR eggNOG; KOG1071; Eukaryota.
DR GeneTree; ENSGT00390000016293; -.
DR InParanoid; Q9QYU2; -.
DR PhylomeDB; Q9QYU2; -.
DR PRO; PR:Q9QYU2; -.
DR Proteomes; UP000002494; Chromosome 7.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0070125; P:mitochondrial translational elongation; IBA:GO_Central.
DR GO; GO:0070129; P:regulation of mitochondrial translation; ISS:UniProtKB.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR Gene3D; 3.30.479.20; -; 2.
DR HAMAP; MF_00050; EF_Ts; 1.
DR InterPro; IPR036402; EF-Ts_dimer_sf.
DR InterPro; IPR001816; Transl_elong_EFTs/EF1B.
DR InterPro; IPR014039; Transl_elong_EFTs/EF1B_dimer.
DR InterPro; IPR018101; Transl_elong_Ts_CS.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR11741; PTHR11741; 1.
DR Pfam; PF00889; EF_TS; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54713; SSF54713; 2.
DR PROSITE; PS01126; EF_TS_1; 1.
DR PROSITE; PS01127; EF_TS_2; 1.
PE 2: Evidence at transcript level;
KW Elongation factor; Mitochondrion; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..44
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03135"
FT CHAIN 45..324
FT /note="Elongation factor Ts, mitochondrial"
FT /id="PRO_0000007470"
FT MOD_RES 75
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZR8"
FT MOD_RES 132
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZR8"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43897"
SQ SEQUENCE 324 AA; 35178 MW; 802AB502BA3B3BE9 CRC64;
MSLLRSLRFF PVACTGRSAR AVLLQPSQPW HTLHAGPSLS SSASSKELLM KLRRTTGYSF
VNCKKALETC GGDLKQAEAW LHKQAQKEGW SKAAKLHGRK TKEGLIGLLQ EENTAVLVEV
NCETDFVSRN VKFQQLVQQV ALGTMAHCQN LTDQLSTYSK GFLNSSELSE LAAGPDGEGS
LKDQLALAIG TLGENMSLKR AAWVKVPSGF YVGSYVHGEM QSPSLQNLVL GKYGALVICQ
TPEQITNLEE VGRRLGQHVV GMAPLSVGSL DDEPGGETET RMLPQPYLLD PSITLGQYVQ
PQGVTVVDFV RFECGEGEQV AEAE