CP17A_ORYLA
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 03-AUG-2022, entry version 138.
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 [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 -!- 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.ENSORLP00000023959; -.
DR PRIDE; P70085; -.
DR Ensembl; ENSORLT00000023960; ENSORLP00000023959; ENSORLG00000019226. [P70085-1]
DR Ensembl; ENSORLT00000023962; ENSORLP00000023961; ENSORLG00000019226. [P70085-2]
DR GeneID; 100125816; -.
DR KEGG; ola:100125816; -.
DR CTD; 100313515; -.
DR eggNOG; KOG0156; Eukaryota.
DR GeneTree; ENSGT00940000155588; -.
DR HOGENOM; CLU_001570_22_0_1; -.
DR InParanoid; P70085; -.
DR OrthoDB; 702827at2759; -.
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 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:0007548; P:sex differentiation; IEA:InterPro.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-UniPathway.
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 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
