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 27-MAR-2024, entry version 164. DE RecName: Full=Mitochondrial carrier homolog 1 {ECO:0000305}; DE AltName: Full=Presenilin-associated protein {ECO:0000303|PubMed:12377771}; GN Name=MTCH1 {ECO:0000303|PubMed:36264797, ECO:0000312|HGNC:HGNC:17586}; GN Synonyms=PSAP {ECO:0000303|PubMed:12377771}; GN 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). RN [12] RP FUNCTION. RX PubMed=36264797; DOI=10.1126/science.add1856; RA Guna A., Stevens T.A., Inglis A.J., Replogle J.M., Esantsi T.K., RA Muthukumar G., Shaffer K.C.L., Wang M.L., Pogson A.N., Jones J.J., RA Lomenick B., Chou T.F., Weissman J.S., Voorhees R.M.; RT "MTCH2 is a mitochondrial outer membrane protein insertase."; RL Science 378:317-322(2022). CC -!- FUNCTION: Protein insertase that mediates insertion of transmembrane CC proteins into the mitochondrial outer membrane (PubMed:36264797). CC Catalyzes insertion of proteins with alpha-helical transmembrane CC regions, such as signal-anchored, tail-anchored and multi-pass membrane CC proteins (By similarity). Does not mediate insertion of beta-barrel CC transmembrane proteins (By similarity). May play a role in apoptosis CC (PubMed:12377771). {ECO:0000250|UniProtKB:Q9Y6C9, CC ECO:0000269|PubMed:12377771, ECO:0000269|PubMed:36264797}. CC -!- SUBUNIT: Interacts with PSEN1. {ECO:0000269|PubMed:10551805, CC ECO:0000269|PubMed:12377771}. CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane CC {ECO:0000305|PubMed:12377771}; Multi-pass membrane protein CC {ECO:0000255}. 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}; 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; 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; 203. 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; 9606-ENSP00000362730; -. DR PeptideAtlas; Q9NZJ7; -. DR ProteomicsDB; 83418; -. [Q9NZJ7-1] DR ProteomicsDB; 83419; -. [Q9NZJ7-2] DR ProteomicsDB; 83420; -. [Q9NZJ7-3] DR Pumba; Q9NZJ7; -. DR Antibodypedia; 3010; 175 antibodies from 25 providers. DR DNASU; 23787; -. DR Ensembl; ENST00000373616.9; ENSP00000362718.5; ENSG00000137409.21. [Q9NZJ7-2] DR Ensembl; ENST00000373627.10; ENSP00000362730.5; ENSG00000137409.21. [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 AGR; HGNC:17586; -. 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; CWNDLQA; -. DR OrthoDB; 3571419at2759; -. DR PhylomeDB; Q9NZJ7; -. DR TreeFam; TF313721; -. DR PathwayCommons; Q9NZJ7; -. DR SignaLink; Q9NZJ7; -. DR SIGNOR; Q9NZJ7; -. DR BioGRID-ORCS; 23787; 10 hits in 1160 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 203 other cell types or tissues. DR ExpressionAtlas; Q9NZJ7; baseline and differential. 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:0032977; F:membrane insertase activity; IDA: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:0045040; P:protein insertion into mitochondrial outer membrane; IDA:UniProtKB. DR GO; GO:0009966; P:regulation of signal transduction; NAS:UniProtKB. 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:SF3; MITOCHONDRIAL CARRIER HOMOLOG 1; 1. DR Pfam; PF00153; Mito_carr; 1. DR SUPFAM; SSF103506; Mitochondrial carrier; 1. DR PROSITE; PS50920; SOLCAR; 2. DR Genevisible; Q9NZJ7; HS. 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 TOPO_DOM 1..93 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000305" FT TRANSMEM 94..104 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 105..155 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 156..176 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 177..209 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000305" FT TRANSMEM 210..229 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 230..254 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 255..279 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 280..322 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000305" FT TRANSMEM 323..342 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 343..371 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 372..389 FT /note="Helical; Name=6" 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 //