CP2CI_HUMAN
ID CP2CI_HUMAN Reviewed; 490 AA.
AC P33260; B2R8K2; Q16703; Q16751; Q4VAT5; Q6GRG1;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 3.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Cytochrome P450 2C18;
DE EC=1.14.14.1 {ECO:0000269|PubMed:11093772};
DE AltName: Full=CYPIIC18;
DE AltName: Full=Cytochrome P450-6b/29c;
DE Flags: Precursor;
GN Name=CYP2C18 {ECO:0000303|PubMed:11093772, ECO:0000312|HGNC:HGNC:2620};
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 VARIANT MET-385.
RC TISSUE=Liver;
RX PubMed=2009263; DOI=10.1021/bi00227a012;
RA Romkes M., Faletto M.B., Blaisdell J.A., Raucy J.L., Goldstein J.A.;
RT "Cloning and expression of complementary DNAs for multiple members of the
RT human cytochrome P450IIC subfamily.";
RL Biochemistry 30:3247-3255(1991).
RN [2]
RP ERRATUM OF PUBMED:2009263, AND SEQUENCE REVISION.
RX PubMed=8095407; DOI=10.1021/bi00056a025;
RA Romkes M., Faletto M.B., Blaisdell J.A., Raucy J.L., Goldstein J.A.;
RL Biochemistry 32:1390-1390(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-385.
RC TISSUE=Liver;
RX PubMed=8333835; DOI=10.1006/bbrc.1993.1803;
RA de Morais S.M., Schweikl H., Blaisdell J., Goldstein J.A.;
RT "Gene structure and upstream regulatory regions of human CYP2C9 and
RT CYP2C18.";
RL Biochem. Biophys. Res. Commun. 194:194-201(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Stomach;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND PATHWAY.
RX PubMed=11093772; DOI=10.1124/mol.58.6.1341;
RA Marill J., Cresteil T., Lanotte M., Chabot G.G.;
RT "Identification of human cytochrome P450s involved in the formation of all-
RT trans-retinoic acid principal metabolites.";
RL Mol. Pharmacol. 58:1341-1348(2000).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 72-80.
RX PubMed=16963442; DOI=10.1074/jbc.m606755200;
RA Archbold J.K., Macdonald W.A., Miles J.J., Brennan R.M., Kjer-Nielsen L.,
RA McCluskey J., Burrows S.R., Rossjohn J.;
RT "Alloreactivity between disparate cognate and allogeneic pMHC-I complexes
RT is the result of highly focused, peptide-dependent structural mimicry.";
RL J. Biol. Chem. 281:34324-34332(2006).
CC -!- FUNCTION: A cytochrome P450 monooxygenase involved in retinoid
CC metabolism. Hydroxylates all trans-retinoic acid (atRA) to 4-
CC hydroxyretinoate and may modulate atRA signaling and clearance.
CC Mechanistically, uses molecular oxygen inserting one oxygen atom into a
CC substrate, and reducing the second into a water molecule, with two
CC electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-
CC ferrihemoprotein reductase). {ECO:0000269|PubMed:11093772}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein
CC reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:142491; EC=1.14.14.1;
CC Evidence={ECO:0000269|PubMed:11093772};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17150;
CC Evidence={ECO:0000305|PubMed:11093772};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = all-trans-4-hydroxyretinoate + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:51984, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:35291,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:134178;
CC Evidence={ECO:0000269|PubMed:11093772};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51985;
CC Evidence={ECO:0000305|PubMed:11093772};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16 uM for all-trans-retinoate {ECO:0000269|PubMed:11093772};
CC Vmax=251 pmol/min/nmol enzyme toward all-trans-retinoate
CC {ECO:0000269|PubMed:11093772};
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC {ECO:0000269|PubMed:11093772}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11093772}; Peripheral membrane protein. Microsome
CC membrane {ECO:0000269|PubMed:11093772}; Peripheral membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P33260-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P33260-2; Sequence=VSP_042520;
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; M61853; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M61856; AAB59356.1; -; mRNA.
DR EMBL; L16876; AAA02630.1; -; Genomic_DNA.
DR EMBL; L16871; AAA02630.1; JOINED; Genomic_DNA.
DR EMBL; L16872; AAA02630.1; JOINED; Genomic_DNA.
DR EMBL; L16869; AAA02630.1; JOINED; Genomic_DNA.
DR EMBL; L16870; AAA02630.1; JOINED; Genomic_DNA.
DR EMBL; L16875; AAA02630.1; JOINED; Genomic_DNA.
DR EMBL; L16873; AAA02630.1; JOINED; Genomic_DNA.
DR EMBL; L16874; AAA02630.1; JOINED; Genomic_DNA.
DR EMBL; AK313403; BAG36199.1; -; mRNA.
DR EMBL; AL583836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW50024.1; -; Genomic_DNA.
DR EMBL; BC069666; AAH69666.1; -; mRNA.
DR EMBL; BC096257; AAH96257.1; -; mRNA.
DR EMBL; BC096258; AAH96258.1; -; mRNA.
DR EMBL; BC096260; AAH96260.1; -; mRNA.
DR CCDS; CCDS44460.1; -. [P33260-2]
DR CCDS; CCDS7435.1; -. [P33260-1]
DR PIR; A61269; A61269.
DR RefSeq; NP_000763.1; NM_000772.2. [P33260-1]
DR RefSeq; NP_001122397.1; NM_001128925.1. [P33260-2]
DR PDB; 2CIK; X-ray; 1.75 A; C=72-80.
DR PDB; 2H6P; X-ray; 1.90 A; C=72-80.
DR PDBsum; 2CIK; -.
DR PDBsum; 2H6P; -.
DR AlphaFoldDB; P33260; -.
DR SMR; P33260; -.
DR BioGRID; 107938; 30.
DR IntAct; P33260; 6.
DR STRING; 9606.ENSP00000285979; -.
DR BindingDB; P33260; -.
DR ChEMBL; CHEMBL2408; -.
DR DrugBank; DB08496; (R)-warfarin.
DR DrugBank; DB14055; (S)-Warfarin.
DR DrugBank; DB01424; Aminophenazone.
DR DrugBank; DB01435; Antipyrine.
DR DrugBank; DB00921; Buprenorphine.
DR DrugBank; DB00349; Clobazam.
DR DrugBank; DB01559; Clotiazepam.
DR DrugBank; DB00531; Cyclophosphamide.
DR DrugBank; DB00250; Dapsone.
DR DrugBank; DB00829; Diazepam.
DR DrugBank; DB00586; Diclofenac.
DR DrugBank; DB09166; Etizolam.
DR DrugBank; DB00986; Glycopyrronium.
DR DrugBank; DB01181; Ifosfamide.
DR DrugBank; DB00458; Imipramine.
DR DrugBank; DB11757; Istradefylline.
DR DrugBank; DB00448; Lansoprazole.
DR DrugBank; DB00333; Methadone.
DR DrugBank; DB07670; N,4-Dimethyl-N-(1-phenyl-1H-pyrazol-5-yl)benzenesulfonamide.
DR DrugBank; DB01183; Naloxone.
DR DrugBank; DB00338; Omeprazole.
DR DrugBank; DB00850; Perphenazine.
DR DrugBank; DB01174; Phenobarbital.
DR DrugBank; DB00252; Phenytoin.
DR DrugBank; DB00818; Propofol.
DR DrugBank; DB01124; Tolbutamide.
DR DrugBank; DB00755; Tretinoin.
DR DrugBank; DB00661; Verapamil.
DR DrugBank; DB00682; Warfarin.
DR GuidetoPHARMACOLOGY; 1327; -.
DR SwissLipids; SLP:000001875; -.
DR iPTMnet; P33260; -.
DR PhosphoSitePlus; P33260; -.
DR BioMuta; CYP2C18; -.
DR DMDM; 67476954; -.
DR MassIVE; P33260; -.
DR PaxDb; P33260; -.
DR PeptideAtlas; P33260; -.
DR PRIDE; P33260; -.
DR ProteomicsDB; 54905; -. [P33260-1]
DR ProteomicsDB; 54906; -. [P33260-2]
DR Antibodypedia; 30592; 109 antibodies from 22 providers.
DR DNASU; 1562; -.
DR Ensembl; ENST00000285979.11; ENSP00000285979.6; ENSG00000108242.13. [P33260-1]
DR Ensembl; ENST00000339022.6; ENSP00000341293.5; ENSG00000108242.13. [P33260-2]
DR GeneID; 1562; -.
DR KEGG; hsa:1562; -.
DR MANE-Select; ENST00000285979.11; ENSP00000285979.6; NM_000772.3; NP_000763.1.
DR UCSC; uc001kjv.6; human. [P33260-1]
DR CTD; 1562; -.
DR DisGeNET; 1562; -.
DR GeneCards; CYP2C18; -.
DR HGNC; HGNC:2620; CYP2C18.
DR HPA; ENSG00000108242; Tissue enhanced (intestine, liver, stomach).
DR MIM; 601131; gene.
DR neXtProt; NX_P33260; -.
DR OpenTargets; ENSG00000108242; -.
DR PharmGKB; PA127; -.
DR VEuPathDB; HostDB:ENSG00000108242; -.
DR eggNOG; KOG0156; Eukaryota.
DR GeneTree; ENSGT00940000162913; -.
DR HOGENOM; CLU_001570_22_0_1; -.
DR InParanoid; P33260; -.
DR OMA; HTLAPMG; -.
DR OrthoDB; 1591226at2759; -.
DR PhylomeDB; P33260; -.
DR TreeFam; TF352043; -.
DR PathwayCommons; P33260; -.
DR Reactome; R-HSA-211981; Xenobiotics.
DR SABIO-RK; P33260; -.
DR SignaLink; P33260; -.
DR UniPathway; UPA00912; -.
DR BioGRID-ORCS; 1562; 16 hits in 1065 CRISPR screens.
DR ChiTaRS; CYP2C18; human.
DR EvolutionaryTrace; P33260; -.
DR GeneWiki; CYP2C18; -.
DR GenomeRNAi; 1562; -.
DR Pharos; P33260; Tchem.
DR PRO; PR:P33260; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P33260; protein.
DR Bgee; ENSG00000108242; Expressed in jejunal mucosa and 79 other tissues.
DR Genevisible; P33260; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0008392; F:arachidonic acid epoxygenase activity; IBA:GO_Central.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0071614; F:linoleic acid epoxygenase activity; IEA:Ensembl.
DR GO; GO:0004497; F:monooxygenase activity; TAS:Reactome.
DR GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
DR GO; GO:0019825; F:oxygen binding; TAS:ProtInc.
DR GO; GO:0008401; F:retinoic acid 4-hydroxylase activity; IDA:UniProtKB.
DR GO; GO:0008395; F:steroid hydroxylase activity; IBA:GO_Central.
DR GO; GO:0019373; P:epoxygenase P450 pathway; IBA:GO_Central.
DR GO; GO:0043651; P:linoleic acid metabolic process; IEA:Ensembl.
DR GO; GO:0006082; P:organic acid metabolic process; IBA:GO_Central.
DR GO; GO:0042573; P:retinoic acid metabolic process; IDA:UniProtKB.
DR GO; GO:0042572; P:retinol metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Endoplasmic reticulum; Heme; Iron;
KW Lipid metabolism; Membrane; Metal-binding; Microsome; Monooxygenase;
KW Oxidoreductase; Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..490
FT /note="Cytochrome P450 2C18"
FT /evidence="ECO:0000255"
FT /id="PRO_0000051707"
FT BINDING 435
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT VAR_SEQ 214..272
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042520"
FT VARIANT 385
FT /note="T -> M (in dbSNP:rs1126545)"
FT /evidence="ECO:0000269|PubMed:2009263,
FT ECO:0000269|PubMed:8333835"
FT /id="VAR_001254"
SQ SEQUENCE 490 AA; 55711 MW; C933CF31F078FD1E CRC64;
MDPAVALVLC LSCLFLLSLW RQSSGRGRLP SGPTPLPIIG NILQLDVKDM SKSLTNFSKV
YGPVFTVYFG LKPIVVLHGY EAVKEALIDH GEEFSGRGSF PVAEKVNKGL GILFSNGKRW
KEIRRFCLMT LRNFGMGKRS IEDRVQEEAR CLVEELRKTN ASPCDPTFIL GCAPCNVICS
VIFHDRFDYK DQRFLNLMEK FNENLRILSS PWIQVCNNFP ALIDYLPGSH NKIAENFAYI
KSYVLERIKE HQESLDMNSA RDFIDCFLIK MEQEKHNQQS EFTVESLIAT VTDMFGAGTE
TTSTTLRYGL LLLLKYPEVT AKVQEEIECV VGRNRSPCMQ DRSHMPYTDA VVHEIQRYID
LLPTNLPHAV TCDVKFKNYL IPKGTTIITS LTSVLHNDKE FPNPEMFDPG HFLDKSGNFK
KSDYFMPFSA GKRMCMGEGL ARMELFLFLT TILQNFNLKS QVDPKDIDIT PIANAFGRVP
PLYQLCFIPV
