MTCH1_HUMAN
ID MTCH1_HUMAN Reviewed; 389 AA.
AC Q9NZJ7; A8KAX5; B2RCE3; Q6PK60; Q6UX45; Q7L465; Q9BW23; Q9NZR6; Q9UJZ5;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Mitochondrial carrier homolog 1;
DE AltName: Full=Presenilin-associated protein;
GN Name=MTCH1; Synonyms=PSAP; ORFNames=CGI-64, UNQ1871/PRO4314;
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] (ISOFORMS 1 AND 2).
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 (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Kidney, Muscle, and Pancreas;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 15-389, TISSUE SPECIFICITY, AND INTERACTION
RP WITH PSEN1.
RC TISSUE=Brain;
RX PubMed=10551805; DOI=10.1074/jbc.274.46.32543;
RA Xu X., Shi Y.-C., Wu X., Gambetti P., Sui D., Cui M.-Z.;
RT "Identification of a novel PSD-95/Dlg/ZO-1 (PDZ)-like protein interacting
RT with the C terminus of presenilin-1.";
RL J. Biol. Chem. 274:32543-32546(1999).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PSEN1.
RX PubMed=12377771; DOI=10.1074/jbc.m209613200;
RA Xu X., Shi Y.-C., Gao W., Mao G., Zhao G., Agrawal S., Chisolm G.M.,
RA Sui D., Cui M.-Z.;
RT "The novel presenilin-1-associated protein is a proapoptotic mitochondrial
RT protein.";
RL J. Biol. Chem. 277:48913-48922(2002).
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 METHYLATION [LARGE SCALE ANALYSIS] AT ARG-29, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [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: Potential mitochondrial transporter. May play a role in
CC apoptosis. {ECO:0000269|PubMed:12377771}.
CC -!- SUBUNIT: Interacts with PSEN1. {ECO:0000269|PubMed:10551805,
CC ECO:0000269|PubMed:12377771}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NZJ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NZJ7-2; Sequence=VSP_017882;
CC Name=3;
CC IsoId=Q9NZJ7-3; Sequence=VSP_017881, VSP_017882;
CC -!- TISSUE SPECIFICITY: Widely expressed with a predominant expression in
CC brain. {ECO:0000269|PubMed:10551805}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF07936.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF176006; AAD52644.3; -; mRNA.
DR EMBL; AF192559; AAF12793.3; -; mRNA.
DR EMBL; AY358519; AAQ88883.1; -; mRNA.
DR EMBL; AK315067; BAG37540.1; -; mRNA.
DR EMBL; AL122034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03927.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03928.1; -; Genomic_DNA.
DR EMBL; BC000702; AAH00702.2; -; mRNA.
DR EMBL; BC006507; AAH06507.1; -; mRNA.
DR EMBL; BC009962; AAH09962.2; -; mRNA.
DR EMBL; BC110914; AAI10915.1; -; mRNA.
DR EMBL; BC153873; AAI53874.1; -; mRNA.
DR EMBL; AF189289; AAF07936.1; ALT_INIT; mRNA.
DR CCDS; CCDS4828.1; -. [Q9NZJ7-2]
DR CCDS; CCDS64411.1; -. [Q9NZJ7-1]
DR RefSeq; NP_001258570.1; NM_001271641.1. [Q9NZJ7-1]
DR RefSeq; NP_055156.1; NM_014341.2. [Q9NZJ7-2]
DR AlphaFoldDB; Q9NZJ7; -.
DR BioGRID; 117286; 201.
DR IntAct; Q9NZJ7; 27.
DR MINT; Q9NZJ7; -.
DR STRING; 9606.ENSP00000362730; -.
DR TCDB; 2.A.29.25.1; the mitochondrial carrier (mc) family.
DR iPTMnet; Q9NZJ7; -.
DR MetOSite; Q9NZJ7; -.
DR PhosphoSitePlus; Q9NZJ7; -.
DR SwissPalm; Q9NZJ7; -.
DR BioMuta; MTCH1; -.
DR DMDM; 74753085; -.
DR EPD; Q9NZJ7; -.
DR jPOST; Q9NZJ7; -.
DR MassIVE; Q9NZJ7; -.
DR MaxQB; Q9NZJ7; -.
DR PaxDb; Q9NZJ7; -.
DR PeptideAtlas; Q9NZJ7; -.
DR PRIDE; Q9NZJ7; -.
DR ProteomicsDB; 83418; -. [Q9NZJ7-1]
DR ProteomicsDB; 83419; -. [Q9NZJ7-2]
DR ProteomicsDB; 83420; -. [Q9NZJ7-3]
DR Antibodypedia; 3010; 150 antibodies from 25 providers.
DR DNASU; 23787; -.
DR Ensembl; ENST00000373616.9; ENSP00000362718.5; ENSG00000137409.20. [Q9NZJ7-2]
DR Ensembl; ENST00000373627.10; ENSP00000362730.5; ENSG00000137409.20. [Q9NZJ7-1]
DR GeneID; 23787; -.
DR KEGG; hsa:23787; -.
DR MANE-Select; ENST00000373627.10; ENSP00000362730.5; NM_001271641.2; NP_001258570.1.
DR UCSC; uc003onc.3; human. [Q9NZJ7-1]
DR CTD; 23787; -.
DR GeneCards; MTCH1; -.
DR HGNC; HGNC:17586; MTCH1.
DR HPA; ENSG00000137409; Low tissue specificity.
DR MIM; 610449; gene.
DR neXtProt; NX_Q9NZJ7; -.
DR OpenTargets; ENSG00000137409; -.
DR PharmGKB; PA134958992; -.
DR VEuPathDB; HostDB:ENSG00000137409; -.
DR eggNOG; KOG2745; Eukaryota.
DR GeneTree; ENSGT00390000000020; -.
DR HOGENOM; CLU_058300_1_0_1; -.
DR InParanoid; Q9NZJ7; -.
DR OMA; KVGHEPM; -.
DR OrthoDB; 1439019at2759; -.
DR PhylomeDB; Q9NZJ7; -.
DR TreeFam; TF313721; -.
DR PathwayCommons; Q9NZJ7; -.
DR SignaLink; Q9NZJ7; -.
DR SIGNOR; Q9NZJ7; -.
DR BioGRID-ORCS; 23787; 8 hits in 1081 CRISPR screens.
DR ChiTaRS; MTCH1; human.
DR GeneWiki; MTCH1; -.
DR GenomeRNAi; 23787; -.
DR Pharos; Q9NZJ7; Tbio.
DR PRO; PR:Q9NZJ7; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9NZJ7; protein.
DR Bgee; ENSG00000137409; Expressed in endothelial cell and 201 other tissues.
DR ExpressionAtlas; Q9NZJ7; baseline and differential.
DR Genevisible; Q9NZJ7; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IMP:UniProtKB.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0045161; P:neuronal ion channel clustering; NAS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEP:UniProtKB.
DR GO; GO:0009966; P:regulation of signal transduction; NAS: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 Alternative splicing; Apoptosis; Membrane; Methylation; Mitochondrion;
KW Mitochondrion outer membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..389
FT /note="Mitochondrial carrier homolog 1"
FT /id="PRO_0000232385"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 81..176
FT /note="Solcar 1"
FT REPEAT 192..280
FT /note="Solcar 2"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 29
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 1..201
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_017881"
FT VAR_SEQ 286..302
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12975309,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|Ref.1"
FT /id="VSP_017882"
SQ SEQUENCE 389 AA; 41544 MW; 13C37758C4D22F4F CRC64;
MGASDPEVAP WARGGAAGMA GAGAGAGARG GAAAGVEARA RDPPPAHRAH PRHPRPAAQP
SARRMDGGSG GLGSGDNAPT TEALFVALGA GVTALSHPLL YVKLLIQVGH EPMPPTLGTN
VLGRKVLYLP SFFTYAKYIV QVDGKIGLFR GLSPRLMSNA LSTVTRGSMK KVFPPDEIEQ
VSNKDDMKTS LKKVVKETSY EMMMQCVSRM LAHPLHVISM RCMVQFVGRE AKYSGVLSSI
GKIFKEEGLL GFFVGLIPHL LGDVVFLWGC NLLAHFINAY LVDDSVSDTP GGLGNDQNPG
SQFSQALAIR SYTKFVMGIA VSMLTYPFLL VGDLMAVNNC GLQAGLPPYS PVFKSWIHCW
KYLSVQGQLF RGSSLLFRRV SSGSCFALE
