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 27-MAR-2024, entry version 183. 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 CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:65760, Rhea:RHEA- CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, CC ChEBI:CHEBI:58210, ChEBI:CHEBI:61313, ChEBI:CHEBI:138141; CC EC=1.14.14.19; 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 CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:46308, Rhea:RHEA- CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17026, CC ChEBI:CHEBI:17252, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; CC EC=1.14.14.19; 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 CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50236, Rhea:RHEA- CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16581, CC ChEBI:CHEBI:28750, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; CC EC=1.14.14.19; 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 CC [NADPH--hemoprotein reductase] = 6beta,16alpha,17alpha- CC trihydroxyprogesterone + H(+) + H2O + oxidized [NADPH--hemoprotein CC reductase]; Xref=Rhea:RHEA:53220, Rhea:RHEA-COMP:11964, Rhea:RHEA- CC COMP:11965, 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 CC [NADPH--hemoprotein reductase] = 3beta,16alpha-dihydroxy-androst-5- CC en-17-one + acetate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein CC reductase]; Xref=Rhea:RHEA:53224, Rhea:RHEA-COMP:11964, Rhea:RHEA- CC COMP:11965, 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 CC [NADPH--hemoprotein reductase] = 3beta,16alpha-dihydroxy-androst-5- CC en-17-one + 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 10116-ENSRNOP00000027160; -. DR Ensembl; ENSRNOT00060051262; ENSRNOP00060042646; ENSRNOG00060029516. DR GeneID; 25146; -. DR KEGG; rno:25146; -. DR UCSC; RGD:2456; rat. DR AGR; RGD:2456; -. DR CTD; 1586; -. DR RGD; 2456; Cyp17a1. DR eggNOG; KOG0156; Eukaryota. DR InParanoid; P11715; -. DR OrthoDB; 2900138at2759; -. 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:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. 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: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 CDD; cd20673; CYP17A1; 1. DR Gene3D; 1.10.630.10; Cytochrome P450; 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 PANTHER; PTHR24289; STEROID 17-ALPHA-HYDROXYLASE/17,20 LYASE; 1. DR PANTHER; PTHR24289:SF13; STEROID 17-ALPHA-HYDROXYLASE_17,20 LYASE; 1. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; Cytochrome P450; 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 //