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   29-MAY-2024, entry version 203.
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};
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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; 136.
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   ABCD; O94826; 1 sequenced antibody.
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.
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
//