CP17A_ONCMY
ID CP17A_ONCMY Reviewed; 514 AA.
AC P30437;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 115.
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 Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1451787; DOI=10.1016/0014-5793(92)80210-8;
RA Sakai N., Tanaka M., Adachi S., Miller W.L., Nagahama Y.;
RT "Rainbow trout cytochrome P-450c17 (17 alpha-hydroxylase/17,20-lyase). cDNA
RT cloning, enzymatic properties and temporal pattern of ovarian P-450c17 mRNA
RT expression during oogenesis.";
RL FEBS Lett. 301:60-64(1992).
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 -!- ACTIVITY REGULATION: Regulated predominantly by intracellular cAMP
CC levels.
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; X65800; CAA46675.1; -; mRNA.
DR PIR; S21125; S21125.
DR RefSeq; NP_001118219.1; NM_001124747.1.
DR AlphaFoldDB; P30437; -.
DR SMR; P30437; -.
DR GeneID; 100137017; -.
DR KEGG; omy:100137017; -.
DR CTD; 1586; -.
DR OrthoDB; 702827at2759; -.
DR UniPathway; UPA00062; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047442; F:17-alpha-hydroxyprogesterone aldolase activity; IEA:InterPro.
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; IMP:AgBase.
DR GO; GO:0042448; P:progesterone metabolic process; IMP:AgBase.
DR GO; GO:0007548; P:sex differentiation; IEA:InterPro.
DR GO; GO:0006694; P:steroid biosynthetic process; IMP:AgBase.
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; Steroidogenesis.
FT CHAIN 1..514
FT /note="Steroid 17-alpha-hydroxylase/17,20 lyase"
FT /id="PRO_0000051944"
FT BINDING 449
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"
SQ SEQUENCE 514 AA; 57408 MW; 9AC19961F921DCCB CRC64;
MAWFLCMCVF SVVGLGLLLL QVKLRRSLET RGGPPSLPVF PLIGSLLSLR SNQAPHVLFQ
KLQQKYGHTY SLMMGPHTVI LVNHHQHAKE VLLKKGKIFA GRPRTVTTDL LTRDGKDIAF
ADYGATWRFH RKTVHGALCM FGEGSASIEK IICREALSLC DTLRESGSAS LDLSPELTRA
VTNVVCSLCF SSSYCRGDPE FEAMLQFSQG IVDTVAKDSL VDIFPWLQVF PNADLRLLKQ
CVSIRDKLLQ KKYEEHKSDY SDHEQRDLLD ALLRAKRSAE NNNTAEITME TVGLSEDHLL
MTVGDIFGAG VETTSTVLKW AIAYLIHHPQ VQQRIQEELD SVVGGDRTPQ LSDRGSLPYL
EATIREVLRI RPVAPLLIPH VAQTDTSIGK FTVRKGARII INLWSLHHDE KEWKNPEMFD
PGRFLNEEGT GLCIPSPSYL PFGAGVRVCL GEALAKMEIF LFLSWILQRL TMTVSPGQPL
PSLEGKFGVV LQPVKYKVNA TPRAGWEKSH LQTS
