TOM70_RAT
ID TOM70_RAT Reviewed; 610 AA.
AC Q75Q39;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
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|RGD:1303049};
GN Name=Tomm70 {ECO:0000312|RGD:1303049}; Synonyms=Tomm70a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11956321; DOI=10.1242/jcs.115.9.1895;
RA Suzuki H., Maeda M., Mihara K.;
RT "Characterization of rat TOM70 as a receptor of the preprotein translocase
RT of the mitochondrial outer membrane.";
RL J. Cell Sci. 115:1895-1905(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 338-356, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16396499; DOI=10.1021/pr0503073;
RA Moser K., White F.M.;
RT "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-
RT MS/MS.";
RL J. Proteome Res. 5:98-104(2006).
RN [5]
RP FUNCTION.
RX PubMed=19401463; DOI=10.1074/jbc.m109.007492;
RA Anandatheerthavarada H.K., Sepuri N.B., Avadhani N.G.;
RT "Mitochondrial targeting of cytochrome P450 proteins containing NH2-
RT terminal chimeric signals involves an unusual TOM20/TOM22 bypass
RT mechanism.";
RL J. Biol. Chem. 284:17352-17363(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94 AND SER-104, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (PubMed:11956321,
CC PubMed:19401463). Mediates TBK1 and IRF3 activation induced by MAVS in
CC response to Sendai virus infection and promotes host antiviral
CC responses during virus infection (By similarity).
CC {ECO:0000250|UniProtKB:O94826, ECO:0000269|PubMed:11956321,
CC ECO:0000269|PubMed:19401463}.
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 (By similarity).
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:0000250|UniProtKB:Q9CZW5}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:11956321}; Single-pass membrane protein
CC {ECO:0000269|PubMed:11956321}.
CC -!- SIMILARITY: Belongs to the Tom70 family. {ECO:0000305}.
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DR EMBL; AB162856; BAD11366.1; -; mRNA.
DR EMBL; BC098640; AAH98640.1; -; mRNA.
DR RefSeq; NP_997684.1; NM_212519.2.
DR AlphaFoldDB; Q75Q39; -.
DR SMR; Q75Q39; -.
DR BioGRID; 257743; 4.
DR CORUM; Q75Q39; -.
DR IntAct; Q75Q39; 1.
DR MINT; Q75Q39; -.
DR STRING; 10116.ENSRNOP00000002238; -.
DR iPTMnet; Q75Q39; -.
DR PhosphoSitePlus; Q75Q39; -.
DR jPOST; Q75Q39; -.
DR PaxDb; Q75Q39; -.
DR PRIDE; Q75Q39; -.
DR Ensembl; ENSRNOT00000002238; ENSRNOP00000002238; ENSRNOG00000001640.
DR GeneID; 304017; -.
DR KEGG; rno:304017; -.
DR UCSC; RGD:1303049; rat.
DR CTD; 9868; -.
DR RGD; 1303049; Tomm70.
DR eggNOG; KOG0547; Eukaryota.
DR InParanoid; Q75Q39; -.
DR OrthoDB; 303136at2759; -.
DR PhylomeDB; Q75Q39; -.
DR TreeFam; TF106203; -.
DR Reactome; R-RNO-168928; DDX58/IFIH1-mediated induction of interferon-alpha/beta.
DR Reactome; R-RNO-5205685; PINK1-PRKN Mediated Mitophagy.
DR Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR PRO; PR:Q75Q39; -.
DR Proteomes; UP000002494; Chromosome 11.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:RGD.
DR GO; GO:0005742; C:mitochondrial outer membrane translocase complex; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
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; IMP:RGD.
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; IMP:RGD.
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; IMP:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0097068; P:response to thyroxine; IEP:RGD.
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; 2.
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..610
FT /note="Mitochondrial import receptor subunit TOM70"
FT /id="PRO_0000288526"
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..610
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 116..149
FT /note="TPR 1"
FT REPEAT 155..188
FT /note="TPR 2"
FT REPEAT 296..329
FT /note="TPR 3"
FT REPEAT 331..364
FT /note="TPR 4"
FT REPEAT 369..402
FT /note="TPR 5"
FT REPEAT 403..436
FT /note="TPR 6"
FT REPEAT 444..477
FT /note="TPR 7"
FT REPEAT 478..511
FT /note="TPR 8"
FT REPEAT 513..546
FT /note="TPR 9"
FT REPEAT 547..580
FT /note="TPR 10"
FT REGION 69..109
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:16396499,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94826"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZW5"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94826"
FT MOD_RES 187
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O94826"
FT CROSSLNK 277
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O94826"
SQ SEQUENCE 610 AA; 67445 MW; BE9E4277FE87F6EF CRC64;
MAASKPVEAA MAAAAAPASG NGVGSSGGTA APGSGAGTLP RWHVALAIGA PLLLGAGAMY
LWSRRRRRRE AGGRGDASGL KRNSERKTPE GRASPALGSG PDGSGDSLEM SSLDRAQAAK
NKGNKYFKAG KYEQAIQCYT EAISLCPTEK NADLSTFYQN RAAAFEQLQK WKEVAQDCTK
AVELNPKYVK ALFRRAKAHE KLDNKKECLE DVTAVCILEG FQNEQSMLLA DKVLKLLGKE
NAKEKYKNRE PLMPSPQFIK SYFSSFTDDI ISQPMLKGEK SDEDKDKEGE ALEVKENSGY
LKAKQYMEEE NYDKIISECS KEIDAQGKYM AEALLLRATF YLLIGSANAA KPDLDKVISL
KEANVKLRAN ALIKRGTMCM QQQQPMLSTQ DFNMAAEIDP MNSDVYHHRG QLKILLDLVE
EAVADFDACI RLRPKFALAQ AQKCFALYRQ AYTANNSSQV QAAMKGFEEV IKKFPRCAEG
YALYAQALTD QQQFGKADEM YDKCIDLEPD NATTYVHKGL LQLQWKQDLD KGLELISKAI
EIDNKCDFAY ETMGTIEVQR GNMEKAIDMF NKAINLAKSE MEMAHLYSLC DAAHAQTEVA
KKYGLKPPTL
