MTCH2_MOUSE
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 03-AUG-2022, entry version 124.
DE RecName: Full=Mitochondrial carrier homolog 2;
DE AltName: Full=Met-induced mitochondrial protein {ECO:0000303|PubMed:12407445};
GN Name=Mtch2; 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 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, 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 [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: Plays important roles in regulating apoptosis, metabolism and
CC mitochondrial dynamics (PubMed:30510213, PubMed:26876167,
CC PubMed:26219591, PubMed:20436477). MTCH2 acts as a receptor for the
CC truncated form of pro-apoptotic BH3-interacting domain death agonist
CC (p15 BID) and has therefore a critical function in apoptosis
CC (PubMed:20436477). Plays a critical role in controlling the
CC quiescence/cycling of hematopoietic stem cells (HSCs) (PubMed:20436477,
CC PubMed:26876167, PubMed:26219591). 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:28127879, PubMed:26876167).
CC {ECO:0000269|PubMed:20436477, ECO:0000269|PubMed:26219591,
CC ECO:0000269|PubMed:26876167, ECO:0000269|PubMed:28127879,
CC 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 BioGRID; 207972; 6.
DR IntAct; Q791V5; 5.
DR MINT; Q791V5; -.
DR STRING; 10090.ENSMUSP00000121851; -.
DR iPTMnet; Q791V5; -.
DR PhosphoSitePlus; Q791V5; -.
DR SwissPalm; Q791V5; -.
DR EPD; Q791V5; -.
DR jPOST; Q791V5; -.
DR MaxQB; Q791V5; -.
DR PaxDb; Q791V5; -.
DR PRIDE; Q791V5; -.
DR ProteomicsDB; 287626; -.
DR Antibodypedia; 26842; 236 antibodies from 32 providers.
DR DNASU; 56428; -.
DR Ensembl; ENSMUST00000136872; ENSMUSP00000121851; ENSMUSG00000027282.
DR GeneID; 56428; -.
DR KEGG; mmu:56428; -.
DR UCSC; uc008ktn.1; mouse.
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; 1439019at2759; -.
DR PhylomeDB; Q791V5; -.
DR TreeFam; TF313721; -.
DR BioGRID-ORCS; 56428; 10 hits in 73 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 83 other tissues.
DR ExpressionAtlas; Q791V5; baseline and differential.
DR Genevisible; Q791V5; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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: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:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:MGI.
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: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; -; 1.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF00153; Mito_carr; 1.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 2.
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 TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
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
