CP17A_RAT
ID CP17A_RAT Reviewed; 507 AA.
AC P11715; Q68FY2; Q6LAE5;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Steroid 17-alpha-hydroxylase/17,20 lyase;
DE EC=1.14.14.19 {ECO:0000250|UniProtKB:P05093};
DE AltName: Full=17-alpha-hydroxyprogesterone aldolase;
DE EC=1.14.14.32 {ECO:0000250|UniProtKB:P05093};
DE AltName: Full=CYPXVII;
DE AltName: Full=Cytochrome P450 17A1;
DE AltName: Full=Cytochrome P450-C17;
DE Short=Cytochrome P450c17;
DE AltName: Full=Steroid 17-alpha-monooxygenase;
GN Name=Cyp17a1; Synonyms=Cyp17;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=2786990; DOI=10.1210/mend-3-6-968;
RA Fevold H.R., Lorence M.C., McCarthy J.L., Trant J.M., Kagimoto M.,
RA Waterman M.R., Mason J.I.;
RT "Rat P450(17 alpha) from testis: characterization of a full-length cDNA
RT encoding a unique steroid hydroxylase capable of catalyzing both delta
RT 4- and delta 5-steroid-17,20-lyase reactions.";
RL Mol. Endocrinol. 3:968-975(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Testis;
RX PubMed=3264499; DOI=10.1016/s0006-291x(88)80307-3;
RA Namiki M., Kitamura M., Buczko E., Dufau M.L.;
RT "Rat testis P-450(17)alpha cDNA: the deduced amino acid sequence,
RT expression and secondary structural configuration.";
RL Biochem. Biophys. Res. Commun. 157:705-712(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=7702752; DOI=10.1089/dna.1994.13.1087;
RA Givens C.R., Zhang P., Bair S.R., Mellon S.H.;
RT "Transcriptional regulation of rat cytochrome P450c17 expression in mouse
RT Leydig MA-10 and adrenal Y-1 cells: identification of a single protein that
RT mediates both basal and cAMP-induced activities.";
RL DNA Cell Biol. 13:1087-1098(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-97.
RX PubMed=1627653; DOI=10.1016/0167-4781(92)90039-3;
RA Zhang P., Nason T.F., Han X.G., Hall P.F.;
RT "Gene for 17 alpha-hydroxylase/C (17-20) lyase P-450: complete nucleotide
RT sequence of the porcine gene and 5' upstream sequence of the rat gene.";
RL Biochim. Biophys. Acta 1131:345-348(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 271-507.
RX PubMed=3260774; DOI=10.1016/0006-291x(88)90663-8;
RA Nishihara M., Winters C.A., Buzko E., Waterman M.R., Dufau M.L.;
RT "Hormonal regulation of rat Leydig cell cytochrome P-45017 alpha mRNA
RT levels and characterization of a partial length rat P-45017 alpha cDNA.";
RL Biochem. Biophys. Res. Commun. 154:151-158(1988).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 273-507.
RX PubMed=2554289; DOI=10.1073/pnas.86.20.7775;
RA Mellon S.H., Vaisse C.;
RT "cAMP regulates P450scc gene expression by a cycloheximide-insensitive
RT mechanism in cultured mouse Leydig MA-10 cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:7775-7779(1989).
RN [8]
RP PROTEIN SEQUENCE OF 1-16.
RX PubMed=3436956; DOI=10.1093/oxfordjournals.jbchem.a122124;
RA Imaoka S., Kamataki T., Funae Y.;
RT "Purification and characterization of six cytochromes P-450 from hepatic
RT microsomes of immature female rats.";
RL J. Biochem. 102:843-851(1987).
CC -!- FUNCTION: A cytochrome P450 monooxygenase involved in corticoid and
CC androgen biosynthesis. Catalyzes 17-alpha hydroxylation of C21
CC steroids, which is common for both pathways. A second oxidative step,
CC required only for androgen synthesis, involves an acyl-carbon cleavage.
CC The 17-alpha hydroxy intermediates, as part of adrenal glucocorticoids
CC biosynthesis pathway, are precursors of cortisol. Hydroxylates steroid
CC hormones, pregnenolone and progesterone to form 17-alpha hydroxy
CC metabolites, followed by the cleavage of the C17-C20 bond to form C19
CC steroids, dehydroepiandrosterone (DHEA) and androstenedione. Has 16-
CC alpha hydroxylase activity. Catalyzes 16-alpha hydroxylation of 17-
CC alpha hydroxy pregnenolone, followed by the cleavage of the C17-C20
CC bond to form 16-alpha-hydroxy DHEA. Also 16-alpha hydroxylates
CC androgens, relevant for estriol synthesis. Mechanistically, uses
CC molecular oxygen inserting one oxygen atom into a substrate, and
CC reducing the second into a water molecule, with two electrons provided
CC by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein
CC reductase). {ECO:0000250|UniProtKB:P05093}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a C21-steroid + O2 + reduced [NADPH--hemoprotein reductase] =
CC a 17alpha-hydroxy-C21-steroid + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:65760, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:61313, ChEBI:CHEBI:138141; EC=1.14.14.19;
CC Evidence={ECO:0000250|UniProtKB:P05093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65761;
CC Evidence={ECO:0000250|UniProtKB:P05093};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + progesterone + reduced [NADPH--hemoprotein reductase] =
CC 17alpha-hydroxyprogesterone + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:46308, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17026, ChEBI:CHEBI:17252,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.19;
CC Evidence={ECO:0000250|UniProtKB:P05093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46309;
CC Evidence={ECO:0000250|UniProtKB:P05093};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + pregnenolone + reduced [NADPH--hemoprotein reductase] =
CC 17alpha-hydroxypregnenolone + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:50236, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16581, ChEBI:CHEBI:28750,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.19;
CC Evidence={ECO:0000250|UniProtKB:P05093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50237;
CC Evidence={ECO:0000250|UniProtKB:P05093};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17alpha-hydroxyprogesterone + O2 + reduced [NADPH--hemoprotein
CC reductase] = acetate + androst-4-ene-3,17-dione + 2 H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:14753,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16422,
CC ChEBI:CHEBI:17252, ChEBI:CHEBI:30089, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; EC=1.14.14.32;
CC Evidence={ECO:0000250|UniProtKB:P05093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14754;
CC Evidence={ECO:0000250|UniProtKB:P05093};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17alpha-hydroxyprogesterone + O2 + reduced [NADPH--hemoprotein
CC reductase] = 16alpha,17alpha-dihydroxyprogesterone + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53216,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:763,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17252, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:P05093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53217;
CC Evidence={ECO:0000250|UniProtKB:P05093};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=16alpha,17alpha-dihydroxyprogesterone + O2 + reduced [NADPH--
CC hemoprotein reductase] = 6beta,16alpha,17alpha-trihydroxyprogesterone
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:53220, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:763, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:137046; Evidence={ECO:0000250|UniProtKB:P05093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53221;
CC Evidence={ECO:0000250|UniProtKB:P05093};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17alpha-hydroxypregnenolone + O2 + reduced [NADPH--hemoprotein
CC reductase] = 3beta-hydroxyandrost-5-en-17-one + acetate + 2 H(+) +
CC H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50244,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:28689,
CC ChEBI:CHEBI:28750, ChEBI:CHEBI:30089, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; EC=1.14.14.32;
CC Evidence={ECO:0000250|UniProtKB:P05093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50245;
CC Evidence={ECO:0000250|UniProtKB:P05093};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=16alpha,17alpha-dihydroxypregnenolone + O2 + reduced [NADPH--
CC hemoprotein reductase] = 3beta,16alpha-dihydroxy-androst-5-en-17-one
CC + acetate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:53224, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:27771, ChEBI:CHEBI:30089, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:137049;
CC Evidence={ECO:0000250|UniProtKB:P05093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53225;
CC Evidence={ECO:0000250|UniProtKB:P05093};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3beta-hydroxyandrost-5-en-17-one + O2 + reduced [NADPH--
CC hemoprotein reductase] = 3beta,16alpha-dihydroxy-androst-5-en-17-one
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:47220, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:27771, ChEBI:CHEBI:28689, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P05093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47221;
CC Evidence={ECO:0000250|UniProtKB:P05093};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=androst-4-ene-3,17-dione + O2 + reduced [NADPH--hemoprotein
CC reductase] = 16alpha-hydroxyandrost-4-ene-3,17-dione + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53228,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16422,
CC ChEBI:CHEBI:27582, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:P05093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53229;
CC Evidence={ECO:0000250|UniProtKB:P05093};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P05093};
CC -!- ACTIVITY REGULATION: Regulated predominantly by intracellular cAMP
CC levels. The 17,20-lyase activity is stimulated by cytochrome b5, which
CC acts as an allosteric effector increasing the Vmax of the lyase
CC activity. {ECO:0000250|UniProtKB:P05093}.
CC -!- PATHWAY: Steroid hormone biosynthesis. {ECO:0000250|UniProtKB:P05093}.
CC -!- PATHWAY: Steroid biosynthesis; glucocorticoid biosynthesis.
CC {ECO:0000250|UniProtKB:P05093}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P05093}. Microsome membrane
CC {ECO:0000250|UniProtKB:P05093}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; X14086; CAA32248.1; -; mRNA.
DR EMBL; X69816; CAA49470.1; -; Genomic_DNA.
DR EMBL; M31681; AAA41777.1; -; mRNA.
DR EMBL; M22204; AAA41783.1; -; mRNA.
DR EMBL; BC078898; AAH78898.1; -; mRNA.
DR EMBL; Z11902; CAA77954.1; -; Genomic_DNA.
DR EMBL; M21208; AAA41050.1; -; mRNA.
DR EMBL; M27282; AAA41779.1; -; mRNA.
DR PIR; A31359; A30828.
DR RefSeq; NP_036885.1; NM_012753.2.
DR RefSeq; XP_006231496.1; XM_006231434.3.
DR RefSeq; XP_006231497.1; XM_006231435.3.
DR AlphaFoldDB; P11715; -.
DR SMR; P11715; -.
DR STRING; 10116.ENSRNOP00000027160; -.
DR BindingDB; P11715; -.
DR ChEMBL; CHEMBL4430; -.
DR DrugCentral; P11715; -.
DR iPTMnet; P11715; -.
DR PhosphoSitePlus; P11715; -.
DR PaxDb; P11715; -.
DR GeneID; 25146; -.
DR KEGG; rno:25146; -.
DR UCSC; RGD:2456; rat.
DR CTD; 1586; -.
DR RGD; 2456; Cyp17a1.
DR eggNOG; KOG0156; Eukaryota.
DR InParanoid; P11715; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; P11715; -.
DR TreeFam; TF105095; -.
DR Reactome; R-RNO-193048; Androgen biosynthesis.
DR Reactome; R-RNO-194002; Glucocorticoid biosynthesis.
DR UniPathway; UPA00788; -.
DR PRO; PR:P11715; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0042995; C:cell projection; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0047442; F:17-alpha-hydroxyprogesterone aldolase activity; ISS:UniProtKB.
DR GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004508; F:steroid 17-alpha-monooxygenase activity; IDA:RGD.
DR GO; GO:0030325; P:adrenal gland development; IEP:RGD.
DR GO; GO:0006702; P:androgen biosynthetic process; TAS:RGD.
DR GO; GO:0018879; P:biphenyl metabolic process; IEP:RGD.
DR GO; GO:0071236; P:cellular response to antibiotic; IEP:RGD.
DR GO; GO:0071371; P:cellular response to gonadotropin stimulus; IEP:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0018894; P:dibenzo-p-dioxin metabolic process; IEP:RGD.
DR GO; GO:0006704; P:glucocorticoid biosynthetic process; ISO:RGD.
DR GO; GO:0021766; P:hippocampus development; IEP:RGD.
DR GO; GO:0042446; P:hormone biosynthetic process; ISS:UniProtKB.
DR GO; GO:0033327; P:Leydig cell differentiation; IEP:RGD.
DR GO; GO:0008584; P:male gonad development; IEP:RGD.
DR GO; GO:0006082; P:organic acid metabolic process; IEP:RGD.
DR GO; GO:0030728; P:ovulation; IEP:RGD.
DR GO; GO:0018958; P:phenol-containing compound metabolic process; IEP:RGD.
DR GO; GO:0018963; P:phthalate metabolic process; IEP:RGD.
DR GO; GO:0090031; P:positive regulation of steroid hormone biosynthetic process; IMP:RGD.
DR GO; GO:0042448; P:progesterone metabolic process; ISS:UniProtKB.
DR GO; GO:0010034; P:response to acetate; IEP:RGD.
DR GO; GO:0051591; P:response to cAMP; IEP:RGD.
DR GO; GO:0034097; P:response to cytokine; IEP:RGD.
DR GO; GO:0060992; P:response to fungicide; IEP:RGD.
DR GO; GO:0034698; P:response to gonadotropin; IEP:RGD.
DR GO; GO:0009635; P:response to herbicide; IEP:RGD.
DR GO; GO:0017085; P:response to insecticide; IEP:RGD.
DR GO; GO:0010212; P:response to ionizing radiation; IEP:RGD.
DR GO; GO:0051597; P:response to methylmercury; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
DR GO; GO:0048545; P:response to steroid hormone; IEP:RGD.
DR GO; GO:0009636; P:response to toxic substance; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0006694; P:steroid biosynthetic process; IMP:RGD.
DR GO; GO:0008202; P:steroid metabolic process; ISS:UniProtKB.
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 Direct protein sequencing; Endoplasmic reticulum; Heme; Iron;
KW Lipid metabolism; Lyase; Membrane; Metal-binding; Microsome; Monooxygenase;
KW Oxidoreductase; Reference proteome; Steroidogenesis.
FT CHAIN 1..507
FT /note="Steroid 17-alpha-hydroxylase/17,20 lyase"
FT /id="PRO_0000051941"
FT BINDING 441
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 CONFLICT 190
FT /note="N -> K (in Ref. 4; AAH78898)"
FT /evidence="ECO:0000305"
FT CONFLICT 505..506
FT /note="VS -> LT (in Ref. 6; AAA41050)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 507 AA; 57250 MW; A535600F7E6A399B CRC64;
MWELVGLLLL ILAYFFWVKS KTPGAKLPRS LPSLPLVGSL PFLPRRGHMH VNFFKLQEKY
GPIYSLRLGT TTTVIIGHYQ LAREVLIKKG KEFSGRPQMV TQSLLSDQGK GVAFADAGSS
WHLHRKLVFS TFSLFKDGQK LEKLICQEAK SLCDMMLAHD KESIDLSTPI FMSVTNIICA
ICFNISYEKN DPKLTAIKTF TEGIVDATGD RNLVDIFPWL TIFPNKGLEV IKGYAKVRNE
VLTGIFEKCR EKFDSQSISS LTDILIQAKM NSDNNNSCEG RDPDVFSDRH ILATVGDIFG
AGIETTTTVL KWILAFLVHN PEVKKKIQKE IDQYVGFSRT PTFNDRSHLL MLEATIREVL
RIRPVAPMLI PHKANVDSSI GEFTVPKDTH VVVNLWALHH DENEWDQPDQ FMPERFLDPT
GSHLITPTQS YLPFGAGPRS CIGEALARQE LFVFTALLLQ RFDLDVSDDK QLPRLEGDPK
VVFLIDPFKV KITVRQAWMD AQAEVST
