ID Q6P200_MOUSE Unreviewed; 507 AA. AC Q6P200; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 02-OCT-2024, entry version 104. 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 ECO:0000256|PIRSR:PIRSR602401-1}; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC064793; AAH64793.1; -; mRNA. DR AlphaFoldDB; Q6P200; -. DR AGR; MGI:88586; -. DR MGI; MGI:88586; Cyp17a1. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. 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 GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW. 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|PIRSR:PIRSR602401-1}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602401-1}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR602401-1}; KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033, KW ECO:0000256|RuleBase:RU000461}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000461}; KW 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" FT BINDING 441 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:0000256|PIRSR:PIRSR602401-1" 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 //