ID   CP17A_PIG               Reviewed;         509 AA.
AC   P19100; Q29553; Q99030;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 3.
DT   27-MAR-2024, entry version 166.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Adrenal gland, and Testis;
RX   PubMed=3025870; DOI=10.1073/pnas.84.2.407;
RA   Chung B.-C., Picado-Leonard J., Haniu M., Bienkowski M., Hall P.F.,
RA   Shively J.E., Miller W.L.;
RT   "Cytochrome P450c17 (steroid 17 alpha-hydroxylase/17,20 lyase): cloning of
RT   human adrenal and testis cDNAs indicates the same gene is expressed in both
RT   tissues.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:407-411(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   PubMed=1543750; DOI=10.1016/0167-4781(92)90464-b;
RA   Conley A.J., Graham-Lorence S.E., Kagimoto M., Lorence M.C., Murry B.A.,
RA   Oka K., Sanders D., Mason J.I.;
RT   "Nucleotide sequence of a cDNA encoding porcine testis 17 alpha-hydroxylase
RT   cytochrome P-450.";
RL   Biochim. Biophys. Acta 1130:75-77(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Kidney;
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   [4]
RP   NUCLEOTIDE SEQUENCE.
RA   Conley A.J., Chu X., Corbin C.J.;
RL   Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; M63507; AAA31008.1; -; mRNA.
DR   EMBL; U41525; AAA84419.1; -; Genomic_DNA.
DR   EMBL; U41519; AAA84419.1; JOINED; Genomic_DNA.
DR   EMBL; U41520; AAA84419.1; JOINED; Genomic_DNA.
DR   EMBL; U41521; AAA84419.1; JOINED; Genomic_DNA.
DR   EMBL; U41522; AAA84419.1; JOINED; Genomic_DNA.
DR   EMBL; U41523; AAA84419.1; JOINED; Genomic_DNA.
DR   EMBL; U41524; AAA84419.1; JOINED; Genomic_DNA.
DR   EMBL; Z11854; CAA77878.1; -; Genomic_DNA.
DR   EMBL; Z11855; CAA77878.1; JOINED; Genomic_DNA.
DR   EMBL; Z11856; CAA77878.1; JOINED; Genomic_DNA.
DR   PIR; S22339; S22339.
DR   RefSeq; NP_999593.1; NM_214428.1.
DR   AlphaFoldDB; P19100; -.
DR   SMR; P19100; -.
DR   STRING; 9823.ENSSSCP00000011283; -.
DR   PaxDb; 9823-ENSSSCP00000011283; -.
DR   PeptideAtlas; P19100; -.
DR   Ensembl; ENSSSCT00000011585.4; ENSSSCP00000011283.2; ENSSSCG00000010591.4.
DR   Ensembl; ENSSSCT00005030769.1; ENSSSCP00005018763.1; ENSSSCG00005019328.1.
DR   Ensembl; ENSSSCT00005030856.1; ENSSSCP00005018814.1; ENSSSCG00005019328.1.
DR   Ensembl; ENSSSCT00015028983.1; ENSSSCP00015011397.1; ENSSSCG00015021503.1.
DR   Ensembl; ENSSSCT00025105077.1; ENSSSCP00025046858.1; ENSSSCG00025075981.1.
DR   Ensembl; ENSSSCT00035110081.1; ENSSSCP00035047911.1; ENSSSCG00035080345.1.
DR   Ensembl; ENSSSCT00040076620.1; ENSSSCP00040032917.1; ENSSSCG00040055008.1.
DR   Ensembl; ENSSSCT00045032693.1; ENSSSCP00045022639.1; ENSSSCG00045019126.1.
DR   Ensembl; ENSSSCT00055007950.1; ENSSSCP00055006290.1; ENSSSCG00055004034.1.
DR   Ensembl; ENSSSCT00060070162.1; ENSSSCP00060030276.1; ENSSSCG00060051529.1.
DR   Ensembl; ENSSSCT00065007534.1; ENSSSCP00065003217.1; ENSSSCG00065005560.1.
DR   Ensembl; ENSSSCT00070022474.1; ENSSSCP00070018599.1; ENSSSCG00070011543.1.
DR   GeneID; 403330; -.
DR   KEGG; ssc:403330; -.
DR   CTD; 1586; -.
DR   VGNC; VGNC:103368; CYP17A1.
DR   eggNOG; KOG0156; Eukaryota.
DR   GeneTree; ENSGT00940000155588; -.
DR   HOGENOM; CLU_001570_22_0_1; -.
DR   InParanoid; P19100; -.
DR   OMA; QKCAYVA; -.
DR   OrthoDB; 2900138at2759; -.
DR   TreeFam; TF105095; -.
DR   BRENDA; 1.14.14.19; 6170.
DR   Reactome; R-SSC-193048; Androgen biosynthesis.
DR   Reactome; R-SSC-194002; Glucocorticoid biosynthesis.
DR   UniPathway; UPA00788; -.
DR   Proteomes; UP000008227; Chromosome 14.
DR   Proteomes; UP000314985; Chromosome 14.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; Unplaced.
DR   Bgee; ENSSSCG00000010591; Expressed in testis and 5 other cell types or tissues.
DR   ExpressionAtlas; P19100; baseline.
DR   GO; GO:0030424; C:axon; IEA:Ensembl.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
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; ISS:UniProtKB.
DR   GO; GO:0006704; P:glucocorticoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0042446; P:hormone biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0042448; P:progesterone metabolic process; ISS:UniProtKB.
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.
DR   Genevisible; P19100; SS.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Heme; Iron; Lipid metabolism; Lyase; Membrane;
KW   Metal-binding; Microsome; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Steroidogenesis.
FT   CHAIN           1..509
FT                   /note="Steroid 17-alpha-hydroxylase/17,20 lyase"
FT                   /id="PRO_0000051940"
FT   BINDING         202
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P05093"
FT   BINDING         442
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        46..53
FT                   /note="RGHQHMNF -> FL (in Ref. 1; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        51
FT                   /note="M -> I (in Ref. 3; CAA77878)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        70
FT                   /note="S -> D (in Ref. 1; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        98
FT                   /note="R -> K (in Ref. 1; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        108..116
FT                   /note="Missing (in Ref. 3; CAA77878)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        117
FT                   /note="H -> E (in Ref. 1; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        126..140
FT                   /note="KLALSTFSLFKGGNL -> SLF (in Ref. 1; no nucleotide
FT                   entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        161..191
FT                   /note="NGESIDLAQPLSLAMTNIVSFICFNFSFKKG -> VIQNACEMDRLKEI
FT                   (in Ref. 1; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        196
FT                   /note="Q -> D (in Ref. 1; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        201..210
FT                   /note="FNDGILDAVG -> IEEGELT (in Ref. 1; no nucleotide
FT                   entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        238
FT                   /note="M -> E (in Ref. 1; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        257..266
FT                   /note="NSITNLLDIM -> IL (in Ref. 1; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        270..284
FT                   /note="Missing (in Ref. 1; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        291..303
FT                   /note="HMLATVADIFGAG -> AC (in Ref. 1; no nucleotide
FT                   entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        292
FT                   /note="M -> S (in Ref. 3; CAA77878)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        308
FT                   /note="A -> V (in Ref. 1; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        311..333
FT                   /note="VKWIVAFLLHYPLLRKKIQDAID -> FIWIQEAIE (in Ref. 1; no
FT                   nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        319..321
FT                   /note="LHY -> ATLC (in Ref. 3; CAA77878)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        330
FT                   /note="D -> E (in Ref. 3; CAA77878)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        333
FT                   /note="D -> E (in Ref. 3; CAA77878)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        389
FT                   /note="D -> A (in Ref. 1; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        395..397
FT                   /note="NLW -> SLF (in Ref. 1; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        407
FT                   /note="H -> L (in Ref. 2; AAA31008)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   509 AA;  57447 MW;  9497D185A1B446B4 CRC64;
     MWVLLVFFLL TLTYLFWPKT KGSGAKYPRS LPVLPVVGSL PFLPRRGHQH MNFFKLQDKY
     GPIFSFRLGS KTTVVIGDHQ LAKEVLLKKG KEFSGRPRVM TLDILSDNQK GIAFADHGTS
     WQLHRKLALS TFSLFKGGNL KLENIINQEI KVLCDFLATR NGESIDLAQP LSLAMTNIVS
     FICFNFSFKK GDPALQAIVN FNDGILDAVG KEILYDMFPG IRILPSQTLE NMKQCVRMRN
     ELLREILENR KENYSRNSIT NLLDIMIQAK TNAESNTGGP DHNLKLLSDR HMLATVADIF
     GAGVETSASV VKWIVAFLLH YPLLRKKIQD AIDQNIGFNR APSISDRNQL VLLEATIREV
     LRFRPVSPTL IPHRAIIDSS IGEFTIDKDT DVVVNLWALH HNEKEWHRPD LFMPERFLDP
     TGTQLISPSL SYLPFGAGPR SCVGEMLARQ ELFLFTAGLL QRFDLELPDD GQLPCLVGNP
     SLVLQIDPFK VKIKERQAWK EAHTEGSTS
//