Full text data of MTCH1
MTCH1
(PSAP)
[Confidence: low (only semi-automatic identification from reviews)]
Mitochondrial carrier homolog 1 (Presenilin-associated protein)
Mitochondrial carrier homolog 1 (Presenilin-associated protein)
UniProt
Q9NZJ7
ID MTCH1_HUMAN Reviewed; 389 AA.
AC Q9NZJ7; A8KAX5; B2RCE3; Q6PK60; Q6UX45; Q7L465; Q9BW23; Q9NZR6;
read moreAC Q9UJZ5;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 96.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT family 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.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 15-389, TISSUE SPECIFICITY, AND
RP INTERACTION 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
RT interacting 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
RT mitochondrial 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Potential mitochondrial transporter. May play a role in
CC apoptosis.
CC -!- SUBUNIT: Interacts with PSEN1.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass
CC membrane protein (Potential).
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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely expressed with a predominant expression
CC in brain.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29)
CC family.
CC -!- SIMILARITY: Contains 2 Solcar repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF07936.1; Type=Erroneous initiation;
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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; CAI23305.1; -; Genomic_DNA.
DR EMBL; AL122034; CAI23306.1; -; 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 RefSeq; NP_001258570.1; NM_001271641.1.
DR RefSeq; NP_055156.1; NM_014341.2.
DR UniGene; Hs.485262; -.
DR ProteinModelPortal; Q9NZJ7; -.
DR IntAct; Q9NZJ7; 3.
DR TCDB; 2.A.29.25.1; the mitochondrial carrier (mc) family.
DR PhosphoSite; Q9NZJ7; -.
DR DMDM; 74753085; -.
DR PaxDb; Q9NZJ7; -.
DR PRIDE; Q9NZJ7; -.
DR DNASU; 23787; -.
DR Ensembl; ENST00000373616; ENSP00000362718; ENSG00000137409.
DR Ensembl; ENST00000373627; ENSP00000362730; ENSG00000137409.
DR GeneID; 23787; -.
DR KEGG; hsa:23787; -.
DR UCSC; uc003ond.2; human.
DR CTD; 23787; -.
DR GeneCards; GC06M036982; -.
DR HGNC; HGNC:17586; MTCH1.
DR HPA; HPA015971; -.
DR MIM; 610449; gene.
DR neXtProt; NX_Q9NZJ7; -.
DR PharmGKB; PA134958992; -.
DR eggNOG; NOG311439; -.
DR HOVERGEN; HBG058632; -.
DR InParanoid; Q9NZJ7; -.
DR OMA; FTYARHI; -.
DR OrthoDB; EOG7966H6; -.
DR PhylomeDB; Q9NZJ7; -.
DR ChiTaRS; MTCH1; human.
DR GeneWiki; MTCH1; -.
DR GenomeRNAi; 23787; -.
DR NextBio; 46793; -.
DR PRO; PR:Q9NZJ7; -.
DR ArrayExpress; Q9NZJ7; -.
DR Bgee; Q9NZJ7; -.
DR CleanEx; HS_MTCH1; -.
DR CleanEx; HS_PSAP; -.
DR Genevestigator; Q9NZJ7; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner 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: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 GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom.
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; Complete proteome; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1 389 Mitochondrial carrier homolog 1.
FT /FTId=PRO_0000232385.
FT TRANSMEM 248 268 Helical; (Potential).
FT TRANSMEM 315 335 Helical; (Potential).
FT REPEAT 81 176 Solcar 1.
FT REPEAT 192 280 Solcar 2.
FT VAR_SEQ 1 201 Missing (in isoform 3).
FT /FTId=VSP_017881.
FT VAR_SEQ 286 302 Missing (in isoform 2 and isoform 3).
FT /FTId=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
//
ID MTCH1_HUMAN Reviewed; 389 AA.
AC Q9NZJ7; A8KAX5; B2RCE3; Q6PK60; Q6UX45; Q7L465; Q9BW23; Q9NZR6;
read moreAC Q9UJZ5;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 96.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT family 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.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 15-389, TISSUE SPECIFICITY, AND
RP INTERACTION 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
RT interacting 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
RT mitochondrial 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Potential mitochondrial transporter. May play a role in
CC apoptosis.
CC -!- SUBUNIT: Interacts with PSEN1.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass
CC membrane protein (Potential).
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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely expressed with a predominant expression
CC in brain.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29)
CC family.
CC -!- SIMILARITY: Contains 2 Solcar repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF07936.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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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; CAI23305.1; -; Genomic_DNA.
DR EMBL; AL122034; CAI23306.1; -; 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 RefSeq; NP_001258570.1; NM_001271641.1.
DR RefSeq; NP_055156.1; NM_014341.2.
DR UniGene; Hs.485262; -.
DR ProteinModelPortal; Q9NZJ7; -.
DR IntAct; Q9NZJ7; 3.
DR TCDB; 2.A.29.25.1; the mitochondrial carrier (mc) family.
DR PhosphoSite; Q9NZJ7; -.
DR DMDM; 74753085; -.
DR PaxDb; Q9NZJ7; -.
DR PRIDE; Q9NZJ7; -.
DR DNASU; 23787; -.
DR Ensembl; ENST00000373616; ENSP00000362718; ENSG00000137409.
DR Ensembl; ENST00000373627; ENSP00000362730; ENSG00000137409.
DR GeneID; 23787; -.
DR KEGG; hsa:23787; -.
DR UCSC; uc003ond.2; human.
DR CTD; 23787; -.
DR GeneCards; GC06M036982; -.
DR HGNC; HGNC:17586; MTCH1.
DR HPA; HPA015971; -.
DR MIM; 610449; gene.
DR neXtProt; NX_Q9NZJ7; -.
DR PharmGKB; PA134958992; -.
DR eggNOG; NOG311439; -.
DR HOVERGEN; HBG058632; -.
DR InParanoid; Q9NZJ7; -.
DR OMA; FTYARHI; -.
DR OrthoDB; EOG7966H6; -.
DR PhylomeDB; Q9NZJ7; -.
DR ChiTaRS; MTCH1; human.
DR GeneWiki; MTCH1; -.
DR GenomeRNAi; 23787; -.
DR NextBio; 46793; -.
DR PRO; PR:Q9NZJ7; -.
DR ArrayExpress; Q9NZJ7; -.
DR Bgee; Q9NZJ7; -.
DR CleanEx; HS_MTCH1; -.
DR CleanEx; HS_PSAP; -.
DR Genevestigator; Q9NZJ7; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner 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: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 GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom.
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; Complete proteome; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1 389 Mitochondrial carrier homolog 1.
FT /FTId=PRO_0000232385.
FT TRANSMEM 248 268 Helical; (Potential).
FT TRANSMEM 315 335 Helical; (Potential).
FT REPEAT 81 176 Solcar 1.
FT REPEAT 192 280 Solcar 2.
FT VAR_SEQ 1 201 Missing (in isoform 3).
FT /FTId=VSP_017881.
FT VAR_SEQ 286 302 Missing (in isoform 2 and isoform 3).
FT /FTId=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
//
MIM
610449
*RECORD*
*FIELD* NO
610449
*FIELD* TI
*610449 MITOCHONDRIAL CARRIER HOMOLOG 1; MTCH1
;;PRESENILIN-ASSOCIATED PROTEIN; PSAP
read more*FIELD* TX
CLONING
On a yeast 2-hybrid screen of a human brain cDNA library for proteins
that interact with the C terminus of presenilin-1 (PSEN1; 104311), Xu et
al. (1999) identified a novel cDNA, which they designated PSAP
(presenilin-associated protein). The deduced 371-amino acid PSAP protein
has a predicted molecular mass of 39.9 kD and contains a PDZ-like domain
and several putative protein kinase C and tyrosine kinase
phosphorylation sites. Northern blot analysis of multiple human tissues
detected a 1.9-kb PSAP transcript with highest expression in brain,
lower expression in heart, and barely detectable expression in all other
tissues tested. PSAP shares 28% sequence identity and 65% similarity
with the C. elegans protein F43E2.7. Using yeast 2-hybrid analysis, Xu
et al. (1999) showed that PSAP specifically interacts with the
C-terminal region of PSEN1 but not with other regions of the protein or
with the C terminus of PSEN2 (600759). By Western blot analysis and
immunofluorescence microscopy of HEK293 cells, Xu et al. (2002) found
that PSAP was present exclusively in the mitochondria-enriched fraction.
The same subcellular distribution was observed for cells of neuronal
origin, including M17 and N2a, and a BLAST search indicated that PSAP
shares regions of homology with mitochondrial carrier proteins.
GENE FUNCTION
Xu et al. (1999) found that PSAP and full-length PSEN1
coimmunoprecipitate in HEK293 cells, indicating that the proteins
interact in vivo. Using deletion mutants, they determined that the
4-amino acid consensus sequence (gln-phe-tyr-ile) for binding PDZ
domains at the extreme C terminus of PSEN1 is required for binding PSAP.
Xu et al. (2002) observed that expression of PSAP cDNA in several cell
lines led to apoptotic cell death. PSAP-induced apoptosis was documented
using multiple independent approaches, including membrane blebbing,
chromosome condensation and fragmentation, DNA laddering, cleavage of
the death substrate poly(ADP-ribose) polymerase (PARP; 173870), and flow
cytometry. PSAP-induced cell death was accompanied by cytochrome c
(123970) release from mitochondria and caspase-3 (600636) activation.
The general caspase inhibitor
benzyloxycarbonyl-val-ala-asp-fluoromethylketone (z-VAD-fmk), which
blocked cell death, did not block the release of cytochrome c from
mitochondria caused by overexpression of PSAP, indicating that
PSAP-induced cytochrome c release was independent of caspase activity.
Coexpression of PSEN1 and PSAP in HEK293 cells showed that PSEN1 has a
weak inhibitory effect on PSAP-induced apoptosis. No significant
differences were detected between wildtype PSEN1 and PSEN1 mutants that
had previously been shown to affect the biologic function of PSEN1.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the MTCH1
gene to chromosome 6 (TMAP WI-5783).
*FIELD* RF
1. Xu, X.; Shi, Y.; Gao, W.; Mao, G.; Zhao, G.; Agrawal, S.; Chisolm,
G. M.; Sui, D.; Cui, M.-Z.: The novel presenilin-1-associated protein
is a proapoptotic mitochondrial protein. J. Biol. Chem. 277: 48913-48922,
2002.
2. Xu, X.; Shi, Y.; Wu, X.; Gambetti, P.; Sui, D.; Cui, M.-Z.: Identification
of a novel PSD-95/Dlg/ZO-1 (PDZ)-like protein interacting with the
C terminus of presenilin-1. J. Biol. Chem. 274: 32543-32546, 1999.
*FIELD* CD
Jennifer L. Goldstein: 9/27/2006
*FIELD* ED
carol: 09/27/2006
carol: 9/27/2006
*RECORD*
*FIELD* NO
610449
*FIELD* TI
*610449 MITOCHONDRIAL CARRIER HOMOLOG 1; MTCH1
;;PRESENILIN-ASSOCIATED PROTEIN; PSAP
read more*FIELD* TX
CLONING
On a yeast 2-hybrid screen of a human brain cDNA library for proteins
that interact with the C terminus of presenilin-1 (PSEN1; 104311), Xu et
al. (1999) identified a novel cDNA, which they designated PSAP
(presenilin-associated protein). The deduced 371-amino acid PSAP protein
has a predicted molecular mass of 39.9 kD and contains a PDZ-like domain
and several putative protein kinase C and tyrosine kinase
phosphorylation sites. Northern blot analysis of multiple human tissues
detected a 1.9-kb PSAP transcript with highest expression in brain,
lower expression in heart, and barely detectable expression in all other
tissues tested. PSAP shares 28% sequence identity and 65% similarity
with the C. elegans protein F43E2.7. Using yeast 2-hybrid analysis, Xu
et al. (1999) showed that PSAP specifically interacts with the
C-terminal region of PSEN1 but not with other regions of the protein or
with the C terminus of PSEN2 (600759). By Western blot analysis and
immunofluorescence microscopy of HEK293 cells, Xu et al. (2002) found
that PSAP was present exclusively in the mitochondria-enriched fraction.
The same subcellular distribution was observed for cells of neuronal
origin, including M17 and N2a, and a BLAST search indicated that PSAP
shares regions of homology with mitochondrial carrier proteins.
GENE FUNCTION
Xu et al. (1999) found that PSAP and full-length PSEN1
coimmunoprecipitate in HEK293 cells, indicating that the proteins
interact in vivo. Using deletion mutants, they determined that the
4-amino acid consensus sequence (gln-phe-tyr-ile) for binding PDZ
domains at the extreme C terminus of PSEN1 is required for binding PSAP.
Xu et al. (2002) observed that expression of PSAP cDNA in several cell
lines led to apoptotic cell death. PSAP-induced apoptosis was documented
using multiple independent approaches, including membrane blebbing,
chromosome condensation and fragmentation, DNA laddering, cleavage of
the death substrate poly(ADP-ribose) polymerase (PARP; 173870), and flow
cytometry. PSAP-induced cell death was accompanied by cytochrome c
(123970) release from mitochondria and caspase-3 (600636) activation.
The general caspase inhibitor
benzyloxycarbonyl-val-ala-asp-fluoromethylketone (z-VAD-fmk), which
blocked cell death, did not block the release of cytochrome c from
mitochondria caused by overexpression of PSAP, indicating that
PSAP-induced cytochrome c release was independent of caspase activity.
Coexpression of PSEN1 and PSAP in HEK293 cells showed that PSEN1 has a
weak inhibitory effect on PSAP-induced apoptosis. No significant
differences were detected between wildtype PSEN1 and PSEN1 mutants that
had previously been shown to affect the biologic function of PSEN1.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the MTCH1
gene to chromosome 6 (TMAP WI-5783).
*FIELD* RF
1. Xu, X.; Shi, Y.; Gao, W.; Mao, G.; Zhao, G.; Agrawal, S.; Chisolm,
G. M.; Sui, D.; Cui, M.-Z.: The novel presenilin-1-associated protein
is a proapoptotic mitochondrial protein. J. Biol. Chem. 277: 48913-48922,
2002.
2. Xu, X.; Shi, Y.; Wu, X.; Gambetti, P.; Sui, D.; Cui, M.-Z.: Identification
of a novel PSD-95/Dlg/ZO-1 (PDZ)-like protein interacting with the
C terminus of presenilin-1. J. Biol. Chem. 274: 32543-32546, 1999.
*FIELD* CD
Jennifer L. Goldstein: 9/27/2006
*FIELD* ED
carol: 09/27/2006
carol: 9/27/2006