ID   EFTU_RAT                Reviewed;         452 AA.
AC   P85834;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=Elongation factor Tu, mitochondrial;
DE   Flags: Precursor;
GN   Name=Tufm {ECO:0000250|UniProtKB:P49411};
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] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000269|PubMed:15057822};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=19343716; DOI=10.1002/pmic.200800664;
RA   Maurya D.K., Sundaram C.S., Bhargava P.;
RT   "Proteome profile of the mature rat olfactory bulb.";
RL   Proteomics 9:2593-2599(2009).
CC   -!- FUNCTION: Plays a role in the regulation of autophagy and innate
CC       immunity. Recruits ATG5-ATG12 and NLRX1 at mitochondria and serves as a
CC       checkpoint of the RIGI-MAVS pathway. In turn, inhibits RLR-mediated
CC       type I interferon while promoting autophagy. Promotes the GTP-dependent
CC       binding of aminoacyl-tRNA to the A-site of ribosomes during protein
CC       biosynthesis. {ECO:0000250|UniProtKB:P49411}.
CC   -!- SUBUNIT: Interacts with NLRX1. Interacts with ATG16L1.
CC       {ECO:0000250|UniProtKB:P49411}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P49411}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR   EMBL; AABR03000083; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001099765.1; NM_001106295.1.
DR   AlphaFoldDB; P85834; -.
DR   SMR; P85834; -.
DR   BioGRID; 254286; 8.
DR   IntAct; P85834; 6.
DR   MINT; P85834; -.
DR   STRING; 10116.ENSRNOP00000025203; -.
DR   GlyGen; P85834; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P85834; -.
DR   PhosphoSitePlus; P85834; -.
DR   jPOST; P85834; -.
DR   PaxDb; 10116-ENSRNOP00000025203; -.
DR   Ensembl; ENSRNOT00000025203.7; ENSRNOP00000025203.6; ENSRNOG00000018604.7.
DR   Ensembl; ENSRNOT00055054012; ENSRNOP00055044694; ENSRNOG00055031153.
DR   Ensembl; ENSRNOT00060050579; ENSRNOP00060042092; ENSRNOG00060029136.
DR   Ensembl; ENSRNOT00065027543; ENSRNOP00065021670; ENSRNOG00065016529.
DR   GeneID; 293481; -.
DR   KEGG; rno:293481; -.
DR   UCSC; RGD:1305501; rat.
DR   AGR; RGD:1305501; -.
DR   CTD; 7284; -.
DR   RGD; 1305501; Tufm.
DR   eggNOG; KOG0460; Eukaryota.
DR   GeneTree; ENSGT00940000156748; -.
DR   HOGENOM; CLU_007265_0_0_1; -.
DR   InParanoid; P85834; -.
DR   OMA; FHNNYRP; -.
DR   OrthoDB; 167272at2759; -.
DR   PhylomeDB; P85834; -.
DR   PRO; PR:P85834; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000018604; Expressed in heart and 20 other cell types or tissues.
DR   GO; GO:0042645; C:mitochondrial nucleoid; ISO:RGD.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0045202; C:synapse; IDA:SynGO.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; ISO:RGD.
DR   GO; GO:0070125; P:mitochondrial translational elongation; IBA:GO_Central.
DR   GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR   GO; GO:0006414; P:translational elongation; ISO:RGD.
DR   CDD; cd01884; EF_Tu; 1.
DR   CDD; cd03697; EFTU_II; 1.
DR   CDD; cd03706; mtEFTU_III; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   InterPro; IPR041709; EF-Tu_GTP-bd.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR033720; EFTU_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; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   NCBIfam; TIGR00485; EF-Tu; 1.
DR   PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
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; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
DR   World-2DPAGE; 0004:P85834; -.
DR   Genevisible; P85834; RN.
PE   1: Evidence at protein level;
KW   Acetylation; Elongation factor; GTP-binding; Mitochondrion;
KW   Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..43
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250|UniProtKB:P49411"
FT   CHAIN           44..452
FT                   /note="Elongation factor Tu, mitochondrial"
FT                   /id="PRO_0000339242"
FT   DOMAIN          55..251
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          64..71
FT                   /note="G1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          105..109
FT                   /note="G2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          126..129
FT                   /note="G3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          181..184
FT                   /note="G4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          219..221
FT                   /note="G5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   BINDING         64..71
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P49411"
FT   BINDING         126..130
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P49411"
FT   BINDING         181..184
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P49411"
FT   MOD_RES         79
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P49411"
FT   MOD_RES         88
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P49411"
FT   MOD_RES         88
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BFR5"
FT   MOD_RES         234
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BFR5"
FT   MOD_RES         256
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P49411"
FT   MOD_RES         278
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P49411"
FT   MOD_RES         286
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BFR5"
FT   MOD_RES         312
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BFR5"
FT   MOD_RES         361
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BFR5"
FT   MOD_RES         418
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P49411"
SQ   SEQUENCE   452 AA;  49522 MW;  67C39530FE8EC7CD CRC64;
     MAAATLLRAT PRFSGLCASP TPFLQGRLRP LKAPASPFLC RGLAVEAKKT YVRDKPHVNV
     GTIGHVDHGK TTLTAAITKI LAEGGGAKFK KYEEIDNAPE ERARGITINA AHVEYSTAAR
     HYAHTDCPGH ADYVKNMITG TAPLDGCILV VAANDGPMPQ TREHLLLAKQ IGVEHVVVYV
     NKADAVQDSE MVELVELEIR ELLTEFGYKG EETPVIVGSA LCALEQRDPE LGVKSVQKLL
     DAVDTYIPVP TRDLEKPFLL PVESVYSIPG RGTVVTGTLE RGILKKGDEC ELLGHNKNIR
     TVVTGIEMFH KSLERAEAGD NLGALVRGLK REDLRRGLVM VKPGSIQPHQ KVEAQVYILS
     KEEGGRHKPF VSHFMPVMFS LTWDMACRVI LPPGKELAMP GEDLKLSLIL RQPMILEKGQ
     RFTLRDGNKT IGTGLVTDVP AMTEEDKNIK WS
//