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Database: UniProt
Entry: A0A0U1RPC4_MOUSE
LinkDB: A0A0U1RPC4_MOUSE
Original site: A0A0U1RPC4_MOUSE 
ID   A0A0U1RPC4_MOUSE        Unreviewed;       116 AA.
AC   A0A0U1RPC4;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Tu translation elongation factor, mitochondrial {ECO:0000313|Ensembl:ENSMUSP00000145924.2};
DE   Flags: Fragment;
GN   Name=Tufm {ECO:0000313|Ensembl:ENSMUSP00000145924.2,
GN   ECO:0000313|MGI:MGI:1923686};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000145924.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000145924.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000145924.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [3] {ECO:0007829|PubMed:23806337}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [4] {ECO:0007829|PubMed:23576753}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA   Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA   Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT   identifies substrates of SIRT3 in metabolic pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN   [5] {ECO:0000313|Ensembl:ENSMUSP00000145924.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000145924.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A0U1RPC4; -.
DR   SMR; A0A0U1RPC4; -.
DR   IntAct; A0A0U1RPC4; 1.
DR   MINT; A0A0U1RPC4; -.
DR   jPOST; A0A0U1RPC4; -.
DR   PaxDb; 10090-ENSMUSP00000091180; -.
DR   ProteomicsDB; 367972; -.
DR   Antibodypedia; 13151; 370 antibodies from 30 providers.
DR   Ensembl; ENSMUST00000206572.2; ENSMUSP00000145924.2; ENSMUSG00000073838.11.
DR   AGR; MGI:1923686; -.
DR   MGI; MGI:1923686; Tufm.
DR   VEuPathDB; HostDB:ENSMUSG00000073838; -.
DR   eggNOG; KOG0460; Eukaryota.
DR   GeneTree; ENSGT00940000156748; -.
DR   ChiTaRS; Tufm; mouse.
DR   Proteomes; UP000000589; Chromosome 7.
DR   Bgee; ENSMUSG00000073838; Expressed in right kidney and 71 other cell types or tissues.
DR   ExpressionAtlas; A0A0U1RPC4; baseline and differential.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
PE   1: Evidence at protein level;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Proteomics identification {ECO:0007829|EPD:A0A0U1RPC4,
KW   ECO:0007829|MaxQB:A0A0U1RPC4};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT   DOMAIN          1..59
FT                   /note="Translation elongation factor EFTu-like"
FT                   /evidence="ECO:0000259|Pfam:PF03144"
FT   DOMAIN          64..108
FT                   /note="Translation elongation factor EFTu/EF1A C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03143"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|Ensembl:ENSMUSP00000145924.2"
SQ   SEQUENCE   116 AA;  12976 MW;  72E0A3A1BA2A3404 CRC64;
     GILKKGDECE LLGHNKNIRT VVTGIEMFHK SLERAEAGDN LGALVRGLKR EDLRRGLVMV
     KPGSIQPHQK VEAQVYILSK EEGGRHKPFV SHFMPVMFSL TWDMACRVIL PPGKVC
//
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