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 24-JAN-2024, entry version 158. 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, 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). 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 3. DR IntAct; Q9QYA2; 3. DR MINT; Q9QYA2; -. DR STRING; 10090.ENSMUSP00000032555; -. DR GlyGen; Q9QYA2; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9QYA2; -. DR PhosphoSitePlus; Q9QYA2; -. DR SwissPalm; Q9QYA2; -. DR EPD; Q9QYA2; -. DR jPOST; Q9QYA2; -. DR MaxQB; Q9QYA2; -. DR PaxDb; 10090-ENSMUSP00000032555; -. DR PeptideAtlas; Q9QYA2; -. DR ProteomicsDB; 259152; -. DR Pumba; Q9QYA2; -. DR Antibodypedia; 3972; 194 antibodies from 35 providers. DR DNASU; 53333; -. DR Ensembl; ENSMUST00000032555.10; ENSMUSP00000032555.10; ENSMUSG00000002984.18. DR Ensembl; ENSMUST00000093552.12; ENSMUSP00000104090.5; ENSMUSG00000002984.18. DR GeneID; 53333; -. DR KEGG; mmu:53333; -. DR UCSC; uc009fna.2; mouse. DR AGR; MGI:1858259; -. 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; TRFNYRW; -. DR OrthoDB; 5489886at2759; -. DR PhylomeDB; Q9QYA2; -. DR TreeFam; TF106204; -. DR Reactome; R-MMU-5205685; PINK1-PRKN Mediated Mitophagy. DR BioGRID-ORCS; 53333; 25 hits in 77 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 252 other cell types or tissues. DR ExpressionAtlas; Q9QYA2; baseline and differential. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0016020; C: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:0031966; C:mitochondrial membrane; IDA: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:monoatomic 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; Porin; 1. DR InterPro; IPR023614; Porin_dom_sf. DR InterPro; IPR027246; Porin_Euk/Tom40. DR InterPro; IPR037930; Tom40. DR PANTHER; PTHR10802; MITOCHONDRIAL IMPORT RECEPTOR SUBUNIT TOM40; 1. DR PANTHER; PTHR10802:SF1; MITOCHONDRIAL IMPORT RECEPTOR SUBUNIT TOM40 HOMOLOG; 1. DR Pfam; PF01459; Porin_3; 1. DR Genevisible; Q9QYA2; MM. 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 //