CP2AD_HUMAN
ID CP2AD_HUMAN Reviewed; 494 AA.
AC Q16696; Q53YR8; Q6R569; Q6R570; Q9H2X2;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 3.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Cytochrome P450 2A13;
DE EC=1.14.14.1;
DE AltName: Full=CYPIIA13;
GN Name=CYP2A13;
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 [GENOMIC DNA].
RX PubMed=7668294;
RA Fernandez-Salguero P., Hoffman S.M., Cholerton S., Mohrenweiser H.,
RA Raunio H., Rautio A., Pelkonen O., Huang J.D., Evans W.E., Idle J.R.;
RT "A genetic polymorphism in coumarin 7-hydroxylation: sequence of the human
RT CYP2A genes and identification of variant CYP2A6 alleles.";
RL Am. J. Hum. Genet. 57:651-660(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND TISSUE SPECIFICITY.
RX PubMed=11016631;
RA Su T., Bao Z., Zhang Q.Y., Smith T.J., Hong J.Y., Ding X.;
RT "Human cytochrome P450 CYP2A13: predominant expression in the respiratory
RT tract and its high efficiency metabolic activation of a tobacco-specific
RT carcinogen, 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone.";
RL Cancer Res. 60:5074-5079(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS GLU-158 AND LEU-323.
RX PubMed=15063809; DOI=10.1016/j.bbrc.2004.03.092;
RA Cauffiez C., Lo-Guidice J.-M., Quaranta S., Allorge D., Chevalier D.,
RA Cenee S., Hamdan R., Lhermitte M., Lafitte J.-J., Libersa C.,
RA Colombel J.-F., Stuecker I., Broly F.;
RT "Genetic polymorphism of the human cytochrome CYP2A13 in a French
RT population: implication in lung cancer susceptibility.";
RL Biochem. Biophys. Res. Commun. 317:662-669(2004).
RN [4]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF LEU-110;
RP ALA-117; SER-208; ALA-213; PHE-300; ALA-301; MET-365; LEU-366; GLY-369 AND
RP HIS-372.
RX PubMed=18779312; DOI=10.1124/dmd.108.023770;
RA DeVore N.M., Smith B.D., Urban M.J., Scott E.E.;
RT "Key residues controlling phenacetin metabolism by human cytochrome P450 2A
RT enzymes.";
RL Drug Metab. Dispos. 36:2582-2590(2008).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 29-494 IN COMPLEX WITH HEME.
RX PubMed=17540336; DOI=10.1016/j.abb.2007.04.028;
RA Sansen S., Hsu M.H., Stout C.D., Johnson E.F.;
RT "Structural insight into the altered substrate specificity of human
RT cytochrome P450 2A6 mutants.";
RL Arch. Biochem. Biophys. 464:197-206(2007).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 31-494 IN COMPLEX WITH SUBSTRATE
RP ANALOG AND HEME.
RX PubMed=17428784; DOI=10.1074/jbc.m702361200;
RA Smith B.D., Sanders J.L., Porubsky P.R., Lushington G.H., Stout C.D.,
RA Scott E.E.;
RT "Structure of the human lung cytochrome P450 2A13.";
RL J. Biol. Chem. 282:17306-17313(2007).
RN [7]
RP VARIANT CYS-257.
RX PubMed=12130698; DOI=10.1124/jpet.302.2.416;
RA Zhang X., Su T., Zhang Q.Y., Gu J., Caggana M., Li H., Ding X.;
RT "Genetic polymorphisms of the human CYP2A13 gene: identification of single-
RT nucleotide polymorphisms and functional characterization of an Arg257Cys
RT variant.";
RL J. Pharmacol. Exp. Ther. 302:416-423(2002).
RN [8]
RP VARIANTS GLN-25; GLN-101; THR-134 INS; GLU-158; TYR-453 AND CYS-494.
RX PubMed=15618722; DOI=10.2133/dmpk.18.86;
RA Fujieda M., Yamazaki H., Kiyotani K., Muroi A., Kunitoh H.,
RA Dosaka-Akita H., Sawamura Y., Kamataki T.;
RT "Eighteen novel polymorphisms of the CYP2A13 gene in Japanese.";
RL Drug Metab. Pharmacokinet. 18:86-90(2003).
RN [9]
RP VARIANTS GLN-25 AND CYS-257.
RX PubMed=12721789; DOI=10.1007/s10038-003-0021-7;
RA Saito S., Iida A., Sekine A., Kawauchi S., Higuchi S., Ogawa C.,
RA Nakamura Y.;
RT "Catalog of 680 variations among eight cytochrome p450 (CYP) genes, nine
RT esterase genes, and two other genes in the Japanese population.";
RL J. Hum. Genet. 48:249-270(2003).
CC -!- FUNCTION: Exhibits a coumarin 7-hydroxylase activity. Active in the
CC metabolic activation of hexamethylphosphoramide, N,N-dimethylaniline,
CC 2'-methoxyacetophenone, N-nitrosomethylphenylamine, and the tobacco-
CC specific carcinogen, 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone.
CC Possesses phenacetin O-deethylation activity.
CC {ECO:0000269|PubMed:18779312}.
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 -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.7 uM for phenacetin {ECO:0000269|PubMed:18779312};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC membrane protein. Microsome membrane; Peripheral membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in liver and a number of extrahepatic
CC tissues, including nasal mucosa, lung, trachea, brain, mammary gland,
CC prostate, testis, and uterus, but not in heart, kidney, bone marrow,
CC colon, small intestine, spleen, stomach, thymus, or skeletal muscle.
CC {ECO:0000269|PubMed:11016631}.
CC -!- POLYMORPHISM: The frequencies of the Cys-257 allele in white, black,
CC Hispanic, and Asian individuals are 1.9%, 14.4%, 5.8%, and 7.7%,
CC respectively. The Cys-257 variant is 37 to 56% less active than the
CC wild-type Arg-257 protein toward all substrates tested.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=PharmVar Pharmacogen Variation Consortium;
CC Note=CYP2A13 alleles;
CC URL="https://www.pharmvar.org/gene/CYP2A13";
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DR EMBL; U22028; AAB40519.1; -; Genomic_DNA.
DR EMBL; AF209774; AAG35775.1; -; mRNA.
DR EMBL; AY513604; AAR90935.1; -; mRNA.
DR EMBL; AY513605; AAR90936.1; -; mRNA.
DR EMBL; AY513606; AAR90937.1; -; mRNA.
DR EMBL; AY513608; AAR90939.1; -; mRNA.
DR EMBL; AY513609; AAR90940.1; -; mRNA.
DR CCDS; CCDS12571.1; -.
DR PIR; I38966; I38966.
DR RefSeq; NP_000757.2; NM_000766.4.
DR PDB; 2P85; X-ray; 2.35 A; A/B/C/D/E/F=26-494.
DR PDB; 2PG5; X-ray; 1.95 A; A/B/C/D=31-494.
DR PDB; 2PG6; X-ray; 2.53 A; A/B/C/D=31-494.
DR PDB; 2PG7; X-ray; 2.80 A; A/B/C/D=31-494.
DR PDB; 3T3S; X-ray; 3.00 A; A/B/C/D/E/F/G/H=31-494.
DR PDB; 4EJG; X-ray; 2.50 A; A/B/C/D/E/F/G/H=31-494.
DR PDB; 4EJH; X-ray; 2.35 A; A/B/C/D/E/F/G/H=31-494.
DR PDB; 4EJI; X-ray; 2.10 A; A=31-494.
DR PDBsum; 2P85; -.
DR PDBsum; 2PG5; -.
DR PDBsum; 2PG6; -.
DR PDBsum; 2PG7; -.
DR PDBsum; 3T3S; -.
DR PDBsum; 4EJG; -.
DR PDBsum; 4EJH; -.
DR PDBsum; 4EJI; -.
DR AlphaFoldDB; Q16696; -.
DR SMR; Q16696; -.
DR BioGRID; 107931; 4.
DR IntAct; Q16696; 1.
DR STRING; 9606.ENSP00000332679; -.
DR BindingDB; Q16696; -.
DR ChEMBL; CHEMBL3542436; -.
DR DrugBank; DB00553; Methoxsalen.
DR DrugBank; DB00184; Nicotine.
DR DrugBank; DB03783; Phenacetin.
DR DrugBank; DB00624; Testosterone.
DR DrugBank; DB13943; Testosterone cypionate.
DR DrugBank; DB13944; Testosterone enanthate.
DR DrugBank; DB13946; Testosterone undecanoate.
DR GuidetoPHARMACOLOGY; 1323; -.
DR iPTMnet; Q16696; -.
DR PhosphoSitePlus; Q16696; -.
DR BioMuta; CYP2A13; -.
DR DMDM; 77416854; -.
DR EPD; Q16696; -.
DR MassIVE; Q16696; -.
DR PaxDb; Q16696; -.
DR PeptideAtlas; Q16696; -.
DR PRIDE; Q16696; -.
DR ProteomicsDB; 61036; -.
DR Antibodypedia; 17121; 183 antibodies from 30 providers.
DR DNASU; 1553; -.
DR Ensembl; ENST00000330436.4; ENSP00000332679.1; ENSG00000197838.5.
DR GeneID; 1553; -.
DR KEGG; hsa:1553; -.
DR MANE-Select; ENST00000330436.4; ENSP00000332679.1; NM_000766.5; NP_000757.2.
DR UCSC; uc002opt.5; human.
DR CTD; 1553; -.
DR DisGeNET; 1553; -.
DR GeneCards; CYP2A13; -.
DR HGNC; HGNC:2608; CYP2A13.
DR HPA; ENSG00000197838; Tissue enriched (liver).
DR MIM; 608055; gene.
DR neXtProt; NX_Q16696; -.
DR OpenTargets; ENSG00000197838; -.
DR PharmGKB; PA27101; -.
DR VEuPathDB; HostDB:ENSG00000197838; -.
DR eggNOG; KOG0156; Eukaryota.
DR GeneTree; ENSGT00940000154117; -.
DR HOGENOM; CLU_001570_22_3_1; -.
DR InParanoid; Q16696; -.
DR OMA; LMARILW; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; Q16696; -.
DR TreeFam; TF352043; -.
DR PathwayCommons; Q16696; -.
DR Reactome; R-HSA-211935; Fatty acids.
DR Reactome; R-HSA-211981; Xenobiotics.
DR Reactome; R-HSA-211999; CYP2E1 reactions.
DR Reactome; R-HSA-5423646; Aflatoxin activation and detoxification.
DR SABIO-RK; Q16696; -.
DR SignaLink; Q16696; -.
DR BioGRID-ORCS; 1553; 160 hits in 1063 CRISPR screens.
DR EvolutionaryTrace; Q16696; -.
DR GeneWiki; CYP2A13; -.
DR GenomeRNAi; 1553; -.
DR Pharos; Q16696; Tchem.
DR PRO; PR:Q16696; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q16696; protein.
DR Bgee; ENSG00000197838; Expressed in nasal cavity epithelium and 25 other tissues.
DR Genevisible; Q16696; 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; IBA:GO_Central.
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:0008389; F:coumarin 7-hydroxylase activity; TAS:Reactome.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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:0008395; F:steroid hydroxylase activity; IBA:GO_Central.
DR GO; GO:0046222; P:aflatoxin metabolic process; TAS:Reactome.
DR GO; GO:0009804; P:coumarin metabolic process; IBA:GO_Central.
DR GO; GO:0019373; P:epoxygenase P450 pathway; IBA:GO_Central.
DR GO; GO:0006082; P:organic acid metabolic process; IBA:GO_Central.
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; IPR008067; Cyt_P450_E_grp-I_CYP2A-like.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR01684; EP450ICYP2A.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding;
KW Microsome; Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..494
FT /note="Cytochrome P450 2A13"
FT /id="PRO_0000051676"
FT BINDING 297
FT /ligand="substrate"
FT BINDING 439
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 VARIANT 25
FT /note="R -> Q (in allele CYP2A13*2; dbSNP:rs8192784)"
FT /evidence="ECO:0000269|PubMed:12721789,
FT ECO:0000269|PubMed:15618722"
FT /id="VAR_018334"
FT VARIANT 101
FT /note="R -> Q (in allele CYP2A13*4; dbSNP:rs148044792)"
FT /evidence="ECO:0000269|PubMed:15618722"
FT /id="VAR_018335"
FT VARIANT 134
FT /note="T -> TT (in allele CYP2A13*3)"
FT /evidence="ECO:0000269|PubMed:15618722"
FT /id="VAR_018336"
FT VARIANT 158
FT /note="D -> E (in allele CYP2A13*3 and allele CYP2A13*8;
FT dbSNP:rs112337232)"
FT /evidence="ECO:0000269|PubMed:15063809,
FT ECO:0000269|PubMed:15618722"
FT /id="VAR_018337"
FT VARIANT 257
FT /note="R -> C (in allele CYP2A13*2; dbSNP:rs8192789)"
FT /evidence="ECO:0000269|PubMed:12130698,
FT ECO:0000269|PubMed:12721789"
FT /id="VAR_013835"
FT VARIANT 323
FT /note="V -> L (in allele CYP2A13*9)"
FT /evidence="ECO:0000269|PubMed:15063809"
FT /id="VAR_018356"
FT VARIANT 453
FT /note="F -> Y (in allele CYP2A13*5; dbSNP:rs72547590)"
FT /evidence="ECO:0000269|PubMed:15618722"
FT /id="VAR_018338"
FT VARIANT 494
FT /note="R -> C (in allele CYP2A13*6; dbSNP:rs138870349)"
FT /evidence="ECO:0000269|PubMed:15618722"
FT /id="VAR_018339"
FT MUTAGEN 110
FT /note="L->V: Decreases phenacetin O-deethylation activity 8
FT fold."
FT /evidence="ECO:0000269|PubMed:18779312"
FT MUTAGEN 117
FT /note="A->V: Increases phenacetin O-deethylation activity 5
FT fold."
FT /evidence="ECO:0000269|PubMed:18779312"
FT MUTAGEN 208
FT /note="S->I: Decreases phenacetin O-deethylation activity
FT 10 fold."
FT /evidence="ECO:0000269|PubMed:18779312"
FT MUTAGEN 213
FT /note="A->S: Decreases phenacetin O-deethylation activity 2
FT fold."
FT /evidence="ECO:0000269|PubMed:18779312"
FT MUTAGEN 300
FT /note="F->I: Decreases phenacetin O-deethylation activity
FT 40 fold."
FT /evidence="ECO:0000269|PubMed:18779312"
FT MUTAGEN 301
FT /note="A->G: Decreases phenacetin O-deethylation activity
FT 20 fold."
FT /evidence="ECO:0000269|PubMed:18779312"
FT MUTAGEN 365
FT /note="M->V: Decreases phenacetin O-deethylation activity 7
FT fold."
FT /evidence="ECO:0000269|PubMed:18779312"
FT MUTAGEN 366
FT /note="L->I: Increases phenacetin O-deethylation activity 3
FT fold."
FT /evidence="ECO:0000269|PubMed:18779312"
FT MUTAGEN 369
FT /note="G->S: Decreases phenacetin O-deethylation activity 9
FT fold."
FT /evidence="ECO:0000269|PubMed:18779312"
FT MUTAGEN 372
FT /note="H->R: Decreases phenacetin O-deethylation activity 3
FT fold."
FT /evidence="ECO:0000269|PubMed:18779312"
FT CONFLICT 208
FT /note="S -> R (in Ref. 1; AAB40519)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="A -> G (in Ref. 1; AAB40519)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="V -> E (in Ref. 1; AAB40519)"
FT /evidence="ECO:0000305"
FT CONFLICT 409..412
FT /note="RDFN -> QDCS (in Ref. 1; AAB40519)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="K -> E (in Ref. 1; AAB40519)"
FT /evidence="ECO:0000305"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:2PG5"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:2PG5"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:2P85"
FT HELIX 54..65
FT /evidence="ECO:0007829|PDB:2PG5"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:2PG5"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:2PG5"
FT HELIX 84..91
FT /evidence="ECO:0007829|PDB:2PG5"
FT TURN 92..98
FT /evidence="ECO:0007829|PDB:2PG5"
FT HELIX 105..111
FT /evidence="ECO:0007829|PDB:2PG5"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:2PG5"
FT HELIX 121..137
FT /evidence="ECO:0007829|PDB:2PG5"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:2PG5"
FT HELIX 143..161
FT /evidence="ECO:0007829|PDB:2PG5"
FT TURN 162..165
FT /evidence="ECO:0007829|PDB:2PG5"
FT HELIX 171..187
FT /evidence="ECO:0007829|PDB:2PG5"
FT HELIX 196..212
FT /evidence="ECO:0007829|PDB:2PG5"
FT HELIX 215..227
FT /evidence="ECO:0007829|PDB:2PG5"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:2PG5"
FT HELIX 233..256
FT /evidence="ECO:0007829|PDB:2PG5"
FT HELIX 267..277
FT /evidence="ECO:0007829|PDB:2PG5"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:2PG5"
FT HELIX 288..319
FT /evidence="ECO:0007829|PDB:2PG5"
FT HELIX 321..334
FT /evidence="ECO:0007829|PDB:2PG5"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:2PG5"
FT HELIX 343..348
FT /evidence="ECO:0007829|PDB:2PG5"
FT HELIX 350..363
FT /evidence="ECO:0007829|PDB:2PG5"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:2PG5"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:2PG5"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:2PG5"
FT HELIX 395..399
FT /evidence="ECO:0007829|PDB:2PG5"
FT TURN 402..404
FT /evidence="ECO:0007829|PDB:2PG5"
FT HELIX 413..416
FT /evidence="ECO:0007829|PDB:2PG5"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:4EJH"
FT HELIX 442..459
FT /evidence="ECO:0007829|PDB:2PG5"
FT STRAND 460..466
FT /evidence="ECO:0007829|PDB:2PG5"
FT HELIX 468..470
FT /evidence="ECO:0007829|PDB:2PG5"
FT STRAND 476..483
FT /evidence="ECO:0007829|PDB:2PG5"
FT STRAND 489..493
FT /evidence="ECO:0007829|PDB:2PG5"
SQ SEQUENCE 494 AA; 56688 MW; A39F18AD71C28821 CRC64;
MLASGLLLVT LLACLTVMVL MSVWRQRKSR GKLPPGPTPL PFIGNYLQLN TEQMYNSLMK
ISERYGPVFT IHLGPRRVVV LCGHDAVKEA LVDQAEEFSG RGEQATFDWL FKGYGVAFSN
GERAKQLRRF SIATLRGFGV GKRGIEERIQ EEAGFLIDAL RGTHGANIDP TFFLSRTVSN
VISSIVFGDR FDYEDKEFLS LLRMMLGSFQ FTATSTGQLY EMFSSVMKHL PGPQQQAFKE
LQGLEDFIAK KVEHNQRTLD PNSPRDFIDS FLIRMQEEEK NPNTEFYLKN LVMTTLNLFF
AGTETVSTTL RYGFLLLMKH PEVEAKVHEE IDRVIGKNRQ PKFEDRAKMP YTEAVIHEIQ
RFGDMLPMGL AHRVNKDTKF RDFFLPKGTE VFPMLGSVLR DPRFFSNPRD FNPQHFLDKK
GQFKKSDAFV PFSIGKRYCF GEGLARMELF LFFTTIMQNF RFKSPQSPKD IDVSPKHVGF
ATIPRNYTMS FLPR
