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};
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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; 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 Genevisible; O94826; HS.
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
//
