CP17A_CHICK
ID CP17A_CHICK Reviewed; 508 AA.
AC P12394;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Steroid 17-alpha-hydroxylase/17,20 lyase;
DE EC=1.14.14.19 {ECO:0000250|UniProtKB:P05093};
DE EC=1.14.14.32 {ECO:0000250|UniProtKB:P05093};
DE AltName: Full=17-alpha-hydroxyprogesterone aldolase;
DE AltName: Full=CYPXVII;
DE AltName: Full=Cytochrome P450 17A1;
DE AltName: Full=Cytochrome P450-C17;
DE Short=Cytochrome P450c17;
GN Name=CYP17A1; Synonyms=CYP17;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3047010; DOI=10.1016/0378-1119(88)90226-0;
RA Ono H., Iwasaki M., Sakamoto N., Mizuno S.;
RT "cDNA cloning and sequence analysis of a chicken gene expressed during the
RT gonadal development and homologous to mammalian cytochrome P-450c17.";
RL Gene 66:77-85(1988).
CC -!- FUNCTION: Conversion of pregnenolone and progesterone to their 17-
CC alpha-hydroxylated products and subsequently to dehydroepiandrosterone
CC (DHEA) and androstenedione. Catalyzes both the 17-alpha-hydroxylation
CC and the 17,20-lyase reaction.
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 -!- 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 -!- 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 -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- PATHWAY: Lipid metabolism; steroid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; M21406; AAA48997.1; -; mRNA.
DR PIR; JT0318; O4CHC7.
DR RefSeq; NP_001001901.1; NM_001001901.2.
DR AlphaFoldDB; P12394; -.
DR SMR; P12394; -.
DR STRING; 9031.ENSGALP00000032532; -.
DR PaxDb; P12394; -.
DR GeneID; 425056; -.
DR KEGG; gga:425056; -.
DR CTD; 1586; -.
DR VEuPathDB; HostDB:geneid_425056; -.
DR eggNOG; KOG0156; Eukaryota.
DR InParanoid; P12394; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; P12394; -.
DR UniPathway; UPA00062; -.
DR PRO; PR:P12394; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047442; F:17-alpha-hydroxyprogesterone aldolase activity; IBA:GO_Central.
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:0042446; P:hormone biosynthetic process; ISS:UniProtKB.
DR GO; GO:0042448; P:progesterone metabolic process; IBA:GO_Central.
DR GO; GO:0007548; P:sex differentiation; IEA:InterPro.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008202; P:steroid metabolic process; ISS:UniProtKB.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR033282; CYP17A1.
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:SF7; PTHR24289:SF7; 1.
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 2: Evidence at transcript level;
KW Heme; Iron; Lipid metabolism; Lyase; Membrane; Metal-binding;
KW Monooxygenase; Oxidoreductase; Reference proteome; Steroidogenesis.
FT CHAIN 1..508
FT /note="Steroid 17-alpha-hydroxylase/17,20 lyase"
FT /id="PRO_0000051943"
FT BINDING 445
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"
SQ SEQUENCE 508 AA; 56984 MW; 52BE915B46E237AF CRC64;
MPPLAVLLLA LALLCAWRLS YSQGPTGTGT GRPRSLPALP LVGSLLQLAG HPQLHLRLWR
LQGRYGSLYG LWMGSHYVVV VNSYQHAREV LLKKGKAFAG RPRTVTTDLL SRGGKDIAFA
SYGPLWKFQR KLVHAALSMF GEGSVALEKI ICREAASLCE TLGAAQDMAL DMAPELTRAV
TNVVCSLCFN SSYRRGDPEF EAMLEYSQGI VDTVAKESLV DIFPWLQIFP NRDLALLKRC
LKVRDQLLQQ KFTEHKEAFC GDTVRDLMDA LLQVRLNAEN NSPLEPGLEL TDDHLLMTVG
DIFGAGVETT TTVLKWAVLY LLHYPEVQKK IQEEMDQKIG LARHPHLSDR PLLPYLEATI
SEGLRIRPVS PLLIPHVSLA DTSIGEYSIP KGARVVINLW SVHHDEKEWD KPEEFNPGRF
LDEQGQHIHS PSPSYLPFGA GIRVCLGEVL AKMELFLFLA WVLQRFTLEC PQDQPLPSLE
GKFGVVLQVQ KFRVKARLRE AWRGEMVR
