COX10_HUMAN
ID COX10_HUMAN Reviewed; 443 AA.
AC Q12887; B2R6U5; B4DJ50; O15334; Q969F7;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 3.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Protoheme IX farnesyltransferase, mitochondrial;
DE EC=2.5.1.141 {ECO:0000250|UniProtKB:P24009};
DE AltName: Full=Heme O synthase;
DE Flags: Precursor;
GN Name=COX10;
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] (ISOFORM 1), AND VARIANTS GLN-159 AND ASP-340.
RX PubMed=8078902; DOI=10.1073/pnas.91.18.8452;
RA Glerum M.D., Tzagoloff A.;
RT "Isolation of a human cDNA for heme A:farnesyltransferase by functional
RT complementation of a yeast cox10 mutant.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:8452-8456(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-159.
RX PubMed=9177788; DOI=10.1006/geno.1997.4711;
RA Murakami T., Reiter L.T., Lupski J.R.;
RT "Genomic structure and expression of the human heme A:farnesyltransferase
RT (COX10) gene.";
RL Genomics 42:161-164(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP GLN-159.
RC TISSUE=Brain, and Substantia nigra;
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 MRNA] (ISOFORM 1), AND VARIANT GLN-159.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLN-159.
RC TISSUE=Brain;
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 VARIANT MC4DN3 LYS-204.
RX PubMed=10767350; DOI=10.1093/hmg/9.8.1245;
RA Valnot I., von Kleist-Retzow J.C., Barrientos A., Gorbatyuk M.,
RA Taanman J.W., Mehaye B., Rustin P., Tzagoloff A., Munnich A., Rotig A.;
RT "A mutation in the human heme A:farnesyltransferase gene (COX10) causes
RT cytochrome c oxidase deficiency.";
RL Hum. Mol. Genet. 9:1245-1249(2000).
RN [8]
RP VARIANTS MC4DN3 LYS-196; LEU-225; GLY-336 AND VAL-336.
RX PubMed=12928484; DOI=10.1093/hmg/ddg284;
RA Antonicka H., Leary S.C., Guercin G.-H., Agar J.N., Horvath R.,
RA Kennaway N.G., Harding C.O., Jaksch M., Shoubridge E.A.;
RT "Mutations in COX10 result in a defect in mitochondrial heme A biosynthesis
RT and account for multiple, early-onset clinical phenotypes associated with
RT isolated COX deficiency.";
RL Hum. Mol. Genet. 12:2693-2702(2003).
RN [9]
RP VARIANT HIS-258.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H.,
RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
RN [10]
RP VARIANTS MC4DN3 ARG-288 AND LEU-420.
RX PubMed=26741492; DOI=10.1371/journal.pgen.1005679;
RA Kohda M., Tokuzawa Y., Kishita Y., Nyuzuki H., Moriyama Y., Mizuno Y.,
RA Hirata T., Yatsuka Y., Yamashita-Sugahara Y., Nakachi Y., Kato H.,
RA Okuda A., Tamaru S., Borna N.N., Banshoya K., Aigaki T., Sato-Miyata Y.,
RA Ohnuma K., Suzuki T., Nagao A., Maehata H., Matsuda F., Higasa K.,
RA Nagasaki M., Yasuda J., Yamamoto M., Fushimi T., Shimura M.,
RA Kaiho-Ichimoto K., Harashima H., Yamazaki T., Mori M., Murayama K.,
RA Ohtake A., Okazaki Y.;
RT "A comprehensive genomic analysis reveals the genetic landscape of
RT mitochondrial respiratory chain complex deficiencies.";
RL PLoS Genet. 12:E1005679-E1005679(2016).
CC -!- FUNCTION: Converts protoheme IX and farnesyl diphosphate to heme O.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate +
CC Fe(II)-heme o; Xref=Rhea:RHEA:28070, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:60344, ChEBI:CHEBI:60530,
CC ChEBI:CHEBI:175763; EC=2.5.1.141;
CC Evidence={ECO:0000250|UniProtKB:P24009};
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q12887-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q12887-2; Sequence=VSP_056867, VSP_056868;
CC -!- DISEASE: Mitochondrial complex IV deficiency, nuclear type 3 (MC4DN3)
CC [MIM:619046]: An autosomal recessive mitochondrial disorder
CC characterized by cytochrome c oxidase deficiency. Clinical features
CC include muscle weakness, hypotonia, ataxia, ptosis, metabolic acidosis,
CC poor feeding, delayed motor development, anemia, sensorineural hearing
CC loss, and cardiomyopathy. {ECO:0000269|PubMed:10767350,
CC ECO:0000269|PubMed:12928484, ECO:0000269|PubMed:26741492}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000305}.
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DR EMBL; U09466; AAA21148.1; -; mRNA.
DR EMBL; U82010; AAC51330.1; -; Genomic_DNA.
DR EMBL; U82004; AAC51330.1; JOINED; Genomic_DNA.
DR EMBL; U82005; AAC51330.1; JOINED; Genomic_DNA.
DR EMBL; U82006; AAC51330.1; JOINED; Genomic_DNA.
DR EMBL; U82007; AAC51330.1; JOINED; Genomic_DNA.
DR EMBL; U82008; AAC51330.1; JOINED; Genomic_DNA.
DR EMBL; U82009; AAC51330.1; JOINED; Genomic_DNA.
DR EMBL; AK295925; BAG58712.1; -; mRNA.
DR EMBL; AK312718; BAG35592.1; -; mRNA.
DR EMBL; BT006985; AAP35631.1; -; mRNA.
DR EMBL; AC005224; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005389; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000060; AAH00060.1; -; mRNA.
DR EMBL; BC006394; AAH06394.1; -; mRNA.
DR CCDS; CCDS11166.1; -. [Q12887-1]
DR PIR; I38603; I38603.
DR RefSeq; NP_001294.2; NM_001303.3. [Q12887-1]
DR AlphaFoldDB; Q12887; -.
DR SMR; Q12887; -.
DR BioGRID; 107745; 8.
DR IntAct; Q12887; 3.
DR MINT; Q12887; -.
DR STRING; 9606.ENSP00000261643; -.
DR iPTMnet; Q12887; -.
DR PhosphoSitePlus; Q12887; -.
DR BioMuta; COX10; -.
DR DMDM; 292495084; -.
DR EPD; Q12887; -.
DR jPOST; Q12887; -.
DR MassIVE; Q12887; -.
DR MaxQB; Q12887; -.
DR PaxDb; Q12887; -.
DR PeptideAtlas; Q12887; -.
DR PRIDE; Q12887; -.
DR ProteomicsDB; 59002; -. [Q12887-1]
DR Antibodypedia; 25099; 228 antibodies from 25 providers.
DR DNASU; 1352; -.
DR Ensembl; ENST00000261643.8; ENSP00000261643.3; ENSG00000006695.12. [Q12887-1]
DR Ensembl; ENST00000664217.1; ENSP00000499396.1; ENSG00000006695.12. [Q12887-1]
DR GeneID; 1352; -.
DR KEGG; hsa:1352; -.
DR MANE-Select; ENST00000261643.8; ENSP00000261643.3; NM_001303.4; NP_001294.2.
DR UCSC; uc002gof.5; human. [Q12887-1]
DR CTD; 1352; -.
DR DisGeNET; 1352; -.
DR GeneCards; COX10; -.
DR GeneReviews; COX10; -.
DR HGNC; HGNC:2260; COX10.
DR HPA; ENSG00000006695; Tissue enhanced (skeletal muscle, tongue).
DR MalaCards; COX10; -.
DR MIM; 602125; gene.
DR MIM; 619046; phenotype.
DR neXtProt; NX_Q12887; -.
DR OpenTargets; ENSG00000006695; -.
DR Orphanet; 254905; Isolated cytochrome C oxidase deficiency.
DR PharmGKB; PA26776; -.
DR VEuPathDB; HostDB:ENSG00000006695; -.
DR eggNOG; KOG1380; Eukaryota.
DR GeneTree; ENSGT00940000153771; -.
DR HOGENOM; CLU_029631_2_2_1; -.
DR InParanoid; Q12887; -.
DR OMA; MGREPDF; -.
DR OrthoDB; 1260807at2759; -.
DR PhylomeDB; Q12887; -.
DR TreeFam; TF105071; -.
DR BioCyc; MetaCyc:HS00191-MON; -.
DR BRENDA; 2.5.1.141; 2681.
DR PathwayCommons; Q12887; -.
DR Reactome; R-HSA-189451; Heme biosynthesis.
DR SignaLink; Q12887; -.
DR BioGRID-ORCS; 1352; 245 hits in 1080 CRISPR screens.
DR ChiTaRS; COX10; human.
DR GeneWiki; COX10; -.
DR GenomeRNAi; 1352; -.
DR Pharos; Q12887; Tbio.
DR PRO; PR:Q12887; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q12887; protein.
DR Bgee; ENSG00000006695; Expressed in tibialis anterior and 170 other tissues.
DR ExpressionAtlas; Q12887; baseline and differential.
DR Genevisible; Q12887; HS.
DR GO; GO:0070069; C:cytochrome complex; IMP:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0004311; F:farnesyltranstransferase activity; IGI:MGI.
DR GO; GO:0008495; F:protoheme IX farnesyltransferase activity; TAS:Reactome.
DR GO; GO:0009060; P:aerobic respiration; IEA:Ensembl.
DR GO; GO:0006784; P:heme A biosynthetic process; IMP:HGNC-UCL.
DR GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000266; P:mitochondrial fission; IEA:Ensembl.
DR GO; GO:0008535; P:respiratory chain complex IV assembly; IMP:HGNC-UCL.
DR CDD; cd13957; PT_UbiA_Cox10; 1.
DR Gene3D; 1.10.357.140; -; 1.
DR HAMAP; MF_00154; CyoE_CtaB; 1.
DR InterPro; IPR006369; Protohaem_IX_farnesylTrfase.
DR InterPro; IPR016315; Protohaem_IX_farnesylTrfase_mt.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR030470; UbiA_prenylTrfase_CS.
DR InterPro; IPR044878; UbiA_sf.
DR PANTHER; PTHR43448; PTHR43448; 1.
DR Pfam; PF01040; UbiA; 1.
DR PIRSF; PIRSF001773; COX10; 1.
DR TIGRFAMs; TIGR01473; cyoE_ctaB; 1.
DR PROSITE; PS00943; UBIA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; Heme biosynthesis; Leigh syndrome;
KW Lipid metabolism; Membrane; Mitochondrion; Primary mitochondrial disease;
KW Reference proteome; Transferase; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..443
FT /note="Protoheme IX farnesyltransferase, mitochondrial"
FT /id="PRO_0000035923"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..15
FT /note="MAASPHTLSSRLLTG -> MICQEFWLDYPKSNS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056867"
FT VAR_SEQ 16..207
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056868"
FT VARIANT 28
FT /note="T -> I (in dbSNP:rs16948978)"
FT /id="VAR_057371"
FT VARIANT 62
FT /note="T -> S (in dbSNP:rs2230351)"
FT /id="VAR_057372"
FT VARIANT 97
FT /note="Y -> C (in dbSNP:rs16948986)"
FT /id="VAR_057373"
FT VARIANT 159
FT /note="R -> Q (in dbSNP:rs2072279)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8078902,
FT ECO:0000269|PubMed:9177788, ECO:0000269|Ref.4"
FT /id="VAR_060233"
FT VARIANT 196
FT /note="T -> K (in MC4DN3; dbSNP:rs104894555)"
FT /evidence="ECO:0000269|PubMed:12928484"
FT /id="VAR_026562"
FT VARIANT 204
FT /note="N -> K (in MC4DN3; dbSNP:rs104894560)"
FT /evidence="ECO:0000269|PubMed:10767350"
FT /id="VAR_026563"
FT VARIANT 225
FT /note="P -> L (in MC4DN3; dbSNP:rs104894556)"
FT /evidence="ECO:0000269|PubMed:12928484"
FT /id="VAR_026564"
FT VARIANT 258
FT /note="L -> H (in dbSNP:rs587780911)"
FT /evidence="ECO:0000269|PubMed:21248752"
FT /id="VAR_064768"
FT VARIANT 288
FT /note="G -> R (in MC4DN3; dbSNP:rs753048807)"
FT /evidence="ECO:0000269|PubMed:26741492"
FT /id="VAR_076181"
FT VARIANT 336
FT /note="D -> G (in MC4DN3; dbSNP:rs104894557)"
FT /evidence="ECO:0000269|PubMed:12928484"
FT /id="VAR_026565"
FT VARIANT 336
FT /note="D -> V (in MC4DN3; dbSNP:rs104894557)"
FT /evidence="ECO:0000269|PubMed:12928484"
FT /id="VAR_026566"
FT VARIANT 340
FT /note="G -> D (in dbSNP:rs1050214)"
FT /evidence="ECO:0000269|PubMed:8078902"
FT /id="VAR_060234"
FT VARIANT 420
FT /note="P -> L (in MC4DN3; dbSNP:rs773079584)"
FT /evidence="ECO:0000269|PubMed:26741492"
FT /id="VAR_076182"
FT CONFLICT 303
FT /note="A -> T (in Ref. 1; AAA21148)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="Y -> H (in Ref. 1; AAA21148)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 443 AA; 48910 MW; EC39E8D8966F4094 CRC64;
MAASPHTLSS RLLTGCVGGS VWYLERRTIQ DSPHKFLHLL RNVNKQWITF QHFSFLKRMY
VTQLNRSHNQ QVRPKPEPVA SPFLEKTSSG QAKAEIYEMR PLSPPSLSLS RKPNEKELIE
LEPDSVIEDS IDVGKETKEE KRWKEMKLQV YDLPGILARL SKIKLTALVV STTAAGFALA
PGPFDWPCFL LTSVGTGLAS CAANSINQFF EVPFDSNMNR TKNRPLVRGQ ISPLLAVSFA
TCCAVPGVAI LTLGVNPLTG ALGLFNIFLY TCCYTPLKRI SIANTWVGAV VGAIPPVMGW
TAATGSLDAG AFLLGGILYS WQFPHFNALS WGLREDYSRG GYCMMSVTHP GLCRRVALRH
CLALLVLSAA APVLDITTWT FPIMALPINA YISYLGFRFY VDADRRSSRR LFFCSLWHLP
LLLLLMLTCK RPSGGGDAGP PPS
