TOM70_MOUSE
ID TOM70_MOUSE Reviewed; 611 AA.
AC Q9CZW5; Q8BNI6;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 174.
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:0000250|UniProtKB:O94826};
GN Name=Tomm70 {ECO:0000312|MGI:MGI:106295}; Synonyms=D16Wsu109e, Tomm70a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP PROTEIN SEQUENCE OF 163-171; 330-357; 451-466 AND 520-527, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP INTERACTION WITH CAPN8, AND TISSUE SPECIFICITY.
RX PubMed=16476741; DOI=10.1074/jbc.m509244200;
RA Hata S., Koyama S., Kawahara H., Doi N., Maeda T., Toyama-Sorimachi N.,
RA Abe K., Suzuki K., Sorimachi H.;
RT "Stomach-specific calpain, nCL-2, localizes in mucus cells and proteolyzes
RT the beta-subunit of coatomer complex, beta-COP.";
RL J. Biol. Chem. 281:11214-11224(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT MS/MS/MS.";
RL Mol. Cell. Proteomics 6:669-676(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94; SER-99 AND SER-108, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP FUNCTION.
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).
CC -!- FUNCTION: Acts as receptor of the preprotein translocase complex of the
CC outer mitochondrial membrane (TOM complex). Recognizes and mediates the
CC translocation of mitochondrial preproteins from the cytosol into the
CC mitochondria in a chaperone dependent manner (By similarity). Mediates
CC TBK1 and IRF3 activation induced by MAVS in response to virus infection
CC and promotes host antiviral responses during virus infection
CC (PubMed:20628368). {ECO:0000250|UniProtKB:O94826,
CC ECO:0000250|UniProtKB:Q75Q39, ECO:0000269|PubMed:20628368}.
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) (By similarity). Interacts with CAPN8 (PubMed:16476741).
CC Interacts with TRADD, TRAF6 and STING. Interacts with MAVS. Interacts
CC with HSPA8 and HSP90AA1; both interactions are required for preprotein
CC mitochondrial import. The interaction with HSP90AA1 is direct and
CC mediates the association of TOMM70 with IRF3 and TBK1 (By similarity).
CC {ECO:0000250|UniProtKB:O94826, ECO:0000269|PubMed:16476741}.
CC -!- INTERACTION:
CC Q9CZW5; Q8K443: Rgs13; NbExp=12; IntAct=EBI-642469, EBI-645999;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:O94826}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the base region of the oxyntic and
CC pyloric mucosae. {ECO:0000269|PubMed:16476741}.
CC -!- SIMILARITY: Belongs to the Tom70 family. {ECO:0000305}.
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DR EMBL; AK012084; BAB28018.1; -; mRNA.
DR EMBL; AK083586; BAC38960.1; -; mRNA.
DR EMBL; AK145458; BAE26448.1; -; mRNA.
DR EMBL; AK150429; BAE29552.1; -; mRNA.
DR EMBL; BC057096; AAH57096.1; -; mRNA.
DR EMBL; BC139420; AAI39421.1; -; mRNA.
DR EMBL; BC139421; AAI39422.1; -; mRNA.
DR CCDS; CCDS28227.1; -.
DR RefSeq; NP_613065.2; NM_138599.5.
DR AlphaFoldDB; Q9CZW5; -.
DR SMR; Q9CZW5; -.
DR BioGRID; 205817; 23.
DR IntAct; Q9CZW5; 3.
DR MINT; Q9CZW5; -.
DR STRING; 10090.ENSMUSP00000129186; -.
DR iPTMnet; Q9CZW5; -.
DR PhosphoSitePlus; Q9CZW5; -.
DR SwissPalm; Q9CZW5; -.
DR EPD; Q9CZW5; -.
DR jPOST; Q9CZW5; -.
DR MaxQB; Q9CZW5; -.
DR PaxDb; Q9CZW5; -.
DR PRIDE; Q9CZW5; -.
DR ProteomicsDB; 260651; -.
DR Antibodypedia; 3025; 241 antibodies from 29 providers.
DR DNASU; 28185; -.
DR Ensembl; ENSMUST00000166897; ENSMUSP00000129186; ENSMUSG00000022752.
DR GeneID; 28185; -.
DR KEGG; mmu:28185; -.
DR UCSC; uc007zmz.1; mouse.
DR CTD; 28185; -.
DR MGI; MGI:106295; Tomm70a.
DR VEuPathDB; HostDB:ENSMUSG00000022752; -.
DR eggNOG; KOG0547; Eukaryota.
DR GeneTree; ENSGT00940000157095; -.
DR HOGENOM; CLU_017516_2_0_1; -.
DR InParanoid; Q9CZW5; -.
DR OMA; HEATKDM; -.
DR OrthoDB; 303136at2759; -.
DR PhylomeDB; Q9CZW5; -.
DR TreeFam; TF106203; -.
DR Reactome; R-MMU-168928; DDX58/IFIH1-mediated induction of interferon-alpha/beta.
DR Reactome; R-MMU-5205685; PINK1-PRKN Mediated Mitophagy.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR BioGRID-ORCS; 28185; 27 hits in 72 CRISPR screens.
DR ChiTaRS; Tomm70a; mouse.
DR PRO; PR:Q9CZW5; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9CZW5; protein.
DR Bgee; ENSMUSG00000022752; Expressed in caudate-putamen and 268 other tissues.
DR Genevisible; Q9CZW5; MM.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0005742; C:mitochondrial outer membrane translocase complex; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0030943; F:mitochondrion targeting sequence binding; IBA:GO_Central.
DR GO; GO:0002218; P:activation of innate immune response; ISS:UniProtKB.
DR GO; GO:0098586; P:cellular response to virus; ISS:UniProtKB.
DR GO; GO:0061052; P:negative regulation of cell growth involved in cardiac muscle cell development; ISO:MGI.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; ISS:UniProtKB.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; ISS:UniProtKB.
DR GO; GO:1904591; P:positive regulation of protein import; ISO:MGI.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0006626; P:protein targeting to mitochondrion; ISO:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0097068; P:response to thyroxine; IEA:Ensembl.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00515; TPR_1; 1.
DR Pfam; PF13174; TPR_6; 1.
DR Pfam; PF13181; TPR_8; 3.
DR SMART; SM00028; TPR; 10.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 7.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Isopeptide bond; Membrane;
KW Methylation; Mitochondrion; Mitochondrion outer membrane; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O94826"
FT CHAIN 2..611
FT /note="Mitochondrial import receptor subunit TOM70"
FT /id="PRO_0000106337"
FT TOPO_DOM 2..41
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..611
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 117..150
FT /note="TPR 1"
FT REPEAT 156..189
FT /note="TPR 2"
FT REPEAT 297..330
FT /note="TPR 3"
FT REPEAT 332..365
FT /note="TPR 4"
FT REPEAT 370..403
FT /note="TPR 5"
FT REPEAT 404..437
FT /note="TPR 6"
FT REPEAT 445..478
FT /note="TPR 7"
FT REPEAT 479..512
FT /note="TPR 8"
FT REPEAT 514..547
FT /note="TPR 9"
FT REPEAT 548..581
FT /note="TPR 10"
FT REGION 69..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O94826"
FT MOD_RES 74
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O94826"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17208939,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q75Q39"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94826"
FT MOD_RES 188
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O94826"
FT CROSSLNK 278
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O94826"
FT CONFLICT 116
FT /note="R -> S (in Ref. 1; BAB28018)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 611 AA; 67590 MW; 5103C658D8BF9C53 CRC64;
MAASKPIEAA MAAAAAPGSG NGVGGGGGTA GPGSGAGTLP RWHVALAIGA PLLLGAGAMY
LWSRRRRRRE AGGRGDASGL KRNSERKTPE GRASPALGSG HHDGSGDSLE MSSLDRAQAA
KNKGNKYFKA GKYEQAIQCY TEAISLCPTE KNVDLSTFYQ NRAAAFEQLQ KWKEVAQDCT
KAVELNPKYV KALFRRAKAH EKLDNKKECL EDVTAVCILE GFQNEQSMLL ADKVLKLLGK
ENAKEKYKNR EPLMPSPQFI KSYFSSFTDD IISQPMLKGE KSDEDKDKEG EALEVKENSG
YLKAKQYMEE ENYDKIISEC SKEIDAQGKY MAEALLLRAT FYLLIGSANA AKPDLDKVIS
LKEANVKLRA NALIKRGTMC MQQQQPMLST QDFNMAAEID PMNSDVYHHR GQLKILLDLV
EEAVADFDAC IRLRPKFALA QAQKCFALYR QAYTANNSSQ VQAAMKGFEE IIKKFPRCAE
GYALYAQALT DQQQFGKADE MYDKCIDLEP DNATTYVHKG LLQLQWKQDL DKGLELISKA
IEIDNKCDFA YETMGTIEVQ RGNMEKAIDM FNKAINLAKS EMEMAHLYSL CDAAHAQTEV
AKKYGLKPPT L
