TOM40_MOUSE
ID TOM40_MOUSE Reviewed; 361 AA.
AC Q9QYA2; Q3TBZ2; Q3TQA1; Q8VI26; Q8VI27; Q9Z2N1;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Mitochondrial import receptor subunit TOM40 homolog;
DE AltName: Full=Mitochondrial outer membrane protein of 35 kDa;
DE Short=MOM35;
DE AltName: Full=Protein Haymaker;
DE AltName: Full=Translocase of outer membrane 40 kDa subunit homolog;
GN Name=Tomm40; Synonyms=Mom35, Tom40;
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 [MRNA].
RX PubMed=11768756; DOI=10.1023/a:1005524815130;
RA Lee Rivera I., Shore G.C., Schleiff E.;
RT "Cloning and characterization of a 35-kDa mouse mitochondrial outer
RT membrane protein MOM35 with high homology to Tom40.";
RL J. Bioenerg. Biomembr. 32:111-121(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mastocytoma;
RX PubMed=11745481; DOI=10.1002/ijc.1555;
RA Das B., Tao S.-Z., Mushnitsky R., Norin A.J.;
RT "Genetic identity and differential expression of p38.5 (Haymaker) in human
RT malignant and non-malignant cells.";
RL Int. J. Cancer 94:800-806(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yoshiura K., Murray J.C.;
RT "A transcriptional map in the region of 19q13 derived using direct
RT sequencing and exon trapping.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Corpus striatum, Dendritic cell, Lung, and Macrophage;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [6]
RP PROTEIN SEQUENCE OF 185-195; 316-330 AND 352-361, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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).
CC -!- FUNCTION: Channel-forming protein essential for import of protein
CC precursors into mitochondria. Plays a role in the assembly of the
CC mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I)
CC by forming a complex with BCAP31 and mediating the translocation of
CC Complex I components from the cytosol to the mitochondria.
CC {ECO:0000250|UniProtKB:O96008}.
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 mitochondrial targeting sequences. Interacts
CC with TIMM29; linking the TIM22 complex to the TOM complex. Forms a
CC complex with BCAP31 (via C-terminus) which mediates the translocation
CC of components of the mitochondrial membrane respiratory chain NADH
CC dehydrogenase (Complex I) from the cytosol to the mitochondria (By
CC similarity). Interacts (via N-terminus) with CYP1A1 (via mitochondrial
CC targeting signal); this interaction is required for CYP1A1
CC translocation across the mitochondrial outer membrane (By similarity).
CC {ECO:0000250|UniProtKB:O96008, ECO:0000250|UniProtKB:Q75Q40}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:O96008}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Associates with the mitochondria-associated ER
CC membrane via interaction with BCAP31. {ECO:0000250|UniProtKB:O96008}.
CC -!- SIMILARITY: Belongs to the Tom40 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC82341.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF109918; AAF21906.1; -; mRNA.
DR EMBL; AF316403; AAL46628.1; -; mRNA.
DR EMBL; AF316404; AAL46629.1; -; mRNA.
DR EMBL; AF043249; AAC82341.1; ALT_FRAME; mRNA.
DR EMBL; AK150019; BAE29244.1; -; mRNA.
DR EMBL; AK163759; BAE37483.1; -; mRNA.
DR EMBL; AK164570; BAE37837.1; -; mRNA.
DR EMBL; AK165173; BAE38058.1; -; mRNA.
DR EMBL; AK170991; BAE42165.1; -; mRNA.
DR EMBL; BC100452; AAI00453.1; -; mRNA.
DR CCDS; CCDS52062.1; -.
DR RefSeq; NP_001103218.1; NM_001109748.1.
DR RefSeq; NP_058567.2; NM_016871.2.
DR AlphaFoldDB; Q9QYA2; -.
DR SMR; Q9QYA2; -.
DR BioGRID; 207293; 2.
DR IntAct; Q9QYA2; 3.
DR MINT; Q9QYA2; -.
DR STRING; 10090.ENSMUSP00000032555; -.
DR iPTMnet; Q9QYA2; -.
DR PhosphoSitePlus; Q9QYA2; -.
DR SwissPalm; Q9QYA2; -.
DR EPD; Q9QYA2; -.
DR jPOST; Q9QYA2; -.
DR MaxQB; Q9QYA2; -.
DR PaxDb; Q9QYA2; -.
DR PeptideAtlas; Q9QYA2; -.
DR PRIDE; Q9QYA2; -.
DR ProteomicsDB; 259152; -.
DR Antibodypedia; 3972; 160 antibodies from 35 providers.
DR DNASU; 53333; -.
DR Ensembl; ENSMUST00000032555; ENSMUSP00000032555; ENSMUSG00000002984.
DR Ensembl; ENSMUST00000093552; ENSMUSP00000104090; ENSMUSG00000002984.
DR GeneID; 53333; -.
DR KEGG; mmu:53333; -.
DR UCSC; uc009fna.2; mouse.
DR CTD; 10452; -.
DR MGI; MGI:1858259; Tomm40.
DR VEuPathDB; HostDB:ENSMUSG00000002984; -.
DR eggNOG; KOG3296; Eukaryota.
DR GeneTree; ENSGT00390000003308; -.
DR HOGENOM; CLU_054399_0_0_1; -.
DR InParanoid; Q9QYA2; -.
DR OMA; SHQFAMG; -.
DR OrthoDB; 1346842at2759; -.
DR PhylomeDB; Q9QYA2; -.
DR TreeFam; TF106204; -.
DR Reactome; R-MMU-5205685; PINK1-PRKN Mediated Mitophagy.
DR BioGRID-ORCS; 53333; 25 hits in 72 CRISPR screens.
DR ChiTaRS; Tomm40; mouse.
DR PRO; PR:Q9QYA2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9QYA2; protein.
DR Bgee; ENSMUSG00000002984; Expressed in yolk sac and 248 other tissues.
DR ExpressionAtlas; Q9QYA2; baseline and differential.
DR Genevisible; Q9QYA2; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0032592; C:integral component of mitochondrial membrane; IDA:MGI.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:MGI.
DR GO; GO:0005742; C:mitochondrial outer membrane translocase complex; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0005261; F:cation channel activity; ISO:MGI.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0070678; F:preprotein binding; ISO:MGI.
DR GO; GO:0008320; F:protein transmembrane transporter activity; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0051204; P:protein insertion into mitochondrial membrane; ISO:MGI.
DR GO; GO:0006626; P:protein targeting to mitochondrion; ISS:UniProtKB.
DR CDD; cd07305; Porin3_Tom40; 1.
DR Gene3D; 2.40.160.10; -; 1.
DR InterPro; IPR023614; Porin_dom_sf.
DR InterPro; IPR027246; Porin_Euk/Tom40.
DR InterPro; IPR037930; Tom40.
DR PANTHER; PTHR10802; PTHR10802; 1.
DR Pfam; PF01459; Porin_3; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Porin; Protein transport; Reference proteome;
KW Transmembrane; Transmembrane beta strand; Transport.
FT CHAIN 1..361
FT /note="Mitochondrial import receptor subunit TOM40 homolog"
FT /id="PRO_0000051524"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..37
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 1..78
FT /note="MGNVLAASSPPAGPPPPPTPSLVGLPPPPPSPPGFTLPPLGGGLGTGSSTGR
FT GSERTPGAAASGAAAASEDGSCGCLP -> MMKSGDWVKHWPWFGTDSRGCGQRRCGGL
FT GRWELRMPA (in Ref. 1; AAF21906)"
FT /evidence="ECO:0000305"
FT CONFLICT 13..14
FT /note="GP -> R (in Ref. 3; AAC82341)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="E -> D (in Ref. 4; BAE42165)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="E -> G (in Ref. 3; AAL46628)"
FT /evidence="ECO:0000305"
FT CONFLICT 185..234
FT /note="Missing (in Ref. 3; AAC82341)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 37895 MW; 8415114963EBAB9B CRC64;
MGNVLAASSP PAGPPPPPTP SLVGLPPPPP SPPGFTLPPL GGGLGTGSST GRGSERTPGA
AASGAAAASE DGSCGCLPNP GTFEECHRKC KELFPVQMEG VKLTVNKGLS NRFQVTHTVA
LGTIGESNYH FGVTYVGTKQ LSPTEAFPVL VGDMDNSGSL NAQVIHQLSP GLRSKMAIQT
QQSKFVNWQV DGEYRGSDFT AAVTLGNPDV LVGSGILVAH YLQSITPCLA LGGELVYHRR
PGEEGTVMSL AGKYTLNNWL ATVTLGQAGM HATYYHKASD QLQVGVEFEA STRMQDTSAS
FGYQLDLPKA NFLFKGSVNS NWIVGATLEK KLPPLPLTLS LCAFLNHRKN KFLCGFGLTI
G
