TOM20_MOUSE
ID TOM20_MOUSE Reviewed; 145 AA.
AC Q9DCC8;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Mitochondrial import receptor subunit TOM20 homolog;
DE AltName: Full=Mitochondrial 20 kDa outer membrane protein;
DE AltName: Full=Outer mitochondrial membrane receptor Tom20;
GN Name=Tomm20;
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=Kidney;
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=FVB/N; TISSUE=Mammary tumor;
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 126-132, AND 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 TISSUE SPECIFICITY.
RX PubMed=19492028; DOI=10.1267/ahc.08012;
RA Miyoshi K., Akazawa Y., Horiguchi T., Noma T.;
RT "Localization of adenylate kinase 4 in mouse tissues.";
RL Acta Histochem. Cytochem. 42:55-64(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135 AND SER-138, 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 [6]
RP INTERACTION WITH TBC1D21, AND TISSUE SPECIFICITY.
RX PubMed=32976492; DOI=10.1371/journal.pgen.1009020;
RA Wang Y.Y., Ke C.C., Chen Y.L., Lin Y.H., Yu I.S., Ku W.C., O'Bryan M.K.,
RA Lin Y.H.;
RT "Deficiency of the Tbc1d21 gene causes male infertility with morphological
RT abnormalities of the sperm mitochondria and flagellum in mice.";
RL PLoS Genet. 16:e1009020-e1009020(2020).
CC -!- FUNCTION: Central component of the receptor complex responsible for the
CC recognition and translocation of cytosolically synthesized
CC mitochondrial preproteins. Together with TOM22 functions as the transit
CC peptide receptor at the surface of the mitochondrion outer membrane and
CC facilitates the movement of preproteins into the TOM40 translocation
CC pore (By similarity). Required for the translocation across the
CC mitochondrial outer membrane of cytochrome P450 monooxygenases.
CC {ECO:0000250, ECO:0000250|UniProtKB:Q62760}.
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). Interacts with TOM22. Interacts with APEX1 (By similarity).
CC Interacts with TBC1D21 (PubMed:32976492).
CC {ECO:0000250|UniProtKB:Q15388, ECO:0000269|PubMed:32976492}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q15388}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, kidney, stomach, colon,
CC jejunum, ileum, testis, ovary and oviduct (at protein level)
CC (PubMed:19492028). In the brain, expressed in neural cells of the
CC cerebrum and cerebellum (at protein level) (PubMed:19492028). In the
CC kidney, expressed in the proximal to distal tubule in the cortex and
CC the outer and inner zones of the medulla (at protein level)
CC (PubMed:19492028). In the stomach, expressed in the basal layer of
CC stratified squamous epithelia in the forestomach and in the gastric pit
CC and fundic gland of the glandular stomach (at protein level)
CC (PubMed:19492028). Expressed in epithelial cells of the jejunum, ileum,
CC and colon (at protein level) (PubMed:19492028). In the testis,
CC expressed by spermatocytes and spermatogonia (at protein level)
CC (PubMed:19492028). In the ovaries, expressed by follicular epithelial
CC cells and corpus luteum cells (at protein level) (PubMed:19492028). In
CC the oviduct, expressed in the epithelia of the isthmus and the ciliated
CC cells of the ampulla (at protein level) (PubMed:19492028). Expressed in
CC the sperm midpiece (at protein level) (PubMed:19492028,
CC PubMed:32976492). {ECO:0000269|PubMed:19492028,
CC ECO:0000269|PubMed:32976492}.
CC -!- PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation
CC and enhancement of mitophagy. Deubiquitinated by USP30.
CC {ECO:0000250|UniProtKB:Q15388}.
CC -!- SIMILARITY: Belongs to the Tom20 family. {ECO:0000305}.
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DR EMBL; AK002902; BAB22444.1; -; mRNA.
DR EMBL; BC002087; AAH02087.1; -; mRNA.
DR CCDS; CCDS22786.1; -.
DR RefSeq; NP_077176.1; NM_024214.2.
DR AlphaFoldDB; Q9DCC8; -.
DR BMRB; Q9DCC8; -.
DR SMR; Q9DCC8; -.
DR BioGRID; 212562; 5.
DR DIP; DIP-60017N; -.
DR IntAct; Q9DCC8; 2.
DR MINT; Q9DCC8; -.
DR STRING; 10090.ENSMUSP00000136493; -.
DR iPTMnet; Q9DCC8; -.
DR PhosphoSitePlus; Q9DCC8; -.
DR EPD; Q9DCC8; -.
DR jPOST; Q9DCC8; -.
DR MaxQB; Q9DCC8; -.
DR PaxDb; Q9DCC8; -.
DR PRIDE; Q9DCC8; -.
DR ProteomicsDB; 260648; -.
DR Antibodypedia; 2619; 234 antibodies from 34 providers.
DR DNASU; 67952; -.
DR Ensembl; ENSMUST00000179857; ENSMUSP00000136493; ENSMUSG00000093904.
DR GeneID; 67952; -.
DR KEGG; mmu:67952; -.
DR UCSC; uc009nza.2; mouse.
DR CTD; 9804; -.
DR MGI; MGI:1915202; Tomm20.
DR VEuPathDB; HostDB:ENSMUSG00000093904; -.
DR eggNOG; KOG4056; Eukaryota.
DR GeneTree; ENSGT00390000011698; -.
DR HOGENOM; CLU_100000_0_0_1; -.
DR InParanoid; Q9DCC8; -.
DR OMA; VGYCFYF; -.
DR OrthoDB; 1316067at2759; -.
DR PhylomeDB; Q9DCC8; -.
DR TreeFam; TF106200; -.
DR Reactome; R-MMU-5205685; PINK1-PRKN Mediated Mitophagy.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR BioGRID-ORCS; 67952; 9 hits in 51 CRISPR screens.
DR ChiTaRS; Tomm20; mouse.
DR PRO; PR:Q9DCC8; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9DCC8; protein.
DR Bgee; ENSMUSG00000093904; Expressed in yolk sac and 254 other tissues.
DR ExpressionAtlas; Q9DCC8; baseline and differential.
DR Genevisible; Q9DCC8; MM.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0005740; C:mitochondrial envelope; IDA:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0005742; C:mitochondrial outer membrane translocase complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0097225; C:sperm midpiece; IDA:UniProtKB.
DR GO; GO:0030943; F:mitochondrion targeting sequence binding; ISO:MGI.
DR GO; GO:0015450; F:protein-transporting ATPase activity; ISS:HGNC-UCL.
DR GO; GO:0051082; F:unfolded protein binding; ISS:HGNC-UCL.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0006626; P:protein targeting to mitochondrion; ISS:UniProtKB.
DR GO; GO:1905242; P:response to 3,3',5-triiodo-L-thyronine; IEA:Ensembl.
DR GO; GO:0014850; P:response to muscle activity; IEA:Ensembl.
DR GO; GO:0016031; P:tRNA import into mitochondrion; IBA:GO_Central.
DR Gene3D; 1.20.960.10; -; 1.
DR InterPro; IPR002056; MAS20.
DR InterPro; IPR022422; MAS20_rcpt_metazoan.
DR InterPro; IPR023392; Tom20_dom_sf.
DR PANTHER; PTHR12430; PTHR12430; 1.
DR Pfam; PF02064; MAS20; 1.
DR PIRSF; PIRSF037707; MAS20_rcpt; 1.
DR PRINTS; PR01989; EUOM20RECPTR.
DR PRINTS; PR00351; OM20RECEPTOR.
DR SUPFAM; SSF47157; SSF47157; 1.
DR TIGRFAMs; TIGR00985; 3a0801s04tom; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Isopeptide bond; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation.
FT CHAIN 1..145
FT /note="Mitochondrial import receptor subunit TOM20 homolog"
FT /id="PRO_0000051539"
FT TOPO_DOM 1..6
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 35
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q15388"
FT CROSSLNK 56
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q15388"
FT CROSSLNK 61
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q15388"
FT CROSSLNK 68
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q15388"
SQ SEQUENCE 145 AA; 16284 MW; 50E3BD25AD5C9B3B CRC64;
MVGRNSAIAA GVCGALFIGY CIYFDRKRRS DPNFKNRLRE RRKKQKLAKE RAGLSKLPDL
KDAEAVQKFF LEEIQLGEEL LAQGDYEKGV DHLTNAIAVC GQPQQLLQVL QQTLPPPVFQ
MLLTKLPTIS QRIVSAQSLA EDDVE
