ORNT1_HUMAN
ID ORNT1_HUMAN Reviewed; 301 AA.
AC Q9Y619; Q5VZD8; Q9HC45;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Mitochondrial ornithine transporter 1;
DE AltName: Full=Solute carrier family 25 member 15;
GN Name=SLC25A15; Synonyms=ORC1 {ECO:0000303|PubMed:12807890}, ORNT1;
GN ORFNames=SP1855;
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], AND VARIANTS HHHS LYS-180 AND PHE-188 DEL.
RX PubMed=10369256; DOI=10.1038/9658;
RA Camacho J.A., Obie C., Biery B., Goodman B.K., Hu A., Almashanu S.,
RA Steel G., Casey R., Lombard M., Mitchell G.A., Valle D.;
RT "Hyperornithinaemia-hyperammonaemia-homocitrullinuria syndrome is caused by
RT mutations in a gene encoding a mitochondrial ornithine transporter.";
RL Nat. Genet. 22:151-158(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
RP CHARACTERIZATION OF VARIANTS HHHS ARG-27; PHE-188 DEL; ASP-190 AND GLN-275.
RX PubMed=12807890; DOI=10.1074/jbc.m302317200;
RA Fiermonte G., Dolce V., David L., Santorelli F.M., Dionisi-Vici C.,
RA Palmieri F., Walker J.E.;
RT "The mitochondrial ornithine transporter. Bacterial expression,
RT reconstitution, functional characterization, and tissue distribution of two
RT human isoforms.";
RL J. Biol. Chem. 278:32778-32783(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 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 [8]
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 [9]
RP VARIANT HHHS GLU-27.
RX PubMed=10805333;
RX DOI=10.1002/1531-8249(200005)47:5<625::aid-ana10>3.0.co;2-q;
RA Tsujino S., Kanazawa N., Ohashi T., Eto Y., Saito T., Kira J., Yamada T.;
RT "Three novel mutations (G27E, insAAC, R179X) in the ORNT1 gene of Japanese
RT patients with hyperornithinemia, hyperammonemia, and homocitrullinuria
RT syndrome.";
RL Ann. Neurol. 47:625-631(2000).
RN [10]
RP VARIANTS HHHS ARG-27; PHE-188 DEL; ASP-190 AND GLN-275.
RX PubMed=11668643; DOI=10.1002/humu.1221;
RA Salvi S., Dionisi-Vici C., Bertini E., Verardo M., Santorelli F.M.;
RT "Seven novel mutations in the ORNT1 gene (SLC25A15) in patients with
RT hyperornithinemia, hyperammonemia, and homocitrullinuria syndrome.";
RL Hum. Mutat. 18:460-460(2001).
RN [11]
RP VARIANTS HHHS ARG-27; PHE-188 DEL; ASP-190 AND GLN-275.
RX PubMed=11552031; DOI=10.1212/wnl.57.5.911;
RA Salvi S., Santorelli F.M., Bertini E., Boldrini R., Meli C., Donati A.,
RA Burlina A.B., Rizzo C., Di Capua M., Fariello G., Dionisi-Vici C.;
RT "Clinical and molecular findings in hyperornithinemia-hyperammonemia-
RT homocitrullinuria syndrome.";
RL Neurology 57:911-914(2001).
RN [12]
RP VARIANT HHHS ARG-126.
RX PubMed=11814739; DOI=10.1016/s0887-8994(01)00335-6;
RA Miyamoto T., Kanazawa N., Hayakawa C., Tsujino S.;
RT "A novel mutation, P126R, in a Japanese patient with HHH syndrome.";
RL Pediatr. Neurol. 26:65-67(2002).
RN [13]
RP VARIANTS HHHS CYS-113 AND LYS-273.
RX PubMed=16601889; DOI=10.1007/s10545-006-0120-7;
RA Fecarotta S., Parenti G., Vajro P., Zuppaldi A., Della Casa R.,
RA Carbone M.T., Correra A., Torre G., Riva S., Dionisi-Vici C.,
RA Santorelli F.M., Andria G.;
RT "HHH syndrome (hyperornithinaemia, hyperammonaemia, homocitrullinuria),
RT with fulminant hepatitis-like presentation.";
RL J. Inherit. Metab. Dis. 29:186-189(2006).
RN [14]
RP VARIANTS HHHS ARG-27; ARG-37; LEU-70; GLN-71; LEU-188; SER-216; ILE-272 AND
RP PHE-283, AND CHARACTERIZATION OF VARIANTS HHHS ARG-37; GLN-71; CYS-113;
RP ILE-272; LYS-273 AND PHE-283.
RX PubMed=19242930; DOI=10.1002/humu.20930;
RA Tessa A., Fiermonte G., Dionisi-Vici C., Paradies E., Baumgartner M.R.,
RA Chien Y.-H., Loguercio C., de Baulny H.O., Nassogne M.-C., Schiff M.,
RA Deodato F., Parenti G., Rutledge S.L., Vilaseca M.A., Melone M.A.B.,
RA Scarano G., Aldamiz-Echevarria L., Besley G., Walter J.,
RA Martinez-Hernandez E., Hernandez J.M., Pierri C.L., Palmieri F.,
RA Santorelli F.M.;
RT "Identification of novel mutations in the SLC25A15 gene in
RT hyperornithinemia-hyperammonemia-homocitrullinuria (HHH) syndrome: a
RT clinical, molecular, and functional study.";
RL Hum. Mutat. 30:741-748(2009).
CC -!- FUNCTION: Ornithine-citrulline antiporter. Connects the cytosolic and
CC the intramitochondrial reactions of the urea cycle by exchanging
CC cytosolic ornithine with matrix citrulline (PubMed:12807890). The
CC stoichiometry is close to 1:1 (By similarity).
CC {ECO:0000250|UniProtKB:A0A0G2K309, ECO:0000269|PubMed:12807890}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:A0A0G2K309}.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver, pancreas, testis, lung
CC and small intestine. Lower levels are detected in spleen, kidney, brain
CC and heart. {ECO:0000269|PubMed:12807890}.
CC -!- DISEASE: Hyperornithinemia-hyperammonemia-homocitrullinuria syndrome
CC (HHHS) [MIM:238970]: An autosomal recessive disorder of the urea cycle
CC characterized by onset in early life. The acute phase of the disease is
CC characterized by vomiting, ataxia, lethargy, confusion, and coma.
CC Chronic clinical manifestations include hypotonia, developmental delay,
CC progressive encephalopathy with mental regression, and spastic
CC paraparesis with pyramidal signs. {ECO:0000269|PubMed:10369256,
CC ECO:0000269|PubMed:10805333, ECO:0000269|PubMed:11552031,
CC ECO:0000269|PubMed:11668643, ECO:0000269|PubMed:11814739,
CC ECO:0000269|PubMed:12807890, ECO:0000269|PubMed:16601889,
CC ECO:0000269|PubMed:19242930}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; AF112968; AAD45238.1; -; mRNA.
DR EMBL; AJ309943; CAC83972.1; -; Genomic_DNA.
DR EMBL; AF177333; AAG17977.1; -; mRNA.
DR EMBL; AL161614; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08630.1; -; Genomic_DNA.
DR EMBL; BC002702; AAH02702.1; -; mRNA.
DR CCDS; CCDS9373.1; -.
DR RefSeq; NP_055067.1; NM_014252.3.
DR AlphaFoldDB; Q9Y619; -.
DR SMR; Q9Y619; -.
DR BioGRID; 115468; 89.
DR IntAct; Q9Y619; 10.
DR STRING; 9606.ENSP00000342267; -.
DR DrugBank; DB00129; Ornithine.
DR TCDB; 2.A.29.19.2; the mitochondrial carrier (mc) family.
DR GlyGen; Q9Y619; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y619; -.
DR PhosphoSitePlus; Q9Y619; -.
DR SwissPalm; Q9Y619; -.
DR BioMuta; SLC25A15; -.
DR DMDM; 20139303; -.
DR EPD; Q9Y619; -.
DR jPOST; Q9Y619; -.
DR MassIVE; Q9Y619; -.
DR MaxQB; Q9Y619; -.
DR PaxDb; Q9Y619; -.
DR PeptideAtlas; Q9Y619; -.
DR PRIDE; Q9Y619; -.
DR ProteomicsDB; 86587; -.
DR Antibodypedia; 42171; 81 antibodies from 20 providers.
DR DNASU; 10166; -.
DR Ensembl; ENST00000338625.9; ENSP00000342267.4; ENSG00000102743.15.
DR GeneID; 10166; -.
DR KEGG; hsa:10166; -.
DR MANE-Select; ENST00000338625.9; ENSP00000342267.4; NM_014252.4; NP_055067.1.
DR UCSC; uc001uxn.4; human.
DR CTD; 10166; -.
DR DisGeNET; 10166; -.
DR GeneCards; SLC25A15; -.
DR GeneReviews; SLC25A15; -.
DR HGNC; HGNC:10985; SLC25A15.
DR HPA; ENSG00000102743; Tissue enhanced (intestine, liver, pancreas).
DR MalaCards; SLC25A15; -.
DR MIM; 238970; phenotype.
DR MIM; 603861; gene.
DR neXtProt; NX_Q9Y619; -.
DR OpenTargets; ENSG00000102743; -.
DR Orphanet; 415; Hyperornithinemia-hyperammonemia-homocitrullinuria syndrome.
DR PharmGKB; PA35861; -.
DR VEuPathDB; HostDB:ENSG00000102743; -.
DR eggNOG; KOG0763; Eukaryota.
DR GeneTree; ENSGT00730000110966; -.
DR HOGENOM; CLU_015166_16_3_1; -.
DR InParanoid; Q9Y619; -.
DR OMA; PIDCFRQ; -.
DR OrthoDB; 1072378at2759; -.
DR PhylomeDB; Q9Y619; -.
DR TreeFam; TF314880; -.
DR PathwayCommons; Q9Y619; -.
DR Reactome; R-HSA-70635; Urea cycle.
DR SABIO-RK; Q9Y619; -.
DR SignaLink; Q9Y619; -.
DR BioGRID-ORCS; 10166; 12 hits in 1081 CRISPR screens.
DR ChiTaRS; SLC25A15; human.
DR GenomeRNAi; 10166; -.
DR Pharos; Q9Y619; Tbio.
DR PRO; PR:Q9Y619; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9Y619; protein.
DR Bgee; ENSG00000102743; Expressed in liver and 137 other tissues.
DR ExpressionAtlas; Q9Y619; baseline and differential.
DR Genevisible; Q9Y619; HS.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0015297; F:antiporter activity; IDA:UniProtKB.
DR GO; GO:0061459; F:L-arginine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015189; F:L-lysine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0000064; F:L-ornithine transmembrane transporter activity; EXP:Reactome.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1903826; P:L-arginine transmembrane transport; IDA:UniProtKB.
DR GO; GO:1903401; P:L-lysine transmembrane transport; IDA:UniProtKB.
DR GO; GO:1990575; P:mitochondrial L-ornithine transmembrane transport; IBA:GO_Central.
DR GO; GO:0000050; P:urea cycle; TAS:Reactome.
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; 3.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Disease variant; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..301
FT /note="Mitochondrial ornithine transporter 1"
FT /id="PRO_0000090650"
FT TRANSMEM 5..25
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 7..91
FT /note="Solcar 1"
FT REPEAT 104..197
FT /note="Solcar 2"
FT REPEAT 207..293
FT /note="Solcar 3"
FT VARIANT 27
FT /note="G -> E (in HHHS; dbSNP:rs1208994024)"
FT /evidence="ECO:0000269|PubMed:10805333"
FT /id="VAR_012757"
FT VARIANT 27
FT /note="G -> R (in HHHS; incapable of catalyzing homo-
FT exchanges of ornithine, arginine, lysine and citrulline;
FT dbSNP:rs104894430)"
FT /evidence="ECO:0000269|PubMed:11552031,
FT ECO:0000269|PubMed:11668643, ECO:0000269|PubMed:12807890,
FT ECO:0000269|PubMed:19242930"
FT /id="VAR_012758"
FT VARIANT 37
FT /note="M -> R (in HHHS; exhibits very low transport
FT activity despite normal insertion in the liposomal
FT membrane; dbSNP:rs121908533)"
FT /evidence="ECO:0000269|PubMed:19242930"
FT /id="VAR_058948"
FT VARIANT 70
FT /note="A -> L (in HHHS; requires 2 nucleotide
FT substitutions; unknown pathological significance;
FT dbSNP:rs1064793683)"
FT /evidence="ECO:0000269|PubMed:19242930"
FT /id="VAR_058949"
FT VARIANT 71
FT /note="L -> Q (in HHHS; exhibits very low transport
FT activity despite normal insertion in the liposomal
FT membrane; dbSNP:rs121908534)"
FT /evidence="ECO:0000269|PubMed:19242930"
FT /id="VAR_058950"
FT VARIANT 113
FT /note="G -> C (in HHHS; exhibits very low transport
FT activity despite normal insertion in the liposomal
FT membrane; dbSNP:rs199894905)"
FT /evidence="ECO:0000269|PubMed:16601889,
FT ECO:0000269|PubMed:19242930"
FT /id="VAR_058951"
FT VARIANT 126
FT /note="P -> R (in HHHS)"
FT /evidence="ECO:0000269|PubMed:11814739"
FT /id="VAR_012759"
FT VARIANT 180
FT /note="E -> K (in HHHS; dbSNP:rs104894424)"
FT /evidence="ECO:0000269|PubMed:10369256"
FT /id="VAR_012760"
FT VARIANT 188
FT /note="F -> L (in HHHS; dbSNP:rs141028076)"
FT /evidence="ECO:0000269|PubMed:19242930"
FT /id="VAR_058952"
FT VARIANT 188
FT /note="Missing (in HHHS; maintains a residual transport
FT activity of 10%; dbSNP:rs202247803)"
FT /evidence="ECO:0000269|PubMed:10369256,
FT ECO:0000269|PubMed:11552031, ECO:0000269|PubMed:11668643,
FT ECO:0000269|PubMed:12807890"
FT /id="VAR_012761"
FT VARIANT 190
FT /note="G -> D (in HHHS; maintains a residual transport
FT activity of 35%; dbSNP:rs202247804)"
FT /evidence="ECO:0000269|PubMed:11552031,
FT ECO:0000269|PubMed:11668643, ECO:0000269|PubMed:12807890"
FT /id="VAR_012762"
FT VARIANT 216
FT /note="G -> S (in HHHS; dbSNP:rs1417167600)"
FT /evidence="ECO:0000269|PubMed:19242930"
FT /id="VAR_058953"
FT VARIANT 254
FT /note="I -> L (in dbSNP:rs17849654)"
FT /id="VAR_012763"
FT VARIANT 272
FT /note="T -> I (in HHHS; exhibits very low transport
FT activity despite normal insertion in the liposomal
FT membrane; dbSNP:rs121908535)"
FT /evidence="ECO:0000269|PubMed:19242930"
FT /id="VAR_058954"
FT VARIANT 273
FT /note="M -> K (in HHHS; exhibits very low transport
FT activity despite normal insertion in the liposomal
FT membrane; dbSNP:rs202247808)"
FT /evidence="ECO:0000269|PubMed:16601889,
FT ECO:0000269|PubMed:19242930"
FT /id="VAR_058955"
FT VARIANT 275
FT /note="R -> Q (in HHHS; dbSNP:rs104894431)"
FT /evidence="ECO:0000269|PubMed:11552031,
FT ECO:0000269|PubMed:11668643, ECO:0000269|PubMed:12807890"
FT /id="VAR_012764"
FT VARIANT 283
FT /note="L -> F (in HHHS; exhibits very low transport
FT activity despite normal insertion in the liposomal
FT membrane; dbSNP:rs202247809)"
FT /evidence="ECO:0000269|PubMed:19242930"
FT /id="VAR_058956"
SQ SEQUENCE 301 AA; 32736 MW; 34436A15B105DC53 CRC64;
MKSNPAIQAA IDLTAGAAGG TACVLTGQPF DTMKVKMQTF PDLYRGLTDC CLKTYSQVGF
RGFYKGTSPA LIANIAENSV LFMCYGFCQQ VVRKVAGLDK QAKLSDLQNA AAGSFASAFA
ALVLCPTELV KCRLQTMYEM ETSGKIAKSQ NTVWSVIKSI LRKDGPLGFY HGLSSTLLRE
VPGYFFFFGG YELSRSFFAS GRSKDELGPV PLMLSGGVGG ICLWLAVYPV DCIKSRIQVL
SMSGKQAGFI RTFINVVKNE GITALYSGLK PTMIRAFPAN GALFLAYEYS RKLMMNQLEA
Y
