ID   CP17A_ORYLA             Reviewed;         517 AA.
AC   P70085; P70086;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 145.
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   Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=8090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS C17L AND C17S).
RC   STRAIN=Orange-red; TISSUE=Ovarian follicle;
RX   PubMed=8916038;
RX   DOI=10.1002/(sici)1098-2795(199611)45:3<285::aid-mrd4>3.0.co;2-o;
RA   Fukada S., Tanaka M., Matsuyama M., Kobayashi D., Nagahama Y.;
RT   "Isolation, characterization, and expression of cDNAs encoding the medaka
RT   (Oryzias latipes) ovarian follicle cytochrome P-450 aromatase.";
RL   Mol. Reprod. Dev. 45:285-290(1996).
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
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   -!- 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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=C17L;
CC         IsoId=P70085-1; Sequence=Displayed;
CC       Name=C17S;
CC         IsoId=P70085-2; Sequence=VSP_000615;
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; D87121; BAA13252.1; -; mRNA.
DR   EMBL; D87122; BAA13253.1; -; mRNA.
DR   RefSeq; NP_001098564.1; NM_001105094.1. [P70085-1]
DR   AlphaFoldDB; P70085; -.
DR   SMR; P70085; -.
DR   STRING; 8090.ENSORLP00000023956; -.
DR   Ensembl; ENSORLT00000023960.2; ENSORLP00000023959.2; ENSORLG00000019226.2. [P70085-1]
DR   Ensembl; ENSORLT00000023962.2; ENSORLP00000023961.1; ENSORLG00000019226.2. [P70085-2]
DR   GeneID; 100125816; -.
DR   KEGG; ola:100125816; -.
DR   CTD; 105601846; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   GeneTree; ENSGT00940000155588; -.
DR   HOGENOM; CLU_001570_22_0_1; -.
DR   InParanoid; P70085; -.
DR   OrthoDB; 2900138at2759; -.
DR   UniPathway; UPA00062; -.
DR   Proteomes; UP000001038; Chromosome 15.
DR   Proteomes; UP000265180; Unplaced.
DR   Proteomes; UP000265200; Unplaced.
DR   Bgee; ENSORLG00000019226; Expressed in testis and 5 other cell types or tissues.
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; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004508; F:steroid 17-alpha-monooxygenase activity; IBA:GO_Central.
DR   GO; GO:0042446; P:hormone biosynthetic process; IBA:GO_Central.
DR   GO; GO:0042448; P:progesterone metabolic process; IBA:GO_Central.
DR   GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-UniPathway.
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   Alternative splicing; Heme; Iron; Lipid metabolism; Lyase; Membrane;
KW   Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome;
KW   Steroidogenesis.
FT   CHAIN           1..517
FT                   /note="Steroid 17-alpha-hydroxylase/17,20 lyase"
FT                   /id="PRO_0000051946"
FT   BINDING         451
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   VAR_SEQ         230..258
FT                   /note="Missing (in isoform C17S)"
FT                   /evidence="ECO:0000303|PubMed:8916038"
FT                   /id="VSP_000615"
SQ   SEQUENCE   517 AA;  57524 MW;  7A67509437ED6C6E CRC64;
     MAWFLCLSVL VVLVLALAAL LWRVRTRDRP QEAPSLPYLP VLGSLLSLRS PHPPHVLFKE
     LQQKYGQTYS LKMGSHQVII VNHHAHAREV LLKRGRTFAG RPRTVTTDVL TRDGKDIAFG
     DYSATWRFHR KIVHGALCMF GEGSASLQRI ICTEAQSLCS TLSEAAATGL ALDLSPELTR
     AVTNVICSLC FNSSYSRGDP EFEAMLRYSQ GIVDTVAKDS LVDIFPWLQI FPNKDLRLLK
     QCVAVRDQLL QKKFEEHKSD YSDHVQRDLL DALLRAKRSA ENNNTAAEFS AEAVGLSDDH
     LLMTVGDIFG AGVETTTTVL KWAITYLIHY PEVQKQIQEE LDRKVGVDRP PQLSDRGSLP
     FLEATIREVL RIRPVAPLLI PHVALSDTSL GDFTVRKGTR VVINLWSLHH DEKEWTNPDL
     FNPGRFLSAD GSSLTLPSSS YLPFGAGLRV CLGEALAKME LFLFLSWILQ RFTLSVPPSQ
     SLPSLEGKFG VVLQPVKYAV KATPRPGCHS GLFPANP
//