ID MTCH2_MOUSE Reviewed; 303 AA. AC Q791V5; Q3TPS5; Q99LZ6; Q9D060; Q9D7Y2; Q9QZP3; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 24-JAN-2024, entry version 132. DE RecName: Full=Mitochondrial carrier homolog 2; DE AltName: Full=Met-induced mitochondrial protein {ECO:0000303|PubMed:12407445}; GN Name=Mtch2 {ECO:0000312|MGI:MGI:1929260}; GN Synonyms=Mimp {ECO:0000303|PubMed:12407445}; 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]. RA Jang J.S., Hahn Y., Park C., Chung J.H.; RT "Identification of an evolutionary conserved mitochondrial carrier family RT from various organisms."; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RC TISSUE=Heart, Hippocampus, Small intestine, Stomach, Testis, and RC Tongue; 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 [3] 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 [4] RP PROTEIN SEQUENCE OF 69-77; 91-119 AND 172-185, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC STRAIN=C57BL/6J; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [5] RP TISSUE SPECIFICITY. RX PubMed=12407445; DOI=10.1038/sj.neo.7900272; RA Yerushalmi G.M., Leibowitz-Amit R., Shaharabany M., Tsarfaty I.; RT "Met-HGF/SF signal transduction induces mimp, a novel mitochondrial carrier RT homologue, which leads to mitochondrial depolarization."; RL Neoplasia 4:510-522(2002). RN [6] RP SUBUNIT, SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH P15 BID. RX PubMed=15899861; DOI=10.1128/mcb.25.11.4579-4590.2005; RA Grinberg M., Schwarz M., Zaltsman Y., Eini T., Niv H., Pietrokovski S., RA Gross A.; RT "Mitochondrial carrier homolog 2 is a target of tBID in cells signaled to RT die by tumor necrosis factor alpha."; RL Mol. Cell. Biol. 25:4579-4590(2005). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, 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 [8] RP SUBCELLULAR LOCATION, FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH RP P15 BID. RX PubMed=20436477; DOI=10.1038/ncb2057; RA Zaltsman Y., Shachnai L., Yivgi-Ohana N., Schwarz M., Maryanovich M., RA Houtkooper R.H., Vaz F.M., De Leonardis F., Fiermonte G., Palmieri F., RA Gillissen B., Daniel P.T., Jimenez E., Walsh S., Koehler C.M., Roy S.S., RA Walter L., Hajnoczky G., Gross A.; RT "MTCH2/MIMP is a major facilitator of tBID recruitment to mitochondria."; RL Nat. Cell Biol. 12:553-562(2010). RN [9] RP FUNCTION. RX PubMed=26219591; DOI=10.1038/ncomms8901; RA Maryanovich M., Zaltsman Y., Ruggiero A., Goldman A., Shachnai L., RA Zaidman S.L., Porat Z., Golan K., Lapidot T., Gross A.; RT "An MTCH2 pathway repressing mitochondria metabolism regulates RT haematopoietic stem cell fate."; RL Nat. Commun. 6:7901-7901(2015). RN [10] RP DISRUPTION PHENOTYPE, FUNCTION, AND CONDITIONAL KNOCKOUT IN MUSCLE CELLS. RX PubMed=26876167; DOI=10.1016/j.celrep.2016.01.046; RA Buzaglo-Azriel L., Kuperman Y., Tsoory M., Zaltsman Y., Shachnai L., RA Zaidman S.L., Bassat E., Michailovici I., Sarver A., Tzahor E., Haran M., RA Vernochet C., Gross A.; RT "Loss of Muscle MTCH2 Increases Whole-Body Energy Utilization and Protects RT from Diet-Induced Obesity."; RL Cell Rep. 14:1602-1610(2016). RN [11] RP FUNCTION. RX PubMed=28127879; DOI=10.1002/oby.21751; RA Rottiers V., Francisco A., Platov M., Zaltsman Y., Ruggiero A., Lee S.S., RA Gross A., Libert S.; RT "MTCH2 is a conserved regulator of lipid homeostasis."; RL Obesity 25:616-625(2017). RN [12] RP FUNCTION. RX PubMed=30510213; DOI=10.1038/s41467-018-07519-w; RA Bahat A., Goldman A., Zaltsman Y., Khan D.H., Halperin C., Amzallag E., RA Krupalnik V., Mullokandov M., Silberman A., Erez A., Schimmer A.D., RA Hanna J.H., Gross A.; RT "MTCH2-mediated mitochondrial fusion drives exit from naive pluripotency in RT embryonic stem cells."; RL Nat. Commun. 9:5132-5132(2018). CC -!- FUNCTION: Protein insertase that mediates insertion of transmembrane CC proteins into the mitochondrial outer membrane. Catalyzes insertion of CC proteins with alpha-helical transmembrane regions, such as signal- CC anchored, tail-anchored and multi-pass membrane proteins. Does not CC mediate insertion of beta-barrel transmembrane proteins (By CC similarity). Also acts as a receptor for the truncated form of pro- CC apoptotic BH3-interacting domain death agonist (p15 BID) and has CC therefore a critical function in apoptosis (PubMed:20436477, CC PubMed:26219591, PubMed:26876167, PubMed:30510213). Regulates the CC quiescence/cycling of hematopoietic stem cells (HSCs) (PubMed:20436477, CC PubMed:26219591, PubMed:26876167). Acts as a regulator of mitochondrial CC fusion, essential for the naive-to-primed interconversion of embryonic CC stem cells (ESCs) (PubMed:30510213). Acts as a regulator of lipid CC homeostasis and has a regulatory role in adipocyte differentiation and CC biology (PubMed:26876167, PubMed:28127879). CC {ECO:0000250|UniProtKB:Q9Y6C9, ECO:0000269|PubMed:20436477, CC ECO:0000269|PubMed:26219591, ECO:0000269|PubMed:26876167, CC ECO:0000269|PubMed:28127879, ECO:0000269|PubMed:30510213}. CC -!- SUBUNIT: Interacts with p15BID. {ECO:0000269|PubMed:15899861, CC ECO:0000269|PubMed:20436477}. CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane CC {ECO:0000269|PubMed:15899861, ECO:0000269|PubMed:20436477}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Expressed in a wide variety of tissues. Predominant CC expressed in liver, kidney, heart, skeletal muscle and testis. CC {ECO:0000269|PubMed:12407445}. CC -!- DISRUPTION PHENOTYPE: Mice homozygous for a knockout allele exhibit CC abnormal mesoderm development, disorganized extraembryonic tissue, lack CC of amnion and chorion formation, decreased embryo size and lethality at CC around 7.5 dpc (PubMed:20436477). Conditional knockout in the liver CC decreases the sensitivity of mice to Fas-induced hepatocellular CC apoptosis and prevents the recruitment of tBID to liver mitochondria CC (PubMed:20436477). Conditional knockout in skeletal muscle results in CC increased mitochondrial mass and metabolism granting protection against CC diet-induced obesity (PubMed:26876167). {ECO:0000269|PubMed:20436477, CC ECO:0000269|PubMed:26876167}. CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family. CC {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; AF176009; AAD52647.1; -; mRNA. DR EMBL; AK003100; BAB22565.1; -; mRNA. DR EMBL; AK008487; BAB25694.1; -; mRNA. DR EMBL; AK008712; BAB25848.1; -; mRNA. DR EMBL; AK011785; BAB27839.1; -; mRNA. DR EMBL; AK011874; BAB27892.1; -; mRNA. DR EMBL; AK075890; BAC36033.1; -; mRNA. DR EMBL; AK161441; BAE36399.1; -; mRNA. DR EMBL; AK164169; BAE37660.1; -; mRNA. DR EMBL; BC002152; AAH02152.1; -; mRNA. DR EMBL; BC038899; AAH38899.1; -; mRNA. DR EMBL; BC038916; AAH38916.1; -; mRNA. DR CCDS; CCDS16416.1; -. DR RefSeq; NP_001304170.1; NM_001317241.1. DR RefSeq; NP_001304171.1; NM_001317242.1. DR RefSeq; NP_001304172.1; NM_001317243.1. DR RefSeq; NP_001304173.1; NM_001317244.1. DR RefSeq; NP_062732.1; NM_019758.3. DR AlphaFoldDB; Q791V5; -. DR SMR; Q791V5; -. DR BioGRID; 207972; 6. DR IntAct; Q791V5; 5. DR MINT; Q791V5; -. DR STRING; 10090.ENSMUSP00000118566; -. DR GlyGen; Q791V5; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q791V5; -. DR PhosphoSitePlus; Q791V5; -. DR SwissPalm; Q791V5; -. DR EPD; Q791V5; -. DR jPOST; Q791V5; -. DR MaxQB; Q791V5; -. DR PaxDb; 10090-ENSMUSP00000121851; -. DR ProteomicsDB; 287626; -. DR Pumba; Q791V5; -. DR Antibodypedia; 26842; 254 antibodies from 32 providers. DR DNASU; 56428; -. DR Ensembl; ENSMUST00000136872.8; ENSMUSP00000121851.2; ENSMUSG00000027282.18. DR GeneID; 56428; -. DR KEGG; mmu:56428; -. DR UCSC; uc008ktn.1; mouse. DR AGR; MGI:1929260; -. DR CTD; 23788; -. DR MGI; MGI:1929260; Mtch2. DR VEuPathDB; HostDB:ENSMUSG00000027282; -. DR eggNOG; KOG2745; Eukaryota. DR GeneTree; ENSGT00390000000020; -. DR InParanoid; Q791V5; -. DR OMA; PYAPIYT; -. DR OrthoDB; 3571419at2759; -. DR PhylomeDB; Q791V5; -. DR TreeFam; TF313721; -. DR BioGRID-ORCS; 56428; 10 hits in 78 CRISPR screens. DR ChiTaRS; Mtch2; mouse. DR PRO; PR:Q791V5; -. DR Proteomes; UP000000589; Chromosome 2. DR RNAct; Q791V5; Protein. DR Bgee; ENSMUSG00000027282; Expressed in spermatid and 85 other cell types or tissues. DR ExpressionAtlas; Q791V5; baseline and differential. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI. DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:MGI. DR GO; GO:0005739; C:mitochondrion; HDA:MGI. DR GO; GO:0032977; F:membrane insertase activity; ISS:UniProtKB. DR GO; GO:0071478; P:cellular response to radiation; IMP:MGI. DR GO; GO:0090152; P:establishment of protein localization to mitochondrial membrane involved in mitochondrial fission; IMP:MGI. DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; IMP:MGI. DR GO; GO:0035701; P:hematopoietic stem cell migration; IMP:MGI. DR GO; GO:0097284; P:hepatocyte apoptotic process; IGI:MGI. DR GO; GO:0006089; P:lactate metabolic process; IMP:MGI. DR GO; GO:0055088; P:lipid homeostasis; IMP:UniProtKB. DR GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; IMP:MGI. DR GO; GO:0045820; P:negative regulation of glycolytic process; IMP:MGI. DR GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; IMP:MGI. DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB. DR GO; GO:1902231; P:positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI. DR GO; GO:2000738; P:positive regulation of stem cell differentiation; IMP:UniProtKB. DR GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; ISS:UniProtKB. DR GO; GO:0070585; P:protein localization to mitochondrion; IMP:MGI. DR GO; GO:0010635; P:regulation of mitochondrial fusion; IMP:UniProtKB. DR GO; GO:1902108; P:regulation of mitochondrial membrane permeability involved in apoptotic process; IGI:MGI. DR Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1. DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier. DR InterPro; IPR023395; Mt_carrier_dom_sf. DR PANTHER; PTHR10780; MITOCHONDRIAL CARRIER HOMOLOG; 1. DR PANTHER; PTHR10780:SF20; MITOCHONDRIAL CARRIER HOMOLOG 2; 1. DR Pfam; PF00153; Mito_carr; 1. DR SUPFAM; SSF103506; Mitochondrial carrier; 1. DR PROSITE; PS50920; SOLCAR; 2. DR Genevisible; Q791V5; MM. PE 1: Evidence at protein level; KW Acetylation; Apoptosis; Direct protein sequencing; Membrane; Mitochondrion; KW Mitochondrion outer membrane; Reference proteome; Repeat; Transmembrane; KW Transmembrane helix. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:Q9Y6C9" FT CHAIN 2..303 FT /note="Mitochondrial carrier homolog 2" FT /id="PRO_0000090638" FT TOPO_DOM 2..15 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000305" FT TRANSMEM 16..36 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 37..77 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 78..92 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 93..135 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000305" FT TRANSMEM 136..156 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 157..180 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 181..199 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 200..231 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000305" FT TRANSMEM 232..252 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 253..280 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 281..303 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT REPEAT 2..98 FT /note="Solcar 1" FT REPEAT 118..206 FT /note="Solcar 2" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:Q9Y6C9" FT CONFLICT 206 FT /note="Y -> C (in Ref. 2; BAB27839)" FT /evidence="ECO:0000305" FT CONFLICT 207 FT /note="A -> T (in Ref. 2; BAB25848)" FT /evidence="ECO:0000305" SQ SEQUENCE 303 AA; 33499 MW; 248F8A1E4CF29975 CRC64; MADAASQVLL GSGLTILSQP LMYVKVLIQV GYEPLPPTIG RNIFGRQVCQ LPGLFCYAQH IASIDGRRGL FTGLTPRLCS GVLGTVVHGK VLQYYQESEK PEELGSVTVQ KEYSSSFDRV IKETTREMIA RSAATLITHP FHVITLRSMV QFIGRESKYC GLCDSIVTIY REEGIVGFFA GLIPRLLGDI ISLWLCNSLA YLINTYALDS GVSTMNEMKS YSQAVTGFFA SMLTYPFVLV SNLMAVNNCG LAGGSPPYSP IYTSWIDCWC MLQKAGNMSR GNSLFFRKVP CGKTYCYDLR MLI //