ID A0A1W2PRY0_HUMAN Unreviewed; 407 AA. AC A0A1W2PRY0; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 05-DEC-2018, entry version 9. DE SubName: Full=Steroid 17-alpha-hydroxylase/17,20 lyase {ECO:0000313|Ensembl:ENSP00000492539}; GN Name=CYP17A1 {ECO:0000313|Ensembl:ENSP00000492539}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000492539, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000492539, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., RA Siebert R., Fechtel K., Bentley D., Durbin R., Hubbard T., RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [2] {ECO:0000313|Ensembl:ENSP00000492539} RP IDENTIFICATION. RG Ensembl; RL Submitted (APR-2017) to UniProtKB. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC {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; AL358790; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PeptideAtlas; A0A1W2PRY0; -. DR Ensembl; ENST00000638190; ENSP00000492539; ENSG00000148795. DR HGNC; HGNC:2593; CYP17A1. DR OpenTargets; ENSG00000148795; -. DR GeneTree; ENSGT00940000155588; -. DR ChiTaRS; CYP17A1; human. DR Proteomes; UP000005640; Chromosome 10. DR ExpressionAtlas; A0A1W2PRY0; baseline and differential. 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 Gene3D; 1.10.630.10; -; 2. 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 Pfam; PF00067; p450; 2. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Heme {ECO:0000256|RuleBase:RU000461}; KW Iron {ECO:0000256|RuleBase:RU000461}; KW Metal-binding {ECO:0000256|RuleBase:RU000461}; KW Monooxygenase {ECO:0000256|RuleBase:RU000461}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000461}; KW Proteomics identification {ECO:0000213|MaxQB:A0A1W2PRY0, KW ECO:0000213|PeptideAtlas:A0A1W2PRY0}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 407 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5012709686. SQ SEQUENCE 407 AA; 46030 MW; CA3F2DA4BAFCAA49 CRC64; MWELVALLLL TLAYLFWPKR RCPGAKYPKS LLSLPLVGSL PFLPRHGHMH NNFFKLQKKY GPIYSVRMGT KTTVIVGHHQ LAKEVLIKKG KDFSGRPQMA TLDIASNNRK GIAFADSGAH WQLHRRLAMA TFALFKDGDQ KLEKIICQEI STLCDMLATH NGQSIDISFP VFVAVTNVIS LICFNTSYKN GDPELNVIQN YNEGIIDNLS KDSLVDLVPW LKVKKKLYEE IDQNVGFSRT PTISDRNRLL LLEATIREVL RLRPVAPMLI PHKANVDSSI GEFAVDKGTE VIINLWALHH NEKEWHQPDQ FMPERFLNPA GTQLISPSVS YLPFGAGPRS CIGEILARQE LFLIMAWLLQ RFDLEVPDDG QLPSLEGIPK VVFLIDSFKV KIKVRQAWRE AQAEGST //