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 [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; 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 Genevisible; P19100; SS.
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.
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
//
