EFTU_RAT
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 03-AUG-2022, entry version 95.
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 RIG-I/DDX58-MAVS pathway. In turn, inhibits RLR-
CC mediated type I interferon while promoting autophagy. Promotes the GTP-
CC dependent binding of aminoacyl-tRNA to the A-site of ribosomes during
CC protein 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; 7.
DR IntAct; P85834; 6.
DR MINT; P85834; -.
DR STRING; 10116.ENSRNOP00000025203; -.
DR iPTMnet; P85834; -.
DR PhosphoSitePlus; P85834; -.
DR World-2DPAGE; 0004:P85834; -.
DR jPOST; P85834; -.
DR PaxDb; P85834; -.
DR PRIDE; P85834; -.
DR Ensembl; ENSRNOT00000025203; ENSRNOP00000025203; ENSRNOG00000018604.
DR GeneID; 293481; -.
DR KEGG; rno:293481; -.
DR UCSC; RGD:1305501; rat.
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; EGDKEWG; -.
DR OrthoDB; 491836at2759; -.
DR PhylomeDB; P85834; -.
DR PRO; PR:P85834; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000018604; Expressed in heart and 20 other tissues.
DR Genevisible; P85834; RN.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
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 Gene3D; 3.40.50.300; -; 1.
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 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; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00485; EF-Tu; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
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
