MTCH2_HUMAN
ID MTCH2_HUMAN Reviewed; 303 AA.
AC Q9Y6C9; B2R7L8;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Mitochondrial carrier homolog 2;
DE AltName: Full=Met-induced mitochondrial protein {ECO:0000303|PubMed:12407445};
GN Name=MTCH2 {ECO:0000312|HGNC:HGNC:17587};
GN Synonyms=MIMP {ECO:0000303|PubMed:12407445}; ORFNames=HSPC032;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
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 [7]
RP PROTEIN SEQUENCE OF 78-90; 112-122; 132-155 AND 281-287, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Plays important roles in regulating apoptosis, metabolism and
CC mitochondrial dynamics. MTCH2 acts as a receptor for the truncated form
CC of pro-apoptotic BH3-interacting domain death agonist (p15 BID) and has
CC therefore a critical function in apoptosis. Plays a critical role in
CC controlling the quiescence/cycling of hematopoietic stem cells (HSCs).
CC Acts as a regulator of mitochondrial fusion, essential for the naive-
CC to-primed interconversion of embryonic stem cells (ESCs). Acts as a
CC regulator of lipid homeostasis and has a regulatory role in adipocyte
CC differentiation and biology. {ECO:0000250|UniProtKB:Q791V5}.
CC -!- SUBUNIT: Interacts with p15BID. {ECO:0000250|UniProtKB:Q791V5}.
CC -!- INTERACTION:
CC Q9Y6C9; P02654: APOC1; NbExp=3; IntAct=EBI-6164522, EBI-1220105;
CC Q9Y6C9; P56378-2: ATP5MPL; NbExp=3; IntAct=EBI-6164522, EBI-17870477;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q791V5}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q791V5}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; AY380792; AAQ88168.1; -; mRNA.
DR EMBL; AF176008; AAD52646.1; -; mRNA.
DR EMBL; AF085361; AAD40196.1; -; mRNA.
DR EMBL; AK313032; BAG35865.1; -; mRNA.
DR EMBL; CH471064; EAW67892.1; -; Genomic_DNA.
DR EMBL; BC000875; AAH00875.1; -; mRNA.
DR CCDS; CCDS7943.1; -.
DR RefSeq; NP_001304160.1; NM_001317231.1.
DR RefSeq; NP_001304161.1; NM_001317232.1.
DR RefSeq; NP_001304162.1; NM_001317233.1.
DR RefSeq; NP_055157.1; NM_014342.3.
DR AlphaFoldDB; Q9Y6C9; -.
DR BioGRID; 117287; 399.
DR IntAct; Q9Y6C9; 56.
DR MINT; Q9Y6C9; -.
DR STRING; 9606.ENSP00000303222; -.
DR ChEMBL; CHEMBL4523511; -.
DR TCDB; 2.A.29.25.2; the mitochondrial carrier (mc) family.
DR iPTMnet; Q9Y6C9; -.
DR MetOSite; Q9Y6C9; -.
DR PhosphoSitePlus; Q9Y6C9; -.
DR SwissPalm; Q9Y6C9; -.
DR BioMuta; MTCH2; -.
DR DMDM; 67461088; -.
DR EPD; Q9Y6C9; -.
DR jPOST; Q9Y6C9; -.
DR MassIVE; Q9Y6C9; -.
DR MaxQB; Q9Y6C9; -.
DR PaxDb; Q9Y6C9; -.
DR PeptideAtlas; Q9Y6C9; -.
DR PRIDE; Q9Y6C9; -.
DR ProteomicsDB; 86652; -.
DR TopDownProteomics; Q9Y6C9; -.
DR Antibodypedia; 26842; 236 antibodies from 32 providers.
DR DNASU; 23788; -.
DR Ensembl; ENST00000302503.8; ENSP00000303222.3; ENSG00000109919.10.
DR Ensembl; ENST00000643223.2; ENSP00000495027.1; ENSG00000285121.2.
DR GeneID; 23788; -.
DR KEGG; hsa:23788; -.
DR MANE-Select; ENST00000302503.8; ENSP00000303222.3; NM_014342.4; NP_055157.1.
DR UCSC; uc010rho.3; human.
DR CTD; 23788; -.
DR DisGeNET; 23788; -.
DR GeneCards; MTCH2; -.
DR HGNC; HGNC:17587; MTCH2.
DR HPA; ENSG00000109919; Low tissue specificity.
DR MIM; 613221; gene.
DR neXtProt; NX_Q9Y6C9; -.
DR NIAGADS; ENSG00000109919; -.
DR OpenTargets; ENSG00000109919; -.
DR PharmGKB; PA134951260; -.
DR VEuPathDB; HostDB:ENSG00000109919; -.
DR eggNOG; KOG2745; Eukaryota.
DR GeneTree; ENSGT00390000000020; -.
DR InParanoid; Q9Y6C9; -.
DR OMA; PYAPIYT; -.
DR OrthoDB; 1439019at2759; -.
DR PhylomeDB; Q9Y6C9; -.
DR TreeFam; TF313721; -.
DR PathwayCommons; Q9Y6C9; -.
DR SignaLink; Q9Y6C9; -.
DR SIGNOR; Q9Y6C9; -.
DR BioGRID-ORCS; 23788; 86 hits in 1084 CRISPR screens.
DR ChiTaRS; MTCH2; human.
DR GeneWiki; MTCH2; -.
DR GenomeRNAi; 23788; -.
DR Pharos; Q9Y6C9; Tbio.
DR PRO; PR:Q9Y6C9; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9Y6C9; protein.
DR Bgee; ENSG00000109919; Expressed in left testis and 102 other tissues.
DR ExpressionAtlas; Q9Y6C9; baseline and differential.
DR Genevisible; Q9Y6C9; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0055088; P:lipid homeostasis; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:2000738; P:positive regulation of stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0070585; P:protein localization to mitochondrion; IMP:MGI.
DR GO; GO:0010635; P:regulation of mitochondrial fusion; ISS:UniProtKB.
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; Direct protein sequencing; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..303
FT /note="Mitochondrial carrier homolog 2"
FT /id="PRO_0000090637"
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:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:25944712"
FT VARIANT 68
FT /note="R -> S (in dbSNP:rs34072236)"
FT /id="VAR_050128"
FT VARIANT 290
FT /note="P -> A (in dbSNP:rs1064608)"
FT /id="VAR_050129"
SQ SEQUENCE 303 AA; 33331 MW; 339087A8AF4A4508 CRC64;
MADAASQVLL GSGLTILSQP LMYVKVLIQV GYEPLPPTIG RNIFGRQVCQ LPGLFSYAQH
IASIDGRRGL FTGLTPRLCS GVLGTVVHGK VLQHYQESDK GEELGPGNVQ KEVSSSFDHV
IKETTREMIA RSAATLITHP FHVITLRSMV QFIGRESKYC GLCDSIITIY REEGILGFFA
GLVPRLLGDI LSLWLCNSLA YLVNTYALDS GVSTMNEMKS YSQAVTGFFA SMLTYPFVLV
SNLMAVNNCG LAGGCPPYSP IYTSWIDCWC MLQKEGNMSR GNSLFFRKVP FGKTYCCDLK
MLI
