ID   Q6P200_MOUSE            Unreviewed;       507 AA.
AC   Q6P200;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=Steroid 17-alpha-hydroxylase/17,20 lyase {ECO:0000256|ARBA:ARBA00014119};
DE            EC=1.14.14.19 {ECO:0000256|ARBA:ARBA00012359};
DE            EC=1.14.14.32 {ECO:0000256|ARBA:ARBA00012354};
DE   AltName: Full=CYPXVII {ECO:0000256|ARBA:ARBA00032037};
DE   AltName: Full=Cytochrome P450 17A1 {ECO:0000256|ARBA:ARBA00030382};
DE   AltName: Full=Cytochrome P450-C17 {ECO:0000256|ARBA:ARBA00032167};
DE   AltName: Full=Steroid 17-alpha-monooxygenase {ECO:0000256|ARBA:ARBA00044223};
GN   Name=Cyp17a1 {ECO:0000313|EMBL:AAH64793.1, ECO:0000313|MGI:MGI:88586};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:AAH64793.1};
RN   [1] {ECO:0000313|EMBL:AAH64793.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:AAH64793.1};
RC   TISSUE=Embryo {ECO:0000313|EMBL:AAH64793.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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:0000256|ARBA:ARBA00043778};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50245;
CC         Evidence={ECO:0000256|ARBA:ARBA00043778};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + pregnenolone + reduced [NADPH--hemoprotein reductase] =
CC         17alpha-hydroxypregnenolone + H(+) + H2O + oxidized
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50236, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16581,
CC         ChEBI:CHEBI:28750, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC         EC=1.14.14.19; Evidence={ECO:0000256|ARBA:ARBA00043658};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50237;
CC         Evidence={ECO:0000256|ARBA:ARBA00043658};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + progesterone + reduced [NADPH--hemoprotein reductase] =
CC         17alpha-hydroxyprogesterone + H(+) + H2O + oxidized
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:46308, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17026,
CC         ChEBI:CHEBI:17252, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC         EC=1.14.14.19; Evidence={ECO:0000256|ARBA:ARBA00043730};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46309;
CC         Evidence={ECO:0000256|ARBA:ARBA00043730};
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:0000256|ARBA:ARBA00043780};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65761;
CC         Evidence={ECO:0000256|ARBA:ARBA00043780};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971};
CC   -!- PATHWAY: Hormone biosynthesis. {ECO:0000256|ARBA:ARBA00004972}.
CC   -!- PATHWAY: Steroid biosynthesis; glucocorticoid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00043954}.
CC   -!- PATHWAY: Steroid hormone biosynthesis. {ECO:0000256|ARBA:ARBA00025710}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004586}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004370}. Microsome membrane
CC       {ECO:0000256|ARBA:ARBA00004524}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR   EMBL; BC064793; AAH64793.1; -; mRNA.
DR   AlphaFoldDB; Q6P200; -.
DR   AGR; MGI:88586; -.
DR   MGI; MGI:88586; Cyp17a1.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
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   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU000461};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000461};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000461};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW   ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000461}; Signal {ECO:0000256|SAM:SignalP};
KW   Steroidogenesis {ECO:0000256|ARBA:ARBA00023250}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..507
FT                   /note="Steroid 17-alpha-hydroxylase/17,20 lyase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004277699"
SQ   SEQUENCE   507 AA;  57611 MW;  F548788917A6057E CRC64;
     MWELVGLLLL ILAYFFWPKS KTPNAKFPRS LPFLPLVGSL PFLPRRGHMH ANFFKLQEKY
     GPIYSLRLGT TTAVIVGHYQ LAREVLVKKG KEFSGRPQMV TLGLLSDQGK GVAFADSSSS
     WQLHRKLVFS TFSLFRDDQK LEKMICQEAN SLCDLILTYD GESRDLSTLI FKSVINIICT
     ICFNISFENK DPILTTIQTF TEGIVDVLGH SDLVDIFPWL KIFPNKNLEM IKEHTKIREK
     TLVEMFEKCK EKFNSESLSS LTDILIQAKM NAENNNTGEG QDPSVFSDKH ILVTVGDIFG
     AGIETTSSVL SWILAFLVHN PEVKRKIQKE IDQYVGFSRT PSFNDRTHLL MLEATIREVL
     RIRPVAPLLI PHKANIDSSI GEFAIPKDTH VIINLWALHH DKNEWDQPDR FMPERFLDPT
     GSHLITPTPS YLPFGAGPRS CIGEALARQE LFIFMALLLQ RFDFDVSDDK QLPCLVGDPK
     VVFLIDPFKV KITVRQAWKD AQVEVST
//