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Steroid 17-alpha-hydroxylase/17,20 lyase (EC 1.14.14.19) (17-alpha-hydroxyprogesterone aldolase) (EC 1.14.14.32) (CYPXVII) (Cytochrome P450 17A1) (Cytochrome P450-C17) (Cytochrome P450c17) (Steroid 17-alpha-monooxygenase)

 CP17A_HUMAN             Reviewed;         508 AA.
P05093; Q5TZV7;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
27-SEP-2017, entry version 199.
RecName: Full=Steroid 17-alpha-hydroxylase/17,20 lyase;
EC=1.14.14.19 {ECO:0000269|PubMed:22266943};
AltName: Full=17-alpha-hydroxyprogesterone aldolase;
EC=1.14.14.32 {ECO:0000269|PubMed:22266943};
AltName: Full=CYPXVII;
AltName: Full=Cytochrome P450 17A1;
AltName: Full=Cytochrome P450-C17;
Short=Cytochrome P450c17;
AltName: Full=Steroid 17-alpha-monooxygenase;
Name=CYP17A1; Synonyms=CYP17, S17AH;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3025870; DOI=10.1073/pnas.84.2.407;
Chung B.-C., Picado-Leonard J., Haniu M., Bienkowski M., Hall P.F.,
Shively J.E., Miller W.L.;
"Cytochrome P450c17 (steroid 17 alpha-hydroxylase/17,20 lyase):
cloning of human adrenal and testis cDNAs indicates the same gene is
expressed in both tissues.";
Proc. Natl. Acad. Sci. U.S.A. 84:407-411(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3500022; DOI=10.1089/dna.1987.6.439;
Picado-Leonard J., Miller W.L.;
"Cloning and sequence of the human gene for P450c17 (steroid 17 alpha-
hydroxylase/17,20 lyase): similarity with the gene for P450c21.";
DNA 6:439-448(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3274893; DOI=10.1210/mend-1-5-348;
Bradshaw K.D., Waterman M.R., Couch R.T., Simpson E.R., Zuber M.X.;
"Characterization of complementary deoxyribonucleic acid for human
adrenocortical 17 alpha-hydroxylase: a probe for analysis of 17 alpha-
hydroxylase deficiency.";
Mol. Endocrinol. 1:348-354(1987).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1964490; DOI=10.1210/mend-4-12-1972;
Brentano S.T., Picado-Leonard J., Mellon S.H., Moore C.C.,
Miller W.L.;
"Tissue-specific, cyclic adenosine 3',5'-monophosphate-induced, and
phorbol ester-repressed transcription from the human P450c17 promoter
in mouse cells.";
Mol. Endocrinol. 4:1972-1979(1990).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2843762; DOI=10.1210/mend-2-6-564;
Kagimoto M., Winter J.S.D., Kagimoto K., Simpson E.R., Waterman M.R.;
"Structural characterization of normal and mutant human steroid 17
alpha-hydroxylase genes: molecular basis of one example of combined 17
alpha-hydroxylase/17,20 lyase deficiency.";
Mol. Endocrinol. 2:564-570(1988).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
3D-STRUCTURE MODELING OF 48-501.
PubMed=10406467; DOI=10.1210/mend.13.7.0326;
Auchus R.J., Miller W.L.;
"Molecular modeling of human P450c17 (17alpha-hydroxylase/17,20-
lyase): insights into reaction mechanisms and effects of mutations.";
Mol. Endocrinol. 13:1169-1182(1999).
[10]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 24-508 IN COMPLEXES WITH
HEME; ABIRATERONE AND TOK-001, FUNCTION, CATALYTIC ACTIVITY, AND
COFACTOR.
PubMed=22266943; DOI=10.1038/nature10743;
DeVore N.M., Scott E.E.;
"Structures of cytochrome P450 17A1 with prostate cancer drugs
abiraterone and TOK-001.";
Nature 482:116-119(2012).
[11]
VARIANT AH5 PHE-53 DEL.
PubMed=2808364;
Yanase T., Kagimoto M., Suzuki S., Hashiba K., Simpson E.R.,
Waterman M.R.;
"Deletion of a phenylalanine in the N-terminal region of human
cytochrome P-450(17 alpha) results in partial combined 17 alpha-
hydroxylase/17,20-lyase deficiency.";
J. Biol. Chem. 264:18076-18082(1989).
[12]
VARIANT AH5 PRO-106.
PubMed=1714904;
Lin D., Harikrishna J.A., Moore C.C.D., Jones K.L., Miller W.L.;
"Missense mutation serine106-->proline causes 17 alpha-hydroxylase
deficiency.";
J. Biol. Chem. 266:15992-15998(1991).
[13]
VARIANT AH5 CYS-496.
PubMed=1515452; DOI=10.1016/0925-4439(92)90100-2;
Yanase T., Waterman M.R., Zachmann M., Winter J.S.D., Kagimoto M.;
"Molecular basis of apparent isolated 17,20-lyase deficiency: compound
heterozygous mutations in the C-terminal region (Arg(496)-->Cys,
Gln(461)-->Stop) actually cause combined 17 alpha-hydroxylase/17,20-
lyase deficiency.";
Biochim. Biophys. Acta 1139:275-279(1992).
[14]
VARIANT AH5 THR-342.
PubMed=1740503; DOI=10.1210/jcem.74.3.1740503;
Ahlgren R., Yanase T., Simpson E.R., Winter J.S.D., Waterman M.R.;
"Compound heterozygous mutations (Arg 239-->Stop, Pro 342-->Thr) in
the CYP17 (P45017 alpha) gene lead to ambiguous external genitalia in
a male patient with partial combined 17 alpha-hydroxylase/17,20-lyase
deficiency.";
J. Clin. Endocrinol. Metab. 74:667-672(1992).
[15]
VARIANTS AH5 SER-64 AND ILE-112 INS.
PubMed=8396144;
Imai T., Globerman H., Gertner J.M., Kagawa N., Waterman M.R.;
"Expression and purification of functional human 17 alpha-
hydroxylase/17,20-lyase (P450c17) in Escherichia coli. Use of this
system for study of a novel form of combined 17 alpha-
hydroxylase/17,20-lyase deficiency.";
J. Biol. Chem. 268:19681-19689(1993).
[16]
VARIANT AH5 LEU-373.
PubMed=8245018;
Monno S., Ogawa H., Date T., Fujioka M., Miller W.L., Kobayashi M.;
"Mutation of histidine 373 to leucine in cytochrome P450c17 causes 17
alpha-hydroxylase deficiency.";
J. Biol. Chem. 268:25811-25817(1993).
[17]
VARIANT AH5 487-ASP--PHE-489 DEL.
PubMed=8345056; DOI=10.1210/jcem.77.2.8345056;
Fardella C.E., Zhang L.H., Mahacholklertwattana P., Lin D.,
Miller W.L.;
"Deletion of amino acids Asp487-Ser488-Phe489 in human cytochrome
P450c17 causes severe 17 alpha-hydroxylase deficiency.";
J. Clin. Endocrinol. Metab. 77:489-493(1993).
[18]
VARIANT AH5 HIS-440.
PubMed=8027220; DOI=10.1210/jcem.79.1.8027220;
Fardella C.E., Hum D.W., Homoki J., Miller W.L.;
"Point mutation of Arg440 to His in cytochrome P450c17 causes severe
17 alpha-hydroxylase deficiency.";
J. Clin. Endocrinol. Metab. 79:160-164(1994).
[19]
VARIANT AH5 TRP-96.
PubMed=8550762; DOI=10.1210/jcem.81.1.8550762;
Laflamme N., Leblanc J.-F., Mailloux J., Faure N., Labrie F.,
Simard J.;
"Mutation R96W in cytochrome P450c17 gene causes combined 17 alpha-
hydroxylase/17-20-lyase deficiency in two French Canadian patients.";
J. Clin. Endocrinol. Metab. 81:264-268(1996).
[20]
VARIANTS AH5 HIS-347 AND GLN-358.
Geller D.H., Mendonca B.B., Miller W.L.;
"The molecular basis of isolated 17,20 lyase deficiency.";
Pediatr. Res. 39:89A-89A(1996).
[21]
VARIANTS AH5 LEU-35; PHE-53 DEL; TRP-96; ASP-177; GLU-330 DEL; CYS-417
AND HIS-496, AND PHOSPHORYLATION.
PubMed=10720067; DOI=10.1210/jcem.85.3.6475;
Biason-Lauber A., Kempken B., Werder E., Forest M.G., Einaudi S.,
Ranke M.B., Matsuo N., Brunelli V., Schoenle E.J., Zachmann M.;
"17alpha-hydroxylase/17,20-lyase deficiency as a model to study
enzymatic activity regulation: role of phosphorylation.";
J. Clin. Endocrinol. Metab. 85:1226-1231(2000).
[22]
VARIANTS AH5 HIS-347; GLN-358 AND CYS-417.
PubMed=11549685; DOI=10.1210/jcem.86.9.7812;
Gupta M.K., Geller D.H., Auchus R.J.;
"Pitfalls in characterizing P450c17 mutations associated with isolated
17,20-lyase deficiency.";
J. Clin. Endocrinol. Metab. 86:4416-4423(2001).
[23]
VARIANT AH5 CYS-93.
PubMed=11836339; DOI=10.1210/jc.87.2.898;
Di Cerbo A., Biason-Lauber A., Savino M., Piemontese M.R.,
Di Giorgio A., Perona M., Savoia A.;
"Combined 17alpha-hydroxylase/17,20-lyase deficiency caused by
Phe93Cys mutation in the CYP17 gene.";
J. Clin. Endocrinol. Metab. 87:898-905(2002).
[24]
VARIANTS AH5 VAL-114; VAL-116; CYS-347 AND HIS-347.
PubMed=12466376; DOI=10.1210/jc.2001-011880;
Van Den Akker E.L.T., Koper J.W., Boehmer A.L.M., Themmen A.P.N.,
Verhoef-Post M., Timmerman M.A., Otten B.J., Drop S.L.S.,
De Jong F.H.;
"Differential inhibition of 17alpha-hydroxylase and 17,20-lyase
activities by three novel missense CYP17 mutations identified in
patients with P450c17 deficiency.";
J. Clin. Endocrinol. Metab. 87:5714-5721(2002).
[25]
VARIANTS AH5 TRP-96; ASP-329; CYS-362; ARG-406 AND LEU-428.
PubMed=14671162; DOI=10.1210/jc.2003-030988;
Martin R.M., Lin C.J., Costa E.M.F., de Oliveira M.L., Carrilho A.,
Villar H., Longui C.A., Mendonca B.B.;
"P450c17 deficiency in Brazilian patients: biochemical diagnosis
through progesterone levels confirmed by CYP17 genotyping.";
J. Clin. Endocrinol. Metab. 88:5739-5746(2003).
[26]
VARIANTS AH5 PHE-53 DEL AND ASN-373.
PubMed=19793597; DOI=10.1016/j.metabol.2009.07.024;
Katsumata N., Ogawa E., Fujiwara I., Fujikura K.;
"Novel CYP17A1 mutation in a Japanese patient with combined 17alpha-
hydroxylase/17,20-lyase deficiency.";
Metabolism 59:275-278(2010).
[27]
VARIANT AH5 GLN-96.
PubMed=24498484; DOI=10.5001/omj.2014.12;
Mula-Abed W.A., Pambinezhuth F.B., Al-Kindi M.K., Al-Busaidi N.B.,
Al-Muslahi H.N., Al-Lamki M.A.;
"Congenital adrenal hyperplasia due to 17-alpha-hydoxylase/17,20-lyase
deficiency presenting with hypertension and pseudohermaphroditism:
first case report from Oman.";
Oman Med. J. 29:55-59(2014).
[28]
VARIANTS AH5 GLU-174; LEU-373 AND LEU-406, AND CHARACTERIZATION OF
VARIANT AH5 LEU-406.
PubMed=24140098; DOI=10.1016/j.metabol.2013.08.015;
Kim Y.M., Kang M., Choi J.H., Lee B.H., Kim G.H., Ohn J.H., Kim S.Y.,
Park M.S., Yoo H.W.;
"A review of the literature on common CYP17A1 mutations in adults with
17-hydroxylase/17,20-lyase deficiency, a case series of such mutations
among Koreans and functional characteristics of a novel mutation.";
Metabolism 63:42-49(2014).
[29]
VARIANT AH5 ARG-121, AND CHARACTERIZATION OF VARIANT AH5 ARG-121.
PubMed=25650406; DOI=10.1530/EJE-14-0834;
Rubtsov P., Nizhnik A., Dedov I.I., Kalinchenko N., Petrov V.,
Orekhova A., Spirin P., Prassolov V., Tiulpakov A.;
"Partial deficiency of 17alpha-hydroxylase/17,20-lyase caused by a
novel missense mutation in the canonical cytochrome heme-interacting
motif.";
Eur. J. Endocrinol. 172:K19-25(2015).
-!- FUNCTION: Conversion of pregnenolone and progesterone to their 17-
alpha-hydroxylated products and subsequently to
dehydroepiandrosterone (DHEA) and androstenedione. Catalyzes both
the 17-alpha-hydroxylation and the 17,20-lyase reaction. Involved
in sexual development during fetal life and at puberty.
{ECO:0000269|PubMed:22266943}.
-!- CATALYTIC ACTIVITY: A C(21)-steroid + [reduced NADPH--hemoprotein
reductase] + O(2) = a 17-alpha-hydroxy-C(21)-steroid + [oxidized
NADPH--hemoprotein reductase] + H(2)O.
{ECO:0000269|PubMed:22266943}.
-!- CATALYTIC ACTIVITY: 17-alpha-hydroxyprogesterone + [reduced
NADPH--hemoprotein reductase] + O(2) = androstenedione + acetate +
[oxidized NADPH--hemoprotein reductase] + H(2)O.
{ECO:0000269|PubMed:22266943}.
-!- CATALYTIC ACTIVITY: 17-alpha-hydroxypregnenolone + [reduced
NADPH--hemoprotein reductase] + O(2) = 3-beta-hydroxyandrost-5-en-
17-one + acetate + [oxidized NADPH--hemoprotein reductase] +
H(2)O. {ECO:0000269|PubMed:22266943}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000269|PubMed:22266943};
-!- ENZYME REGULATION: Regulated predominantly by intracellular cAMP
levels.
-!- PATHWAY: Lipid metabolism; steroid biosynthesis.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}.
-!- PTM: Phosphorylation is necessary for 17,20-lyase, but not for 17-
alpha-hydroxylase activity. {ECO:0000269|PubMed:10720067}.
-!- DISEASE: Adrenal hyperplasia 5 (AH5) [MIM:202110]: A form of
congenital adrenal hyperplasia, a common recessive disease due to
defective synthesis of cortisol. Congenital adrenal hyperplasia is
characterized by androgen excess leading to ambiguous genitalia in
affected females, rapid somatic growth during childhood in both
sexes with premature closure of the epiphyses and short adult
stature. Four clinical types: 'salt wasting' (SW, the most severe
type), 'simple virilizing' (SV, less severely affected patients),
with normal aldosterone biosynthesis, 'non-classic form' or late-
onset (NC or LOAH) and 'cryptic' (asymptomatic).
{ECO:0000269|PubMed:10720067, ECO:0000269|PubMed:11549685,
ECO:0000269|PubMed:11836339, ECO:0000269|PubMed:12466376,
ECO:0000269|PubMed:14671162, ECO:0000269|PubMed:1515452,
ECO:0000269|PubMed:1714904, ECO:0000269|PubMed:1740503,
ECO:0000269|PubMed:19793597, ECO:0000269|PubMed:24140098,
ECO:0000269|PubMed:24498484, ECO:0000269|PubMed:25650406,
ECO:0000269|PubMed:2808364, ECO:0000269|PubMed:8027220,
ECO:0000269|PubMed:8245018, ECO:0000269|PubMed:8345056,
ECO:0000269|PubMed:8396144, ECO:0000269|PubMed:8550762,
ECO:0000269|Ref.20}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=CYP17A1";
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EMBL; M14564; AAA52151.1; -; mRNA.
EMBL; M19489; AAA36405.1; -; Genomic_DNA.
EMBL; M63871; AAA59984.1; -; Genomic_DNA.
EMBL; M31153; AAA52140.1; ALT_SEQ; Genomic_DNA.
EMBL; M31146; AAA52140.1; JOINED; Genomic_DNA.
EMBL; M31147; AAA52140.1; JOINED; Genomic_DNA.
EMBL; M31148; AAA52140.1; JOINED; Genomic_DNA.
EMBL; M31149; AAA52140.1; JOINED; Genomic_DNA.
EMBL; M31150; AAA52140.1; JOINED; Genomic_DNA.
EMBL; M31151; AAA52140.1; JOINED; Genomic_DNA.
EMBL; M31152; AAA52140.1; JOINED; Genomic_DNA.
EMBL; BT020000; AAV38803.1; -; mRNA.
EMBL; AL358790; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC062997; AAH62997.1; -; mRNA.
EMBL; BC063388; AAH63388.1; -; mRNA.
CCDS; CCDS7541.1; -.
PIR; A40921; A26366.
RefSeq; NP_000093.1; NM_000102.3.
UniGene; Hs.438016; -.
PDB; 2C17; Model; -; A=48-501.
PDB; 3RUK; X-ray; 2.60 A; A/B/C/D=24-508.
PDB; 3SWZ; X-ray; 2.40 A; A/B/C/D=24-508.
PDB; 4NKV; X-ray; 2.65 A; A/B/C/D=24-508.
PDB; 4NKW; X-ray; 2.50 A; A/B/C/D=24-508.
PDB; 4NKX; X-ray; 2.79 A; A/B/C/D=24-508.
PDB; 4NKY; X-ray; 2.55 A; A/B/C/D=24-508.
PDB; 4NKZ; X-ray; 3.00 A; A/B/C/D=24-508.
PDB; 5IRQ; X-ray; 2.20 A; A/B/C/D=24-508.
PDB; 5IRV; X-ray; 3.10 A; A/B/C/D=24-508.
PDBsum; 2C17; -.
PDBsum; 3RUK; -.
PDBsum; 3SWZ; -.
PDBsum; 4NKV; -.
PDBsum; 4NKW; -.
PDBsum; 4NKX; -.
PDBsum; 4NKY; -.
PDBsum; 4NKZ; -.
PDBsum; 5IRQ; -.
PDBsum; 5IRV; -.
ProteinModelPortal; P05093; -.
SMR; P05093; -.
BioGrid; 107958; 14.
IntAct; P05093; 13.
STRING; 9606.ENSP00000358903; -.
BindingDB; P05093; -.
ChEMBL; CHEMBL3522; -.
DrugBank; DB05812; Abiraterone.
DrugBank; DB04630; Aldosterone.
DrugBank; DB01424; Aminophenazone.
DrugBank; DB01234; Dexamethasone.
DrugBank; DB02901; Dihydrotestosterone.
DrugBank; DB01233; Metoclopramide.
DrugBank; DB00157; NADH.
DrugBank; DB00396; Progesterone.
GuidetoPHARMACOLOGY; 1361; -.
SwissLipids; SLP:000001611; -.
iPTMnet; P05093; -.
PhosphoSitePlus; P05093; -.
BioMuta; CYP17A1; -.
DMDM; 117283; -.
PaxDb; P05093; -.
PeptideAtlas; P05093; -.
PRIDE; P05093; -.
DNASU; 1586; -.
Ensembl; ENST00000369887; ENSP00000358903; ENSG00000148795.
GeneID; 1586; -.
KEGG; hsa:1586; -.
CTD; 1586; -.
DisGeNET; 1586; -.
EuPathDB; HostDB:ENSG00000148795.5; -.
GeneCards; CYP17A1; -.
HGNC; HGNC:2593; CYP17A1.
HPA; HPA048533; -.
MalaCards; CYP17A1; -.
MIM; 202110; phenotype.
MIM; 609300; gene.
neXtProt; NX_P05093; -.
OpenTargets; ENSG00000148795; -.
Orphanet; 90796; 46,XY disorder of sex development due to isolated 17,20 lyase deficiency.
Orphanet; 90793; Congenital adrenal hyperplasia due to 17-alpha-hydroxylase deficiency.
PharmGKB; PA27090; -.
eggNOG; KOG0156; Eukaryota.
eggNOG; COG2124; LUCA.
GeneTree; ENSGT00880000137854; -.
HOGENOM; HOG000036991; -.
HOVERGEN; HBG106944; -.
InParanoid; P05093; -.
KO; K00512; -.
OMA; YGPIYSF; -.
OrthoDB; EOG091G0BT8; -.
PhylomeDB; P05093; -.
TreeFam; TF105095; -.
BioCyc; MetaCyc:HS07560-MONOMER; -.
BRENDA; 1.14.99.9; 2681.
Reactome; R-HSA-193048; Androgen biosynthesis.
Reactome; R-HSA-194002; Glucocorticoid biosynthesis.
Reactome; R-HSA-211976; Endogenous sterols.
SABIO-RK; P05093; -.
SIGNOR; P05093; -.
UniPathway; UPA00062; -.
ChiTaRS; CYP17A1; human.
GeneWiki; CYP17A1; -.
GenomeRNAi; 1586; -.
PRO; PR:P05093; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000148795; -.
CleanEx; HS_CYP17A1; -.
ExpressionAtlas; P05093; baseline and differential.
Genevisible; P05093; HS.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; NAS:ProtInc.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0047442; F:17-alpha-hydroxyprogesterone aldolase activity; IMP:UniProtKB.
GO; GO:0020037; F:heme binding; IDA:UniProtKB.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0019825; F:oxygen binding; TAS:ProtInc.
GO; GO:0004508; F:steroid 17-alpha-monooxygenase activity; IDA:UniProtKB.
GO; GO:0006702; P:androgen biosynthetic process; TAS:Reactome.
GO; GO:0006704; P:glucocorticoid biosynthetic process; TAS:Reactome.
GO; GO:0042446; P:hormone biosynthetic process; IDA:UniProtKB.
GO; GO:0042448; P:progesterone metabolic process; IDA:UniProtKB.
GO; GO:0007548; P:sex differentiation; TAS:ProtInc.
GO; GO:0006694; P:steroid biosynthetic process; TAS:ProtInc.
GO; GO:0008202; P:steroid metabolic process; IDA:UniProtKB.
GO; GO:0016125; P:sterol metabolic process; TAS:Reactome.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002401; Cyt_P450_E_grp-I.
Pfam; PF00067; p450; 1.
PRINTS; PR00463; EP450I.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Congenital adrenal hyperplasia;
Disease mutation; Heme; Iron; Lyase; Membrane; Metal-binding;
Monooxygenase; Oxidoreductase; Phosphoprotein; Polymorphism;
Reference proteome; Steroidogenesis.
CHAIN 1 508 Steroid 17-alpha-hydroxylase/17,20 lyase.
/FTId=PRO_0000051931.
METAL 442 442 Iron (heme axial ligand).
VARIANT 22 22 C -> W (in dbSNP:rs762563).
/FTId=VAR_011755.
VARIANT 35 35 P -> L (in AH5; 38% 17alpha-hydroxylase
activity and 33% 17,20-lyase activity).
{ECO:0000269|PubMed:10720067}.
/FTId=VAR_022745.
VARIANT 53 53 Missing (in AH5; 10% 17alpha-hydroxylase
activity and 13% 17,20-lyase activity).
{ECO:0000269|PubMed:10720067,
ECO:0000269|PubMed:19793597,
ECO:0000269|PubMed:2808364}.
/FTId=VAR_001270.
VARIANT 64 64 Y -> S (in AH5).
{ECO:0000269|PubMed:8396144}.
/FTId=VAR_001271.
VARIANT 93 93 F -> C (in AH5; dbSNP:rs104894146).
{ECO:0000269|PubMed:11836339}.
/FTId=VAR_013147.
VARIANT 96 96 R -> Q (in AH5; dbSNP:rs104894153).
{ECO:0000269|PubMed:24498484}.
/FTId=VAR_073043.
VARIANT 96 96 R -> W (in AH5; 25% of both 17alpha-
hydroxylase and 17,20-lyase activities;
dbSNP:rs104894138).
{ECO:0000269|PubMed:10720067,
ECO:0000269|PubMed:14671162,
ECO:0000269|PubMed:8550762}.
/FTId=VAR_022746.
VARIANT 106 106 S -> P (in AH5; dbSNP:rs104894135).
{ECO:0000269|PubMed:1714904}.
/FTId=VAR_001272.
VARIANT 112 112 I -> II (in AH5).
{ECO:0000269|PubMed:8396144}.
/FTId=VAR_001273.
VARIANT 114 114 F -> V (in AH5; dbSNP:rs104894147).
{ECO:0000269|PubMed:12466376}.
/FTId=VAR_022747.
VARIANT 116 116 D -> V (in AH5; dbSNP:rs104894148).
{ECO:0000269|PubMed:12466376}.
/FTId=VAR_022748.
VARIANT 121 121 W -> R (in AH5; partial loss of
activity). {ECO:0000269|PubMed:25650406}.
/FTId=VAR_073044.
VARIANT 174 174 A -> E (in AH5).
{ECO:0000269|PubMed:24140098}.
/FTId=VAR_073045.
VARIANT 177 177 N -> D (in AH5; 10% 17alpha-hydroxylase
and 17,20-lyase activities).
{ECO:0000269|PubMed:10720067}.
/FTId=VAR_022749.
VARIANT 329 329 Y -> D (in AH5; dbSNP:rs104894144).
{ECO:0000269|PubMed:14671162}.
/FTId=VAR_022750.
VARIANT 330 330 Missing (in AH5; complete loss of both
17alpha-hydroxylase and 17,20-lyase
activities).
{ECO:0000269|PubMed:10720067}.
/FTId=VAR_022751.
VARIANT 342 342 P -> T (in AH5; dbSNP:rs104894137).
{ECO:0000269|PubMed:1740503}.
/FTId=VAR_001274.
VARIANT 347 347 R -> C (in AH5; dbSNP:rs104894149).
{ECO:0000269|PubMed:12466376}.
/FTId=VAR_022752.
VARIANT 347 347 R -> H (in AH5; selectively ablates
17,20-lyase activity, while preserving
most 17alpha-hydroxylase activity;
dbSNP:rs61754278).
{ECO:0000269|PubMed:11549685,
ECO:0000269|PubMed:12466376,
ECO:0000269|Ref.20}.
/FTId=VAR_001275.
VARIANT 358 358 R -> Q (in AH5; selectively ablates
17,20-lyase activity, while preserving
most 17alpha-hydroxylase activity;
dbSNP:rs104894139).
{ECO:0000269|PubMed:11549685,
ECO:0000269|Ref.20}.
/FTId=VAR_001276.
VARIANT 362 362 R -> C (in AH5; dbSNP:rs104894142).
{ECO:0000269|PubMed:14671162}.
/FTId=VAR_022753.
VARIANT 373 373 H -> L (in AH5; dbSNP:rs760695410).
{ECO:0000269|PubMed:24140098,
ECO:0000269|PubMed:8245018}.
/FTId=VAR_001277.
VARIANT 373 373 H -> N (in AH5).
{ECO:0000269|PubMed:19793597}.
/FTId=VAR_073046.
VARIANT 406 406 W -> L (in AH5; complete loss of both
17alpha-hydroxylase and 17,20-lyase
activities).
{ECO:0000269|PubMed:24140098}.
/FTId=VAR_073047.
VARIANT 406 406 W -> R (in AH5; dbSNP:rs104894143).
{ECO:0000269|PubMed:14671162}.
/FTId=VAR_022754.
VARIANT 417 417 F -> C (in AH5; ablates both 17,20-lyase
activity and 17alpha-hydroxylase
activity; loss of heme-binding and loss
of phosphorylation; dbSNP:rs104894140).
{ECO:0000269|PubMed:10720067,
ECO:0000269|PubMed:11549685}.
/FTId=VAR_022755.
VARIANT 428 428 P -> L (in AH5; dbSNP:rs104894145).
{ECO:0000269|PubMed:14671162}.
/FTId=VAR_022756.
VARIANT 440 440 R -> H (in AH5; dbSNP:rs777638364).
{ECO:0000269|PubMed:8027220}.
/FTId=VAR_001278.
VARIANT 487 489 Missing (in AH5).
{ECO:0000269|PubMed:8345056}.
/FTId=VAR_001279.
VARIANT 496 496 R -> C (in AH5).
{ECO:0000269|PubMed:1515452}.
/FTId=VAR_001280.
VARIANT 496 496 R -> H (in AH5; 30% 17alpha-hydroxylase
activity and 29% 17,20-lyase activity;
dbSNP:rs763398879).
{ECO:0000269|PubMed:10720067}.
/FTId=VAR_022757.
STRAND 36 42 {ECO:0000244|PDB:3SWZ}.
HELIX 49 55 {ECO:0000244|PDB:3SWZ}.
HELIX 57 60 {ECO:0000244|PDB:3SWZ}.
STRAND 62 68 {ECO:0000244|PDB:3SWZ}.
STRAND 71 76 {ECO:0000244|PDB:3SWZ}.
HELIX 79 86 {ECO:0000244|PDB:3SWZ}.
TURN 87 93 {ECO:0000244|PDB:3SWZ}.
HELIX 100 105 {ECO:0000244|PDB:3SWZ}.
TURN 106 109 {ECO:0000244|PDB:3SWZ}.
STRAND 111 115 {ECO:0000244|PDB:3SWZ}.
HELIX 119 131 {ECO:0000244|PDB:3SWZ}.
TURN 132 135 {ECO:0000244|PDB:3SWZ}.
STRAND 136 138 {ECO:0000244|PDB:3SWZ}.
HELIX 142 159 {ECO:0000244|PDB:3SWZ}.
TURN 160 162 {ECO:0000244|PDB:3SWZ}.
STRAND 163 165 {ECO:0000244|PDB:3SWZ}.
HELIX 168 184 {ECO:0000244|PDB:3SWZ}.
HELIX 194 209 {ECO:0000244|PDB:3SWZ}.
STRAND 211 214 {ECO:0000244|PDB:3SWZ}.
HELIX 220 222 {ECO:0000244|PDB:3SWZ}.
HELIX 228 250 {ECO:0000244|PDB:3SWZ}.
TURN 251 253 {ECO:0000244|PDB:3SWZ}.
HELIX 262 271 {ECO:0000244|PDB:3SWZ}.
HELIX 285 287 {ECO:0000244|PDB:3SWZ}.
HELIX 289 320 {ECO:0000244|PDB:3SWZ}.
HELIX 322 335 {ECO:0000244|PDB:3SWZ}.
STRAND 338 340 {ECO:0000244|PDB:3SWZ}.
HELIX 344 348 {ECO:0000244|PDB:3SWZ}.
HELIX 351 363 {ECO:0000244|PDB:3SWZ}.
STRAND 376 381 {ECO:0000244|PDB:3SWZ}.
STRAND 384 386 {ECO:0000244|PDB:3SWZ}.
STRAND 391 394 {ECO:0000244|PDB:3SWZ}.
HELIX 396 401 {ECO:0000244|PDB:3SWZ}.
TURN 403 405 {ECO:0000244|PDB:3SWZ}.
STRAND 406 408 {ECO:0000244|PDB:3SWZ}.
HELIX 414 417 {ECO:0000244|PDB:3SWZ}.
STRAND 422 425 {ECO:0000244|PDB:3SWZ}.
HELIX 438 440 {ECO:0000244|PDB:3SWZ}.
HELIX 445 462 {ECO:0000244|PDB:3SWZ}.
STRAND 463 466 {ECO:0000244|PDB:3SWZ}.
STRAND 479 485 {ECO:0000244|PDB:3SWZ}.
STRAND 491 495 {ECO:0000244|PDB:3SWZ}.
HELIX 497 501 {ECO:0000244|PDB:3SWZ}.
SEQUENCE 508 AA; 57371 MW; E5454E9E18F96B0E CRC64;
MWELVALLLL TLAYLFWPKR RCPGAKYPKS LLSLPLVGSL PFLPRHGHMH NNFFKLQKKY
GPIYSVRMGT KTTVIVGHHQ LAKEVLIKKG KDFSGRPQMA TLDIASNNRK GIAFADSGAH
WQLHRRLAMA TFALFKDGDQ KLEKIICQEI STLCDMLATH NGQSIDISFP VFVAVTNVIS
LICFNTSYKN GDPELNVIQN YNEGIIDNLS KDSLVDLVPW LKIFPNKTLE KLKSHVKIRN
DLLNKILENY KEKFRSDSIT NMLDTLMQAK MNSDNGNAGP DQDSELLSDN HILTTIGDIF
GAGVETTTSV VKWTLAFLLH NPQVKKKLYE EIDQNVGFSR TPTISDRNRL LLLEATIREV
LRLRPVAPML IPHKANVDSS IGEFAVDKGT EVIINLWALH HNEKEWHQPD QFMPERFLNP
AGTQLISPSV SYLPFGAGPR SCIGEILARQ ELFLIMAWLL QRFDLEVPDD GQLPSLEGIP
KVVFLIDSFK VKIKVRQAWR EAQAEGST


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