ID TOM70_HUMAN Reviewed; 608 AA. AC O94826; D3DN48; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 202. DE RecName: Full=Mitochondrial import receptor subunit TOM70 {ECO:0000305}; DE AltName: Full=Mitochondrial precursor proteins import receptor; DE AltName: Full=Translocase of outer membrane 70 kDa subunit; DE AltName: Full=Translocase of outer mitochondrial membrane protein 70 {ECO:0000312|HGNC:HGNC:11985}; GN Name=TOMM70 {ECO:0000312|HGNC:HGNC:11985}; GN Synonyms=KIAA0719, TOM70, TOMM70A; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=9872452; DOI=10.1093/dnares/5.5.277; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., RA Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XI. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 5:277-286(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skin, and Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP FUNCTION, INTERACTION WITH HSP90AA1 AND HSPA8, MUTAGENESIS OF ARG-192, AND RP ACTIVITY REGULATION. RX PubMed=12526792; DOI=10.1016/s0092-8674(02)01250-3; RA Young J.C., Hoogenraad N.J., Hartl F.U.; RT "Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the RT mitochondrial import receptor Tom70."; RL Cell 112:41-50(2003). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [6] RP IDENTIFICATION IN THE TOM COMPLEX. RX PubMed=18331822; DOI=10.1016/j.bbrc.2008.02.150; RA Kato H., Mihara K.; RT "Identification of Tom5 and Tom6 in the preprotein translocase complex of RT human mitochondrial outer membrane."; RL Biochem. Biophys. Res. Commun. 369:958-963(2008). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-185, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [11] RP FUNCTION, INTERACTION WITH TRADD; TRAF6; STING; HSP90AA1 AND MAVS, RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-192. RX PubMed=20628368; DOI=10.1038/cr.2010.103; RA Liu X.Y., Wei B., Shi H.X., Shan Y.F., Wang C.; RT "Tom70 mediates activation of interferon regulatory factor 3 on RT mitochondria."; RL Cell Res. 20:994-1011(2010). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91; SER-110 AND SER-434, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91 AND SER-96, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [19] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-71, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [20] RP FUNCTION, INTERACTION WITH HSP90AA1, SUBCELLULAR LOCATION, AND MUTAGENESIS RP OF ARG-192 AND LYS-195. RX PubMed=25609812; DOI=10.1128/jvi.02959-14; RA Wei B., Cui Y., Huang Y., Liu H., Li L., Li M., Ruan K.C., Zhou Q., RA Wang C.; RT "Tom70 mediates Sendai virus-induced apoptosis on mitochondria."; RL J. Virol. 89:3804-3818(2015). RN [21] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [22] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-275, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [23] RP INTERACTION WITH SARS-COV VIRUS AND SARS-COV-2 VIRUS PROTEIN ORF9B RP (MICROBIAL INFECTION), AND FUNCTION. RX PubMed=32728199; DOI=10.1038/s41423-020-0514-8; RA Jiang H.W., Zhang H.N., Meng Q.F., Xie J., Li Y., Chen H., Zheng Y.X., RA Wang X.N., Qi H., Zhang J., Wang P.H., Han Z.G., Tao S.C.; RT "SARS-CoV-2 Orf9b suppresses type I interferon responses by targeting RT TOM70."; RL Cell. Mol. Immunol. 17:998-1000(2020). RN [24] RP INTERACTION WITH T.GONDII MAF1B1 (MICROBIAL INFECTION), SUBCELLULAR RP LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=33723040; DOI=10.1073/pnas.2013336118; RA Blank M.L., Xia J., Morcos M.M., Sun M., Cantrell P.S., Liu Y., Zeng X., RA Powell C.J., Yates N., Boulanger M.J., Boyle J.P.; RT "Toxoplasma gondii association with host mitochondria requires key RT mitochondrial protein import machinery."; RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021). RN [25] {ECO:0000305} RP FUNCTION, AND INTERACTION WITH T.GONDII MAF1B1 (MICROBIAL INFECTION). RX PubMed=35025629; DOI=10.1126/science.abi4343; RA Li X., Straub J., Medeiros T.C., Mehra C., den Brave F., Peker E., RA Atanassov I., Stillger K., Michaelis J.B., Burbridge E., Adrain C., RA Muench C., Riemer J., Becker T., Pernas L.F.; RT "Mitochondria shed their outer membrane in response to infection-induced RT stress."; RL Science 375:eabi4343-eabi4343(2022). RN [26] {ECO:0007744|PDB:7KDT} RP STRUCTURE BY ELECTRON MICROSCOPY (3.05 ANGSTROMS) OF 109-608 IN COMPLEX RP WITH SARS-COV-2 VIRUS PROTEIN ORF9B, FUNCTION, SUBCELLULAR LOCATION, AND RP INTERACTION WITH SARS-COV VIRUS AND SARS-COV-2 VIRUS PROTEIN ORF9B RP (MICROBIAL INFECTION). RX PubMed=33060197; DOI=10.1126/science.abe9403; RG QCRG Structural Biology Consortium; RG Zoonomia Consortium; RA Gordon D.E., Hiatt J., Bouhaddou M., Rezelj V.V., Ulferts S., Braberg H., RA Jureka A.S., Obernier K., Guo J.Z., Batra J., Kaake R.M., Weckstein A.R., RA Owens T.W., Gupta M., Pourmal S., Titus E.W., Cakir M., Soucheray M., RA McGregor M., Cakir Z., Jang G., O'Meara M.J., Tummino T.A., Zhang Z., RA Foussard H., Rojc A., Zhou Y., Kuchenov D., Huettenhain R., Xu J., RA Eckhardt M., Swaney D.L., Fabius J.M., Ummadi M., Tutuncuoglu B., RA Rathore U., Modak M., Haas P., Haas K.M., Naing Z.Z.C., Pulido E.H., RA Shi Y., Barrio-Hernandez I., Memon D., Petsalaki E., Dunham A., RA Marrero M.C., Burke D., Koh C., Vallet T., Silvas J.A., Azumaya C.M., RA Billesboelle C., Brilot A.F., Campbell M.G., Diallo A., Dickinson M.S., RA Diwanji D., Herrera N., Hoppe N., Kratochvil H.T., Liu Y., Merz G.E., RA Moritz M., Nguyen H.C., Nowotny C., Puchades C., Rizo A.N., RA Schulze-Gahmen U., Smith A.M., Sun M., Young I.D., Zhao J., Asarnow D., RA Biel J., Bowen A., Braxton J.R., Chen J., Chio C.M., Chio U.S., RA Deshpande I., Doan L., Faust B., Flores S., Jin M., Kim K., Lam V.L., RA Li F., Li J., Li Y.L., Li Y., Liu X., Lo M., Lopez K.E., Melo A.A., RA Moss F.R. III, Nguyen P., Paulino J., Pawar K.I., Peters J.K., RA Pospiech T.H. Jr., Safari M., Sangwan S., Schaefer K., Thomas P.V., RA Thwin A.C., Trenker R., Tse E., Tsui T.K.M., Wang F., Whitis N., Yu Z., RA Zhang K., Zhang Y., Zhou F., Saltzberg D., Hodder A.J., Shun-Shion A.S., RA Williams D.M., White K.M., Rosales R., Kehrer T., Miorin L., Moreno E., RA Patel A.H., Rihn S., Khalid M.M., Vallejo-Gracia A., Fozouni P., RA Simoneau C.R., Roth T.L., Wu D., Karim M.A., Ghoussaini M., Dunham I., RA Berardi F., Weigang S., Chazal M., Park J., Logue J., McGrath M., RA Weston S., Haupt R., Hastie C.J., Elliott M., Brown F., Burness K.A., RA Reid E., Dorward M., Johnson C., Wilkinson S.G., Geyer A., Giesel D.M., RA Baillie C., Raggett S., Leech H., Toth R., Goodman N., Keough K.C., RA Lind A.L., Klesh R.J., Hemphill K.R., Carlson-Stevermer J., Oki J., RA Holden K., Maures T., Pollard K.S., Sali A., Agard D.A., Cheng Y., RA Fraser J.S., Frost A., Jura N., Kortemme T., Manglik A., Southworth D.R., RA Stroud R.M., Alessi D.R., Davies P., Frieman M.B., Ideker T., Abate C., RA Jouvenet N., Kochs G., Shoichet B., Ott M., Palmarini M., Shokat K.M., RA Garcia-Sastre A., Rassen J.A., Grosse R., Rosenberg O.S., Verba K.A., RA Basler C.F., Vignuzzi M., Peden A.A., Beltrao P., Krogan N.J.; RT "Comparative host-coronavirus protein interaction networks reveal pan-viral RT disease mechanisms."; RL Science 0:0-0(2020). CC -!- FUNCTION: Acts as a receptor of the preprotein translocase complex of CC the outer mitochondrial membrane (TOM complex) (PubMed:12526792). CC Recognizes and mediates the translocation of mitochondrial preproteins CC from the cytosol into the mitochondria in a chaperone dependent manner CC (PubMed:12526792, PubMed:35025629). Mediates TBK1 and IRF3 activation CC induced by MAVS in response to Sendai virus infection and promotes host CC antiviral responses during virus infection (PubMed:20628368, CC PubMed:25609812, PubMed:32728199). Upon Sendai virus infection, CC recruits HSP90AA1:IRF3:BAX in mitochondrion and the complex induces CC apoptosis (PubMed:25609812). {ECO:0000269|PubMed:12526792, CC ECO:0000269|PubMed:20628368, ECO:0000269|PubMed:25609812, CC ECO:0000269|PubMed:32728199, ECO:0000269|PubMed:35025629}. CC -!- SUBUNIT: Forms part of the preprotein translocase complex of the outer CC mitochondrial membrane (TOM complex) which consists of at least 7 CC different proteins (TOMM5, TOMM6, TOMM7, TOMM20, TOMM22, TOMM40 and CC TOMM70) (PubMed:18331822). Interacts with CAPN8 (By similarity). CC Interacts with TRADD, TRAF6 and STING (PubMed:20628368). Interacts with CC MAVS; the interaction is enhanced by Sendai virus infection CC (PubMed:20628368). Interacts with HSPA8 and HSP90AA1; both interactions CC are required for preprotein mitochondrial import (PubMed:12526792). The CC interaction with HSP90AA1 is direct and mediates the association of CC TOMM70 with IRF3 and TBK1 (PubMed:20628368, PubMed:25609812). CC {ECO:0000250|UniProtKB:Q9CZW5, ECO:0000269|PubMed:12526792, CC ECO:0000269|PubMed:18331822, ECO:0000269|PubMed:20628368, CC ECO:0000269|PubMed:25609812}. CC -!- SUBUNIT: (Microbial infection) Interacts (via C-terminus) with SARS CC coronaviru/SARS-CoV and SARS coronavirus-2/SARS-CoV-2 virus protein CC ORF9b. {ECO:0000269|PubMed:33060197}. CC -!- SUBUNIT: (Microbial infection) Interacts with parasite T.gondii RH CC strain MAF1b1; the interaction impairs TOMM70 import activity, enables CC the parasite to associate with the host mitochondria and facilitates CC the association of MAF1b1 with MIB complex component SAMM50, promoting CC the formation of SPOTs (structures positive for outer mitochondrial CC membrane (OMM)); the interaction is probably indirect. CC {ECO:0000269|PubMed:33723040, ECO:0000269|PubMed:35025629}. CC -!- INTERACTION: CC O94826; P07900: HSP90AA1; NbExp=4; IntAct=EBI-2800236, EBI-296047; CC O94826; P0DTD2: 9b; Xeno; NbExp=28; IntAct=EBI-2800236, EBI-25475909; CC O94826; P59636: 9b; Xeno; NbExp=7; IntAct=EBI-2800236, EBI-9021274; CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane CC {ECO:0000269|PubMed:20628368, ECO:0000269|PubMed:25609812, CC ECO:0000269|PubMed:33723040}; Single-pass membrane protein CC {ECO:0000255}. CC -!- SUBCELLULAR LOCATION: Note=(Microbial infection) During parasite CC T.gondii-mediated infection, enriched at the interface between the host CC mitochondria and the parasitopharous vacuole. CC {ECO:0000269|PubMed:33723040}. CC -!- SIMILARITY: Belongs to the Tom70 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA34439.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB018262; BAA34439.2; ALT_INIT; mRNA. DR EMBL; CH471052; EAW79822.1; -; Genomic_DNA. DR EMBL; CH471052; EAW79823.1; -; Genomic_DNA. DR EMBL; BC003633; AAH03633.1; -; mRNA. DR EMBL; BC052994; AAH52994.1; -; mRNA. DR CCDS; CCDS33807.1; -. DR RefSeq; NP_055635.3; NM_014820.4. DR PDB; 7DHG; X-ray; 2.20 A; C=1-608. DR PDB; 7KDT; EM; 3.05 A; A=109-608. DR PDBsum; 7DHG; -. DR PDBsum; 7KDT; -. DR AlphaFoldDB; O94826; -. DR EMDB; EMD-22829; -. DR SMR; O94826; -. DR BioGRID; 115201; 133. DR ComplexPortal; CPX-6121; TOM40 mitochondrial outer membrane translocase complex. DR CORUM; O94826; -. DR IntAct; O94826; 57. DR MINT; O94826; -. DR STRING; 9606.ENSP00000284320; -. DR GlyGen; O94826; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O94826; -. DR MetOSite; O94826; -. DR PhosphoSitePlus; O94826; -. DR SwissPalm; O94826; -. DR BioMuta; TOMM70; -. DR EPD; O94826; -. DR jPOST; O94826; -. DR MassIVE; O94826; -. DR MaxQB; O94826; -. DR PaxDb; 9606-ENSP00000284320; -. DR PeptideAtlas; O94826; -. DR ProteomicsDB; 50468; -. DR Pumba; O94826; -. DR Antibodypedia; 3025; 265 antibodies from 30 providers. DR DNASU; 9868; -. DR Ensembl; ENST00000284320.6; ENSP00000284320.5; ENSG00000154174.8. DR GeneID; 9868; -. DR KEGG; hsa:9868; -. DR MANE-Select; ENST00000284320.6; ENSP00000284320.5; NM_014820.5; NP_055635.3. DR UCSC; uc003dtw.4; human. DR AGR; HGNC:11985; -. DR CTD; 9868; -. DR DisGeNET; 9868; -. DR GeneCards; TOMM70; -. DR HGNC; HGNC:11985; TOMM70. DR HPA; ENSG00000154174; Low tissue specificity. DR MIM; 606081; gene. DR neXtProt; NX_O94826; -. DR OpenTargets; ENSG00000154174; -. DR PharmGKB; PA36669; -. DR VEuPathDB; HostDB:ENSG00000154174; -. DR eggNOG; KOG0547; Eukaryota. DR GeneTree; ENSGT00940000157095; -. DR HOGENOM; CLU_017516_2_0_1; -. DR InParanoid; O94826; -. DR OMA; QWRGDIE; -. DR OrthoDB; 1083789at2759; -. DR PhylomeDB; O94826; -. DR TreeFam; TF106203; -. DR PathwayCommons; O94826; -. DR Reactome; R-HSA-1268020; Mitochondrial protein import. DR Reactome; R-HSA-168928; DDX58/IFIH1-mediated induction of interferon-alpha/beta. DR Reactome; R-HSA-5205685; PINK1-PRKN Mediated Mitophagy. DR Reactome; R-HSA-5689880; Ub-specific processing proteases. DR Reactome; R-HSA-9692916; SARS-CoV-1 activates/modulates innate immune responses. DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses. DR SignaLink; O94826; -. DR SIGNOR; O94826; -. DR BioGRID-ORCS; 9868; 180 hits in 1161 CRISPR screens. DR ChiTaRS; TOMM70; human. DR GeneWiki; TOMM70A; -. DR GenomeRNAi; 9868; -. DR Pharos; O94826; Tbio. DR PRO; PR:O94826; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; O94826; Protein. DR Bgee; ENSG00000154174; Expressed in endothelial cell and 214 other cell types or tissues. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProt. DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome. DR GO; GO:0005742; C:mitochondrial outer membrane translocase complex; ISS:FlyBase. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0140596; C:TOM complex; NAS:ComplexPortal. DR GO; GO:0030943; F:mitochondrion targeting sequence binding; ISS:FlyBase. DR GO; GO:0060090; F:molecular adaptor activity; IDA:UniProt. DR GO; GO:0008320; F:protein transmembrane transporter activity; TAS:BHF-UCL. DR GO; GO:0002218; P:activation of innate immune response; IDA:UniProtKB. DR GO; GO:0098586; P:cellular response to virus; IDA:UniProtKB. DR GO; GO:0061052; P:negative regulation of cell growth involved in cardiac muscle cell development; IEA:Ensembl. DR GO; GO:0002230; P:positive regulation of defense response to virus by host; IDA:UniProtKB. DR GO; GO:0032728; P:positive regulation of interferon-beta production; IDA:UniProtKB. DR GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; IEA:Ensembl. DR GO; GO:0030150; P:protein import into mitochondrial matrix; ISS:FlyBase. DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; ISS:FlyBase. DR GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; NAS:ComplexPortal. DR GO; GO:0006626; P:protein targeting to mitochondrion; ISS:FlyBase. DR GO; GO:0042981; P:regulation of apoptotic process; IDA:UniProtKB. DR GO; GO:0097068; P:response to thyroxine; IEA:Ensembl. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR001440; TPR_1. DR InterPro; IPR019734; TPR_repeat. DR PANTHER; PTHR46208; MITOCHONDRIAL IMPORT RECEPTOR SUBUNIT TOM70; 1. DR PANTHER; PTHR46208:SF1; MITOCHONDRIAL IMPORT RECEPTOR SUBUNIT TOM70; 1. DR Pfam; PF00515; TPR_1; 1. DR Pfam; PF13181; TPR_8; 4. DR SMART; SM00028; TPR; 10. DR SUPFAM; SSF48452; TPR-like; 2. DR PROSITE; PS50005; TPR; 7. DR PROSITE; PS50293; TPR_REGION; 1. DR Genevisible; O94826; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Host-virus interaction; Isopeptide bond; KW Membrane; Methylation; Mitochondrion; Mitochondrion outer membrane; KW Phosphoprotein; Reference proteome; Repeat; TPR repeat; Transmembrane; KW Transmembrane helix; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, FT ECO:0007744|PubMed:25944712" FT CHAIN 2..608 FT /note="Mitochondrial import receptor subunit TOM70" FT /id="PRO_0000106336" FT TOPO_DOM 2..38 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000255" FT TRANSMEM 39..59 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 60..608 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REPEAT 114..147 FT /note="TPR 1" FT REPEAT 153..186 FT /note="TPR 2" FT REPEAT 294..327 FT /note="TPR 3" FT REPEAT 329..362 FT /note="TPR 4" FT REPEAT 367..400 FT /note="TPR 5" FT REPEAT 401..434 FT /note="TPR 6" FT REPEAT 440..475 FT /note="TPR 7" FT REPEAT 476..509 FT /note="TPR 8" FT REPEAT 511..544 FT /note="TPR 9" FT REPEAT 545..578 FT /note="TPR 10" FT REGION 67..107 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 67..86 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, FT ECO:0007744|PubMed:25944712" FT MOD_RES 71 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 91 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18088087, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 96 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 110 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 185 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 434 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 275 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT MUTAGEN 192 FT /note="R->A: Unable to induce IRF3 activation upon Sendai FT virus infection. Loss of interaction with HSPA8 and FT HSP90AA1. No effect on mitochondrial location." FT /evidence="ECO:0000269|PubMed:12526792, FT ECO:0000269|PubMed:20628368, ECO:0000269|PubMed:25609812" FT MUTAGEN 195 FT /note="K->A: No effect on interaction with HSP90AA1." FT /evidence="ECO:0000269|PubMed:25609812" FT HELIX 110..126 FT /evidence="ECO:0007829|PDB:7DHG" FT HELIX 130..143 FT /evidence="ECO:0007829|PDB:7DHG" FT HELIX 146..148 FT /evidence="ECO:0007829|PDB:7KDT" FT HELIX 149..165 FT /evidence="ECO:0007829|PDB:7DHG" FT HELIX 169..182 FT /evidence="ECO:0007829|PDB:7DHG" FT HELIX 187..199 FT /evidence="ECO:0007829|PDB:7DHG" FT HELIX 203..216 FT /evidence="ECO:0007829|PDB:7DHG" FT TURN 217..219 FT /evidence="ECO:0007829|PDB:7DHG" FT HELIX 222..245 FT /evidence="ECO:0007829|PDB:7DHG" FT HELIX 254..262 FT /evidence="ECO:0007829|PDB:7DHG" FT TURN 268..270 FT /evidence="ECO:0007829|PDB:7KDT" FT HELIX 298..306 FT /evidence="ECO:0007829|PDB:7DHG" FT HELIX 310..312 FT /evidence="ECO:0007829|PDB:7DHG" FT HELIX 313..323 FT /evidence="ECO:0007829|PDB:7DHG" FT HELIX 328..341 FT /evidence="ECO:0007829|PDB:7DHG" FT HELIX 345..357 FT /evidence="ECO:0007829|PDB:7DHG" FT STRAND 359..361 FT /evidence="ECO:0007829|PDB:7DHG" FT HELIX 363..379 FT /evidence="ECO:0007829|PDB:7DHG" FT HELIX 383..396 FT /evidence="ECO:0007829|PDB:7DHG" FT HELIX 401..413 FT /evidence="ECO:0007829|PDB:7DHG" FT HELIX 417..430 FT /evidence="ECO:0007829|PDB:7DHG" FT HELIX 435..452 FT /evidence="ECO:0007829|PDB:7DHG" FT HELIX 455..471 FT /evidence="ECO:0007829|PDB:7DHG" FT HELIX 476..488 FT /evidence="ECO:0007829|PDB:7DHG" FT HELIX 492..505 FT /evidence="ECO:0007829|PDB:7DHG" FT HELIX 510..522 FT /evidence="ECO:0007829|PDB:7DHG" FT HELIX 527..540 FT /evidence="ECO:0007829|PDB:7DHG" FT HELIX 545..558 FT /evidence="ECO:0007829|PDB:7DHG" FT HELIX 561..572 FT /evidence="ECO:0007829|PDB:7DHG" FT HELIX 578..598 FT /evidence="ECO:0007829|PDB:7DHG" SQ SEQUENCE 608 AA; 67455 MW; 5AAF5CAAA8582480 CRC64; MAASKPVEAA VVAAAVPSSG SGVGGGGTAG PGTGGLPRWQ LALAVGAPLL LGAGAIYLWS RQQRRREARG RGDASGLKRN SERKTPEGRA SPAPGSGHPE GPGAHLDMNS LDRAQAAKNK GNKYFKAGKY EQAIQCYTEA ISLCPTEKNV DLSTFYQNRA AAFEQLQKWK EVAQDCTKAV ELNPKYVKAL FRRAKAHEKL DNKKECLEDV TAVCILEGFQ NQQSMLLADK VLKLLGKEKA KEKYKNREPL MPSPQFIKSY FSSFTDDIIS QPMLKGEKSD EDKDKEGEAL EVKENSGYLK AKQYMEEENY DKIISECSKE IDAEGKYMAE ALLLRATFYL LIGNANAAKP DLDKVISLKE ANVKLRANAL IKRGSMYMQQ QQPLLSTQDF NMAADIDPQN ADVYHHRGQL KILLDQVEEA VADFDECIRL RPESALAQAQ KCFALYRQAY TGNNSSQIQA AMKGFEEVIK KFPRCAEGYA LYAQALTDQQ QFGKADEMYD KCIDLEPDNA TTYVHKGLLQ LQWKQDLDRG LELISKAIEI DNKCDFAYET MGTIEVQRGN MEKAIDMFNK AINLAKSEME MAHLYSLCDA AHAQTEVAKK YGLKPPTL //