{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P05093","secondaryAccessions":["Q5TZV7"],"uniProtkbId":"CP17A_HUMAN","entryAudit":{"firstPublicDate":"1987-08-13","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1987-08-13","entryVersion":245,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"3025870"}],"value":"Steroid 17-alpha-hydroxylase/17,20 lyase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22266943"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25301938"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27339894"}],"value":"1.14.14.19"}]},"alternativeNames":[{"fullName":{"value":"17-alpha-hydroxyprogesterone aldolase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22266943"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25301938"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27339894"}],"value":"1.14.14.32"}]},{"fullName":{"value":"CYPXVII"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"27339894"}],"value":"Cytochrome P450 17A1"}},{"fullName":{"value":"Cytochrome P450-C17"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8396144"}],"value":"Cytochrome P450c17"}]},{"fullName":{"value":"Steroid 17-alpha-monooxygenase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19793597"},{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:2593"}],"value":"CYP17A1"},"synonyms":[{"value":"CYP17"},{"value":"S17AH"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22266943"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25301938"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27339894"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36640554"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9452426"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"8027220"}],"value":"A cytochrome P450 monooxygenase involved in corticoid and androgen biosynthesis (PubMed:22266943, PubMed:25301938, PubMed:27339894, PubMed:9452426). Catalyzes 17-alpha hydroxylation of C21 steroids, which is common for both pathways. A second oxidative step, required only for androgen synthesis, involves an acyl-carbon cleavage. The 17-alpha hydroxy intermediates, as part of adrenal glucocorticoids biosynthesis pathway, are precursors of cortisol (Probable) (PubMed:25301938, PubMed:9452426). Hydroxylates steroid hormones, pregnenolone and progesterone to form 17-alpha hydroxy metabolites, followed by the cleavage of the C17-C20 bond to form C19 steroids, dehydroepiandrosterone (DHEA) and androstenedione (PubMed:22266943, PubMed:25301938, PubMed:27339894, PubMed:36640554, PubMed:9452426). Has 16-alpha hydroxylase activity. Catalyzes 16-alpha hydroxylation of 17-alpha hydroxy pregnenolone, followed by the cleavage of the C17-C20 bond to form 16-alpha-hydroxy DHEA (PubMed:36640554). Also 16-alpha hydroxylates androgens, relevant for estriol synthesis (PubMed:25301938, PubMed:27339894). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase) (PubMed:22266943, PubMed:25301938, PubMed:27339894, PubMed:9452426)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a C21-steroid + reduced [NADPH--hemoprotein reductase] + O2 = a 17alpha-hydroxy-C21-steroid + oxidized [NADPH--hemoprotein reductase] + H2O + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:65760"},{"database":"Rhea","id":"RHEA-COMP:11964"},{"database":"Rhea","id":"RHEA-COMP:11965"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:57618"},{"database":"ChEBI","id":"CHEBI:58210"},{"database":"ChEBI","id":"CHEBI:61313"},{"database":"ChEBI","id":"CHEBI:138141"}],"ecNumber":"1.14.14.19","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22266943"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25301938"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27339894"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:65761"},"evidences":[{"evidenceCode":"ECO:0000305"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"progesterone + reduced [NADPH--hemoprotein reductase] + O2 = 17alpha-hydroxyprogesterone + oxidized [NADPH--hemoprotein reductase] + H2O + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46308"},{"database":"Rhea","id":"RHEA-COMP:11964"},{"database":"Rhea","id":"RHEA-COMP:11965"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:17026"},{"database":"ChEBI","id":"CHEBI:17252"},{"database":"ChEBI","id":"CHEBI:57618"},{"database":"ChEBI","id":"CHEBI:58210"}],"ecNumber":"1.14.14.19","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25301938"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36640554"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9452426"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:46309"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"9452426"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"pregnenolone + reduced [NADPH--hemoprotein reductase] + O2 = 17alpha-hydroxypregnenolone + oxidized [NADPH--hemoprotein reductase] + H2O + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:50236"},{"database":"Rhea","id":"RHEA-COMP:11964"},{"database":"Rhea","id":"RHEA-COMP:11965"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16581"},{"database":"ChEBI","id":"CHEBI:28750"},{"database":"ChEBI","id":"CHEBI:57618"},{"database":"ChEBI","id":"CHEBI:58210"}],"ecNumber":"1.14.14.19","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36640554"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9452426"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:50237"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"9452426"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"17alpha-hydroxyprogesterone + reduced [NADPH--hemoprotein reductase] + O2 = androst-4-ene-3,17-dione + acetate + oxidized [NADPH--hemoprotein reductase] + H2O + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:14753"},{"database":"Rhea","id":"RHEA-COMP:11964"},{"database":"Rhea","id":"RHEA-COMP:11965"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16422"},{"database":"ChEBI","id":"CHEBI:17252"},{"database":"ChEBI","id":"CHEBI:30089"},{"database":"ChEBI","id":"CHEBI:57618"},{"database":"ChEBI","id":"CHEBI:58210"}],"ecNumber":"1.14.14.32","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22266943"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27339894"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36640554"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:14754"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"22266943"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"17alpha-hydroxyprogesterone + reduced [NADPH--hemoprotein reductase] + O2 = 16alpha,17alpha-dihydroxyprogesterone + oxidized [NADPH--hemoprotein reductase] + H2O + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:53216"},{"database":"Rhea","id":"RHEA-COMP:11964"},{"database":"Rhea","id":"RHEA-COMP:11965"},{"database":"ChEBI","id":"CHEBI:763"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:17252"},{"database":"ChEBI","id":"CHEBI:57618"},{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27339894"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:53217"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"27339894"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"16alpha,17alpha-dihydroxyprogesterone + reduced [NADPH--hemoprotein reductase] + O2 = 6beta,16alpha,17alpha-trihydroxyprogesterone + oxidized [NADPH--hemoprotein reductase] + H2O + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:53220"},{"database":"Rhea","id":"RHEA-COMP:11964"},{"database":"Rhea","id":"RHEA-COMP:11965"},{"database":"ChEBI","id":"CHEBI:763"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:57618"},{"database":"ChEBI","id":"CHEBI:58210"},{"database":"ChEBI","id":"CHEBI:137046"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27339894"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:53221"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"27339894"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"17alpha-hydroxypregnenolone + reduced [NADPH--hemoprotein reductase] + O2 = 3beta-hydroxyandrost-5-en-17-one + acetate + oxidized [NADPH--hemoprotein reductase] + H2O + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:50244"},{"database":"Rhea","id":"RHEA-COMP:11964"},{"database":"Rhea","id":"RHEA-COMP:11965"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:28689"},{"database":"ChEBI","id":"CHEBI:28750"},{"database":"ChEBI","id":"CHEBI:30089"},{"database":"ChEBI","id":"CHEBI:57618"},{"database":"ChEBI","id":"CHEBI:58210"}],"ecNumber":"1.14.14.32","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22266943"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25301938"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27339894"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:50245"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"22266943"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"16alpha,17alpha-dihydroxypregnenolone + reduced [NADPH--hemoprotein reductase] + O2 = 3beta,16alpha-dihydroxy-androst-5-en-17-one + acetate + oxidized [NADPH--hemoprotein reductase] + H2O + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:53224"},{"database":"Rhea","id":"RHEA-COMP:11964"},{"database":"Rhea","id":"RHEA-COMP:11965"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:27771"},{"database":"ChEBI","id":"CHEBI:30089"},{"database":"ChEBI","id":"CHEBI:57618"},{"database":"ChEBI","id":"CHEBI:58210"},{"database":"ChEBI","id":"CHEBI:137049"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25301938"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27339894"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:53225"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"27339894"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"3beta-hydroxyandrost-5-en-17-one + reduced [NADPH--hemoprotein reductase] + O2 = 3beta,16alpha-dihydroxy-androst-5-en-17-one + oxidized [NADPH--hemoprotein reductase] + H2O + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:47220"},{"database":"Rhea","id":"RHEA-COMP:11964"},{"database":"Rhea","id":"RHEA-COMP:11965"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:27771"},{"database":"ChEBI","id":"CHEBI:28689"},{"database":"ChEBI","id":"CHEBI:57618"},{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27339894"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:47221"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"27339894"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"androst-4-ene-3,17-dione + reduced [NADPH--hemoprotein reductase] + O2 = 16alpha-hydroxyandrost-4-ene-3,17-dione + oxidized [NADPH--hemoprotein reductase] + H2O + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:53228"},{"database":"Rhea","id":"RHEA-COMP:11964"},{"database":"Rhea","id":"RHEA-COMP:11965"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16422"},{"database":"ChEBI","id":"CHEBI:27582"},{"database":"ChEBI","id":"CHEBI:57618"},{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27339894"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:53229"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"27339894"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"heme","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22266943"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25301938"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:30413"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10720067"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27339894"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9452426"}],"value":"Regulated predominantly by intracellular cAMP levels (PubMed:10720067). The 17,20-lyase activity is stimulated by cytochrome b5, which acts as an allosteric effector increasing the Vmax of the lyase activity (PubMed:27339894, PubMed:9452426)"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":10.5,"unit":"uM","substrate":"progesterone (17-alpha hydroxylation)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25301938"}]},{"constant":5.87,"unit":"uM","substrate":"progesterone (17-alpha hydroxylation)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36640554"}]},{"constant":0.93,"unit":"uM","substrate":"pregnenolone (17-alpha hydroxylation)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25301938"}]},{"constant":1.19,"unit":"uM","substrate":"pregnenolone (17-alpha hydroxylation)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36640554"}]},{"constant":1.2,"unit":"uM","substrate":"17alpha-hydroxypregnenolone (17,20 lyase activity)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25301938"}]},{"constant":21.9,"unit":"uM","substrate":"17alpha-hydroxyprogesterone (17,20 lyase activity)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36640554"}]}],"note":{"texts":[{"value":"kcat is 1.01 min(-1) with progesterone as substrate. kcat is 0.39 min(-1) with pregnenolone as substrate. kcat is 0.24 min(-1) with 17alpha-hydroxypregnenolone as substrate."}]}}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22266943"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25301938"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27339894"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9452426"}],"value":"Steroid hormone biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25301938"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9452426"}],"value":"Steroid biosynthesis; glucocorticoid biosynthesis"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"2808364"}],"value":"Endoplasmic reticulum membrane","id":"SL-0097"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"2808364"}],"value":"Microsome membrane","id":"SL-0165"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10720067"}],"value":"Phosphorylation is necessary for 17,20-lyase, but not for 17-alpha-hydroxylase activity"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Adrenal hyperplasia 5","diseaseAccession":"DI-00045","acronym":"AH5","description":"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).","diseaseCrossReference":{"database":"MIM","id":"202110"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10720067"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11549685"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11836339"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12466376"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14671162"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1515452"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1714904"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1740503"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19793597"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24140098"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24498484"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25650406"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2808364"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8027220"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8245018"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8345056"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8396144"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8550762"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.24"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the cytochrome P450 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":508,"modifier":"EXACT"}},"description":"Steroid 17-alpha-hydroxylase/17,20 lyase","featureId":"PRO_0000051931"},{"type":"Binding site","location":{"start":{"value":202,"modifier":"EXACT"},"end":{"value":202,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25301938"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":442,"modifier":"EXACT"},"end":{"value":442,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30413"},{"database":"ChEBI","id":"CHEBI:18248"}],"ligand":{"name":"heme","id":"ChEBI:CHEBI:30413"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Natural variant","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"in dbSNP:rs762563","featureCrossReferences":[{"database":"dbSNP","id":"rs762563"}],"featureId":"VAR_011755","alternativeSequence":{"originalSequence":"C","alternativeSequences":["W"]}},{"type":"Natural variant","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"in AH5; 38% 17alpha-hydroxylase activity and 33% 17,20-lyase activity","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10720067"}],"featureId":"VAR_022745","alternativeSequence":{"originalSequence":"P","alternativeSequences":["L"]}},{"type":"Natural variant","location":{"start":{"value":53,"modifier":"EXACT"},"end":{"value":53,"modifier":"EXACT"}},"description":"in AH5; 10% 17alpha-hydroxylase activity and 13% 17,20-lyase activity","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10720067"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19793597"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2808364"}],"featureId":"VAR_001270","alternativeSequence":{}},{"type":"Natural variant","location":{"start":{"value":64,"modifier":"EXACT"},"end":{"value":64,"modifier":"EXACT"}},"description":"in AH5; dbSNP:rs1183147390","featureCrossReferences":[{"database":"dbSNP","id":"rs1183147390"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8396144"}],"featureId":"VAR_001271","alternativeSequence":{"originalSequence":"Y","alternativeSequences":["S"]}},{"type":"Natural variant","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"in AH5; dbSNP:rs104894146","featureCrossReferences":[{"database":"dbSNP","id":"rs104894146"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11836339"}],"featureId":"VAR_013147","alternativeSequence":{"originalSequence":"F","alternativeSequences":["C"]}},{"type":"Natural variant","location":{"start":{"value":96,"modifier":"EXACT"},"end":{"value":96,"modifier":"EXACT"}},"description":"in AH5; dbSNP:rs104894153","featureCrossReferences":[{"database":"dbSNP","id":"rs104894153"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24498484"}],"featureId":"VAR_073043","alternativeSequence":{"originalSequence":"R","alternativeSequences":["Q"]}},{"type":"Natural variant","location":{"start":{"value":96,"modifier":"EXACT"},"end":{"value":96,"modifier":"EXACT"}},"description":"in AH5; 25% of both 17alpha-hydroxylase and 17,20-lyase activities; dbSNP:rs104894138","featureCrossReferences":[{"database":"dbSNP","id":"rs104894138"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10720067"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14671162"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8550762"}],"featureId":"VAR_022746","alternativeSequence":{"originalSequence":"R","alternativeSequences":["W"]}},{"type":"Natural variant","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"in AH5; dbSNP:rs104894135","featureCrossReferences":[{"database":"dbSNP","id":"rs104894135"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1714904"}],"featureId":"VAR_001272","alternativeSequence":{"originalSequence":"S","alternativeSequences":["P"]}},{"type":"Natural variant","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":112,"modifier":"EXACT"}},"description":"in AH5","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8396144"}],"featureId":"VAR_001273","alternativeSequence":{"originalSequence":"I","alternativeSequences":["II"]}},{"type":"Natural variant","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"in AH5; dbSNP:rs104894147","featureCrossReferences":[{"database":"dbSNP","id":"rs104894147"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12466376"}],"featureId":"VAR_022747","alternativeSequence":{"originalSequence":"F","alternativeSequences":["V"]}},{"type":"Natural variant","location":{"start":{"value":116,"modifier":"EXACT"},"end":{"value":116,"modifier":"EXACT"}},"description":"in AH5; dbSNP:rs104894148","featureCrossReferences":[{"database":"dbSNP","id":"rs104894148"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12466376"}],"featureId":"VAR_022748","alternativeSequence":{"originalSequence":"D","alternativeSequences":["V"]}},{"type":"Natural variant","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":121,"modifier":"EXACT"}},"description":"in AH5; partial loss of activity","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25650406"}],"featureId":"VAR_073044","alternativeSequence":{"originalSequence":"W","alternativeSequences":["R"]}},{"type":"Natural variant","location":{"start":{"value":174,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"in AH5; dbSNP:rs752540777","featureCrossReferences":[{"database":"dbSNP","id":"rs752540777"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24140098"}],"featureId":"VAR_073045","alternativeSequence":{"originalSequence":"A","alternativeSequences":["E"]}},{"type":"Natural variant","location":{"start":{"value":177,"modifier":"EXACT"},"end":{"value":177,"modifier":"EXACT"}},"description":"in AH5; 10% 17alpha-hydroxylase and 17,20-lyase activities","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10720067"}],"featureId":"VAR_022749","alternativeSequence":{"originalSequence":"N","alternativeSequences":["D"]}},{"type":"Natural variant","location":{"start":{"value":329,"modifier":"EXACT"},"end":{"value":329,"modifier":"EXACT"}},"description":"in AH5; dbSNP:rs104894144","featureCrossReferences":[{"database":"dbSNP","id":"rs104894144"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14671162"}],"featureId":"VAR_022750","alternativeSequence":{"originalSequence":"Y","alternativeSequences":["D"]}},{"type":"Natural variant","location":{"start":{"value":330,"modifier":"EXACT"},"end":{"value":330,"modifier":"EXACT"}},"description":"in AH5; complete loss of both 17alpha-hydroxylase and 17,20-lyase activities; dbSNP:rs759060233","featureCrossReferences":[{"database":"dbSNP","id":"rs759060233"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10720067"}],"featureId":"VAR_022751","alternativeSequence":{}},{"type":"Natural variant","location":{"start":{"value":342,"modifier":"EXACT"},"end":{"value":342,"modifier":"EXACT"}},"description":"in AH5; dbSNP:rs104894137","featureCrossReferences":[{"database":"dbSNP","id":"rs104894137"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1740503"}],"featureId":"VAR_001274","alternativeSequence":{"originalSequence":"P","alternativeSequences":["T"]}},{"type":"Natural variant","location":{"start":{"value":347,"modifier":"EXACT"},"end":{"value":347,"modifier":"EXACT"}},"description":"in AH5; dbSNP:rs104894149","featureCrossReferences":[{"database":"dbSNP","id":"rs104894149"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12466376"}],"featureId":"VAR_022752","alternativeSequence":{"originalSequence":"R","alternativeSequences":["C"]}},{"type":"Natural variant","location":{"start":{"value":347,"modifier":"EXACT"},"end":{"value":347,"modifier":"EXACT"}},"description":"in AH5; selectively ablates 17,20-lyase activity, while preserving most 17alpha-hydroxylase activity; dbSNP:rs61754278","featureCrossReferences":[{"database":"dbSNP","id":"rs61754278"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11549685"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12466376"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.24"}],"featureId":"VAR_001275","alternativeSequence":{"originalSequence":"R","alternativeSequences":["H"]}},{"type":"Natural variant","location":{"start":{"value":358,"modifier":"EXACT"},"end":{"value":358,"modifier":"EXACT"}},"description":"in AH5; selectively ablates 17,20-lyase activity, while preserving most 17alpha-hydroxylase activity; dbSNP:rs104894139","featureCrossReferences":[{"database":"dbSNP","id":"rs104894139"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11549685"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.24"}],"featureId":"VAR_001276","alternativeSequence":{"originalSequence":"R","alternativeSequences":["Q"]}},{"type":"Natural variant","location":{"start":{"value":362,"modifier":"EXACT"},"end":{"value":362,"modifier":"EXACT"}},"description":"in AH5; dbSNP:rs104894142","featureCrossReferences":[{"database":"dbSNP","id":"rs104894142"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14671162"}],"featureId":"VAR_022753","alternativeSequence":{"originalSequence":"R","alternativeSequences":["C"]}},{"type":"Natural variant","location":{"start":{"value":373,"modifier":"EXACT"},"end":{"value":373,"modifier":"EXACT"}},"description":"in AH5; dbSNP:rs760695410","featureCrossReferences":[{"database":"dbSNP","id":"rs760695410"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24140098"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8245018"}],"featureId":"VAR_001277","alternativeSequence":{"originalSequence":"H","alternativeSequences":["L"]}},{"type":"Natural variant","location":{"start":{"value":373,"modifier":"EXACT"},"end":{"value":373,"modifier":"EXACT"}},"description":"in AH5; dbSNP:rs1423560123","featureCrossReferences":[{"database":"dbSNP","id":"rs1423560123"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19793597"}],"featureId":"VAR_073046","alternativeSequence":{"originalSequence":"H","alternativeSequences":["N"]}},{"type":"Natural variant","location":{"start":{"value":406,"modifier":"EXACT"},"end":{"value":406,"modifier":"EXACT"}},"description":"in AH5; complete loss of both 17alpha-hydroxylase and 17,20-lyase activities","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24140098"}],"featureId":"VAR_073047","alternativeSequence":{"originalSequence":"W","alternativeSequences":["L"]}},{"type":"Natural variant","location":{"start":{"value":406,"modifier":"EXACT"},"end":{"value":406,"modifier":"EXACT"}},"description":"in AH5; dbSNP:rs104894143","featureCrossReferences":[{"database":"dbSNP","id":"rs104894143"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14671162"}],"featureId":"VAR_022754","alternativeSequence":{"originalSequence":"W","alternativeSequences":["R"]}},{"type":"Natural variant","location":{"start":{"value":417,"modifier":"EXACT"},"end":{"value":417,"modifier":"EXACT"}},"description":"in AH5; ablates both 17,20-lyase activity and 17alpha-hydroxylase activity; loss of heme-binding and loss of phosphorylation; dbSNP:rs104894140","featureCrossReferences":[{"database":"dbSNP","id":"rs104894140"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10720067"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11549685"}],"featureId":"VAR_022755","alternativeSequence":{"originalSequence":"F","alternativeSequences":["C"]}},{"type":"Natural variant","location":{"start":{"value":428,"modifier":"EXACT"},"end":{"value":428,"modifier":"EXACT"}},"description":"in AH5; dbSNP:rs104894145","featureCrossReferences":[{"database":"dbSNP","id":"rs104894145"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14671162"}],"featureId":"VAR_022756","alternativeSequence":{"originalSequence":"P","alternativeSequences":["L"]}},{"type":"Natural variant","location":{"start":{"value":440,"modifier":"EXACT"},"end":{"value":440,"modifier":"EXACT"}},"description":"in AH5; dbSNP:rs777638364","featureCrossReferences":[{"database":"dbSNP","id":"rs777638364"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8027220"}],"featureId":"VAR_001278","alternativeSequence":{"originalSequence":"R","alternativeSequences":["H"]}},{"type":"Natural variant","location":{"start":{"value":487,"modifier":"EXACT"},"end":{"value":489,"modifier":"EXACT"}},"description":"in AH5","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8345056"}],"featureId":"VAR_001279","alternativeSequence":{}},{"type":"Natural variant","location":{"start":{"value":496,"modifier":"EXACT"},"end":{"value":496,"modifier":"EXACT"}},"description":"in AH5; dbSNP:rs1250463562","featureCrossReferences":[{"database":"dbSNP","id":"rs1250463562"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1515452"}],"featureId":"VAR_001280","alternativeSequence":{"originalSequence":"R","alternativeSequences":["C"]}},{"type":"Natural variant","location":{"start":{"value":496,"modifier":"EXACT"},"end":{"value":496,"modifier":"EXACT"}},"description":"in AH5; 30% 17alpha-hydroxylase activity and 29% 17,20-lyase activity; dbSNP:rs763398879","featureCrossReferences":[{"database":"dbSNP","id":"rs763398879"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10720067"}],"featureId":"VAR_022757","alternativeSequence":{"originalSequence":"R","alternativeSequences":["H"]}},{"type":"Mutagenesis","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"Increases the affinity for progesterone, resulting in preferential hydroxylation of progesterone at C17 over C16; increases the catalytic efficiency in the 17,20 lyase reaction.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25301938"}],"alternativeSequence":{"originalSequence":"A","alternativeSequences":["L"]}},{"type":"Helix","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Beta strand","location":{"start":{"value":36,"modifier":"EXACT"},"end":{"value":42,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WW0"}]},{"type":"Helix","location":{"start":{"value":49,"modifier":"EXACT"},"end":{"value":60,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Beta strand","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":68,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Beta strand","location":{"start":{"value":71,"modifier":"EXACT"},"end":{"value":76,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Helix","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":83,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Helix","location":{"start":{"value":84,"modifier":"EXACT"},"end":{"value":88,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Turn","location":{"start":{"value":89,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Helix","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Turn","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":109,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Beta strand","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5UYS"}]},{"type":"Helix","location":{"start":{"value":119,"modifier":"EXACT"},"end":{"value":132,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Helix","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":135,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Beta strand","location":{"start":{"value":136,"modifier":"EXACT"},"end":{"value":140,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WW0"}]},{"type":"Helix","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":159,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Turn","location":{"start":{"value":160,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Beta strand","location":{"start":{"value":163,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WW0"}]},{"type":"Helix","location":{"start":{"value":168,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Helix","location":{"start":{"value":193,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Helix","location":{"start":{"value":213,"modifier":"EXACT"},"end":{"value":217,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Helix","location":{"start":{"value":219,"modifier":"EXACT"},"end":{"value":221,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Helix","location":{"start":{"value":228,"modifier":"EXACT"},"end":{"value":251,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Helix","location":{"start":{"value":262,"modifier":"EXACT"},"end":{"value":271,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Beta strand","location":{"start":{"value":276,"modifier":"EXACT"},"end":{"value":278,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR0"}]},{"type":"Helix","location":{"start":{"value":284,"modifier":"EXACT"},"end":{"value":287,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Helix","location":{"start":{"value":289,"modifier":"EXACT"},"end":{"value":320,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Helix","location":{"start":{"value":322,"modifier":"EXACT"},"end":{"value":335,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Beta strand","location":{"start":{"value":338,"modifier":"EXACT"},"end":{"value":340,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Helix","location":{"start":{"value":344,"modifier":"EXACT"},"end":{"value":348,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Helix","location":{"start":{"value":351,"modifier":"EXACT"},"end":{"value":363,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Beta strand","location":{"start":{"value":366,"modifier":"EXACT"},"end":{"value":368,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3RUK"}]},{"type":"Beta strand","location":{"start":{"value":376,"modifier":"EXACT"},"end":{"value":381,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Beta strand","location":{"start":{"value":384,"modifier":"EXACT"},"end":{"value":386,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Beta strand","location":{"start":{"value":391,"modifier":"EXACT"},"end":{"value":394,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Helix","location":{"start":{"value":396,"modifier":"EXACT"},"end":{"value":400,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Turn","location":{"start":{"value":403,"modifier":"EXACT"},"end":{"value":405,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Beta strand","location":{"start":{"value":406,"modifier":"EXACT"},"end":{"value":408,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Helix","location":{"start":{"value":414,"modifier":"EXACT"},"end":{"value":417,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Beta strand","location":{"start":{"value":422,"modifier":"EXACT"},"end":{"value":425,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WW0"}]},{"type":"Helix","location":{"start":{"value":438,"modifier":"EXACT"},"end":{"value":440,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Helix","location":{"start":{"value":445,"modifier":"EXACT"},"end":{"value":462,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Beta strand","location":{"start":{"value":463,"modifier":"EXACT"},"end":{"value":466,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Beta strand","location":{"start":{"value":469,"modifier":"EXACT"},"end":{"value":471,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6CIR"}]},{"type":"Helix","location":{"start":{"value":473,"modifier":"EXACT"},"end":{"value":475,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Beta strand","location":{"start":{"value":479,"modifier":"EXACT"},"end":{"value":485,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Helix","location":{"start":{"value":486,"modifier":"EXACT"},"end":{"value":488,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"8FDA"}]},{"type":"Beta strand","location":{"start":{"value":491,"modifier":"EXACT"},"end":{"value":495,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]},{"type":"Helix","location":{"start":{"value":497,"modifier":"EXACT"},"end":{"value":500,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6WR1"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0954","category":"Disease","name":"Congenital adrenal hyperplasia"},{"id":"KW-0225","category":"Disease","name":"Disease variant"},{"id":"KW-0256","category":"Cellular component","name":"Endoplasmic reticulum"},{"id":"KW-0349","category":"Ligand","name":"Heme"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0492","category":"Cellular component","name":"Microsome"},{"id":"KW-0503","category":"Molecular function","name":"Monooxygenase"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"id":"KW-1267","category":"Technical term","name":"Proteomics identification"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0755","category":"Biological process","name":"Steroidogenesis"}],"references":[{"referenceNumber":1,"citation":{"id":"3025870","citationType":"journal article","authors":["Chung B.-C.","Picado-Leonard J.","Haniu M.","Bienkowski M.","Hall P.F.","Shively J.E.","Miller W.L."],"citationCrossReferences":[{"database":"PubMed","id":"3025870"},{"database":"DOI","id":"10.1073/pnas.84.2.407"}],"title":"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.","publicationDate":"1987","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"407","lastPage":"411","volume":"84"},"referencePositions":["NUCLEOTIDE SEQUENCE [MRNA]"]},{"referenceNumber":2,"citation":{"id":"3500022","citationType":"journal article","authors":["Picado-Leonard J.","Miller W.L."],"citationCrossReferences":[{"database":"PubMed","id":"3500022"},{"database":"DOI","id":"10.1089/dna.1987.6.439"}],"title":"Cloning and sequence of the human gene for P450c17 (steroid 17 alpha-hydroxylase/17,20 lyase): similarity with the gene for P450c21.","publicationDate":"1987","journal":"DNA","firstPage":"439","lastPage":"448","volume":"6"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"]},{"referenceNumber":3,"citation":{"id":"3274893","citationType":"journal article","authors":["Bradshaw K.D.","Waterman M.R.","Couch R.T.","Simpson E.R.","Zuber M.X."],"citationCrossReferences":[{"database":"PubMed","id":"3274893"},{"database":"DOI","id":"10.1210/mend-1-5-348"}],"title":"Characterization of complementary deoxyribonucleic acid for human adrenocortical 17 alpha-hydroxylase: a probe for analysis of 17 alpha-hydroxylase deficiency.","publicationDate":"1987","journal":"Mol. Endocrinol.","firstPage":"348","lastPage":"354","volume":"1"},"referencePositions":["NUCLEOTIDE SEQUENCE [MRNA]"]},{"referenceNumber":4,"citation":{"id":"1964490","citationType":"journal article","authors":["Brentano S.T.","Picado-Leonard J.","Mellon S.H.","Moore C.C.","Miller W.L."],"citationCrossReferences":[{"database":"PubMed","id":"1964490"},{"database":"DOI","id":"10.1210/mend-4-12-1972"}],"title":"Tissue-specific, cyclic adenosine 3',5'-monophosphate-induced, and phorbol ester-repressed transcription from the human P450c17 promoter in mouse cells.","publicationDate":"1990","journal":"Mol. Endocrinol.","firstPage":"1972","lastPage":"1979","volume":"4"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"]},{"referenceNumber":5,"citation":{"id":"2843762","citationType":"journal article","authors":["Kagimoto M.","Winter J.S.D.","Kagimoto K.","Simpson E.R.","Waterman M.R."],"citationCrossReferences":[{"database":"PubMed","id":"2843762"},{"database":"DOI","id":"10.1210/mend-2-6-564"}],"title":"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.","publicationDate":"1988","journal":"Mol. Endocrinol.","firstPage":"564","lastPage":"570","volume":"2"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"]},{"referenceNumber":6,"citation":{"id":"CI-54UTT6AFSFO1R","citationType":"submission","authors":["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."],"title":"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.","publicationDate":"OCT-2004","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]"]},{"referenceNumber":7,"citation":{"id":"15164054","citationType":"journal article","authors":["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."],"citationCrossReferences":[{"database":"PubMed","id":"15164054"},{"database":"DOI","id":"10.1038/nature02462"}],"title":"The DNA sequence and comparative analysis of human chromosome 10.","publicationDate":"2004","journal":"Nature","firstPage":"375","lastPage":"381","volume":"429"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]},{"referenceNumber":8,"citation":{"id":"15489334","citationType":"journal article","authoringGroup":["The MGC Project Team"],"citationCrossReferences":[{"database":"PubMed","id":"15489334"},{"database":"DOI","id":"10.1101/gr.2596504"}],"title":"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).","publicationDate":"2004","journal":"Genome Res.","firstPage":"2121","lastPage":"2127","volume":"14"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]"],"referenceComments":[{"value":"Brain","type":"TISSUE"}]},{"referenceNumber":9,"citation":{"id":"9452426","citationType":"journal article","authors":["Auchus R.J.","Lee T.C.","Miller W.L."],"citationCrossReferences":[{"database":"PubMed","id":"9452426"},{"database":"DOI","id":"10.1074/jbc.273.6.3158"}],"title":"Cytochrome b5 augments the 17,20-lyase activity of human P450c17 without direct electron transfer.","publicationDate":"1998","journal":"J. Biol. Chem.","firstPage":"3158","lastPage":"3165","volume":"273"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","ACTIVITY REGULATION","PATHWAY"]},{"referenceNumber":10,"citation":{"id":"27339894","citationType":"journal article","authors":["Yoshimoto F.K.","Gonzalez E.","Auchus R.J.","Guengerich F.P."],"citationCrossReferences":[{"database":"PubMed","id":"27339894"},{"database":"DOI","id":"10.1074/jbc.m116.732966"}],"title":"Mechanism of 17alpha,20-Lyase and New Hydroxylation Reactions of Human Cytochrome P450 17A1: 18O LABELING AND OXYGEN SURROGATE EVIDENCE FOR A ROLE OF A PERFERRYL OXYGEN.","publicationDate":"2016","journal":"J. Biol. Chem.","firstPage":"17143","lastPage":"17164","volume":"291"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","ACTIVITY REGULATION","PATHWAY"]},{"referenceNumber":11,"citation":{"id":"36640554","citationType":"journal article","authors":["Lee S.G.","Kim V.","Lee G.H.","Kim C.","Jeong E.","Guengerich F.P.","Kim D."],"citationCrossReferences":[{"database":"PubMed","id":"36640554"},{"database":"DOI","id":"10.1016/j.jinorgbio.2022.112085"}],"title":"Hydroxylation and lyase reactions of steroids catalyzed by mouse cytochrome P450 17A1 (Cyp17a1).","publicationDate":"2023","journal":"J. Inorg. Biochem.","firstPage":"112085","lastPage":"112085","volume":"240"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","BIOPHYSICOCHEMICAL PROPERTIES"]},{"referenceNumber":12,"citation":{"id":"10406467","citationType":"journal article","authors":["Auchus R.J.","Miller W.L."],"citationCrossReferences":[{"database":"PubMed","id":"10406467"},{"database":"DOI","id":"10.1210/mend.13.7.0326"}],"title":"Molecular modeling of human P450c17 (17alpha-hydroxylase/17,20-lyase): insights into reaction mechanisms and effects of mutations.","publicationDate":"1999","journal":"Mol. Endocrinol.","firstPage":"1169","lastPage":"1182","volume":"13"},"referencePositions":["3D-STRUCTURE MODELING OF 48-501"]},{"referenceNumber":13,"citation":{"id":"22266943","citationType":"journal article","authors":["DeVore N.M.","Scott E.E."],"citationCrossReferences":[{"database":"PubMed","id":"22266943"},{"database":"DOI","id":"10.1038/nature10743"}],"title":"Structures of cytochrome P450 17A1 with prostate cancer drugs abiraterone and TOK-001.","publicationDate":"2012","journal":"Nature","firstPage":"116","lastPage":"119","volume":"482"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 24-508 IN COMPLEXES WITH HEME; ABIRATERONE AND TOK-001","FUNCTION","CATALYTIC ACTIVITY","COFACTOR","PATHWAY"]},{"referenceNumber":14,"citation":{"id":"25301938","citationType":"journal article","authors":["Petrunak E.M.","DeVore N.M.","Porubsky P.R.","Scott E.E."],"citationCrossReferences":[{"database":"PubMed","id":"25301938"},{"database":"DOI","id":"10.1074/jbc.m114.610998"}],"title":"Structures of human steroidogenic cytochrome P450 17A1 with substrates.","publicationDate":"2014","journal":"J. Biol. Chem.","firstPage":"32952","lastPage":"32964","volume":"289"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 24-508 IN COMPLEX WITH HEME AND PREGNENOLONE","FUNCTION","CATALYTIC ACTIVITY","COFACTOR","BIOPHYSICOCHEMICAL PROPERTIES","PATHWAY","MUTAGENESIS OF ALA-105"]},{"referenceNumber":15,"citation":{"id":"2808364","citationType":"journal article","authors":["Yanase T.","Kagimoto M.","Suzuki S.","Hashiba K.","Simpson E.R.","Waterman M.R."],"citationCrossReferences":[{"database":"PubMed","id":"2808364"},{"database":"DOI","id":"10.1016/s0021-9258(19)84680-x"}],"title":"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.","publicationDate":"1989","journal":"J. Biol. Chem.","firstPage":"18076","lastPage":"18082","volume":"264"},"referencePositions":["VARIANT AH5 PHE-53 DEL","SUBCELLULAR LOCATION"]},{"referenceNumber":16,"citation":{"id":"1714904","citationType":"journal article","authors":["Lin D.","Harikrishna J.A.","Moore C.C.D.","Jones K.L.","Miller W.L."],"citationCrossReferences":[{"database":"PubMed","id":"1714904"},{"database":"DOI","id":"10.1016/s0021-9258(18)98506-6"}],"title":"Missense mutation serine106-->proline causes 17 alpha-hydroxylase deficiency.","publicationDate":"1991","journal":"J. Biol. Chem.","firstPage":"15992","lastPage":"15998","volume":"266"},"referencePositions":["VARIANT AH5 PRO-106"]},{"referenceNumber":17,"citation":{"id":"1515452","citationType":"journal article","authors":["Yanase T.","Waterman M.R.","Zachmann M.","Winter J.S.D.","Kagimoto M."],"citationCrossReferences":[{"database":"PubMed","id":"1515452"},{"database":"DOI","id":"10.1016/0925-4439(92)90100-2"}],"title":"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.","publicationDate":"1992","journal":"Biochim. Biophys. Acta","firstPage":"275","lastPage":"279","volume":"1139"},"referencePositions":["VARIANT AH5 CYS-496"]},{"referenceNumber":18,"citation":{"id":"1740503","citationType":"journal article","authors":["Ahlgren R.","Yanase T.","Simpson E.R.","Winter J.S.D.","Waterman M.R."],"citationCrossReferences":[{"database":"PubMed","id":"1740503"},{"database":"DOI","id":"10.1210/jcem.74.3.1740503"}],"title":"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.","publicationDate":"1992","journal":"J. Clin. Endocrinol. Metab.","firstPage":"667","lastPage":"672","volume":"74"},"referencePositions":["VARIANT AH5 THR-342"]},{"referenceNumber":19,"citation":{"id":"8396144","citationType":"journal article","authors":["Imai T.","Globerman H.","Gertner J.M.","Kagawa N.","Waterman M.R."],"citationCrossReferences":[{"database":"PubMed","id":"8396144"},{"database":"DOI","id":"10.1016/s0021-9258(19)36570-6"}],"title":"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.","publicationDate":"1993","journal":"J. Biol. Chem.","firstPage":"19681","lastPage":"19689","volume":"268"},"referencePositions":["VARIANTS AH5 SER-64 AND ILE-112 INS"]},{"referenceNumber":20,"citation":{"id":"8245018","citationType":"journal article","authors":["Monno S.","Ogawa H.","Date T.","Fujioka M.","Miller W.L.","Kobayashi M."],"citationCrossReferences":[{"database":"PubMed","id":"8245018"},{"database":"DOI","id":"10.1016/s0021-9258(19)74462-7"}],"title":"Mutation of histidine 373 to leucine in cytochrome P450c17 causes 17 alpha-hydroxylase deficiency.","publicationDate":"1993","journal":"J. Biol. Chem.","firstPage":"25811","lastPage":"25817","volume":"268"},"referencePositions":["VARIANT AH5 LEU-373"]},{"referenceNumber":21,"citation":{"id":"8345056","citationType":"journal article","authors":["Fardella C.E.","Zhang L.H.","Mahacholklertwattana P.","Lin D.","Miller W.L."],"citationCrossReferences":[{"database":"PubMed","id":"8345056"},{"database":"DOI","id":"10.1210/jcem.77.2.8345056"}],"title":"Deletion of amino acids Asp487-Ser488-Phe489 in human cytochrome P450c17 causes severe 17 alpha-hydroxylase deficiency.","publicationDate":"1993","journal":"J. Clin. Endocrinol. Metab.","firstPage":"489","lastPage":"493","volume":"77"},"referencePositions":["VARIANT AH5 487-ASP--PHE-489 DEL"]},{"referenceNumber":22,"citation":{"id":"8027220","citationType":"journal article","authors":["Fardella C.E.","Hum D.W.","Homoki J.","Miller W.L."],"citationCrossReferences":[{"database":"PubMed","id":"8027220"},{"database":"DOI","id":"10.1210/jcem.79.1.8027220"}],"title":"Point mutation of Arg440 to His in cytochrome P450c17 causes severe 17 alpha-hydroxylase deficiency.","publicationDate":"1994","journal":"J. Clin. Endocrinol. Metab.","firstPage":"160","lastPage":"164","volume":"79"},"referencePositions":["VARIANT AH5 HIS-440"]},{"referenceNumber":23,"citation":{"id":"8550762","citationType":"journal article","authors":["Laflamme N.","Leblanc J.-F.","Mailloux J.","Faure N.","Labrie F.","Simard J."],"citationCrossReferences":[{"database":"PubMed","id":"8550762"},{"database":"DOI","id":"10.1210/jcem.81.1.8550762"}],"title":"Mutation R96W in cytochrome P450c17 gene causes combined 17 alpha-hydroxylase/17-20-lyase deficiency in two French Canadian patients.","publicationDate":"1996","journal":"J. Clin. Endocrinol. Metab.","firstPage":"264","lastPage":"268","volume":"81"},"referencePositions":["VARIANT AH5 TRP-96"]},{"referenceNumber":24,"citation":{"id":"CI-ARVS960VMATIB","citationType":"journal article","authors":["Geller D.H.","Mendonca B.B.","Miller W.L."],"title":"The molecular basis of isolated 17,20 lyase deficiency.","publicationDate":"1996","journal":"Pediatr. Res.","firstPage":"89A","lastPage":"89A","volume":"39"},"referencePositions":["VARIANTS AH5 HIS-347 AND GLN-358"]},{"referenceNumber":25,"citation":{"id":"10720067","citationType":"journal article","authors":["Biason-Lauber A.","Kempken B.","Werder E.","Forest M.G.","Einaudi S.","Ranke M.B.","Matsuo N.","Brunelli V.","Schoenle E.J.","Zachmann M."],"citationCrossReferences":[{"database":"PubMed","id":"10720067"},{"database":"DOI","id":"10.1210/jcem.85.3.6475"}],"title":"17alpha-hydroxylase/17,20-lyase deficiency as a model to study enzymatic activity regulation: role of phosphorylation.","publicationDate":"2000","journal":"J. Clin. Endocrinol. Metab.","firstPage":"1226","lastPage":"1231","volume":"85"},"referencePositions":["VARIANTS AH5 LEU-35; PHE-53 DEL; TRP-96; ASP-177; GLU-330 DEL; CYS-417 AND HIS-496","PHOSPHORYLATION"]},{"referenceNumber":26,"citation":{"id":"11549685","citationType":"journal article","authors":["Gupta M.K.","Geller D.H.","Auchus R.J."],"citationCrossReferences":[{"database":"PubMed","id":"11549685"},{"database":"DOI","id":"10.1210/jcem.86.9.7812"}],"title":"Pitfalls in characterizing P450c17 mutations associated with isolated 17,20-lyase deficiency.","publicationDate":"2001","journal":"J. Clin. Endocrinol. Metab.","firstPage":"4416","lastPage":"4423","volume":"86"},"referencePositions":["VARIANTS AH5 HIS-347; GLN-358 AND CYS-417"]},{"referenceNumber":27,"citation":{"id":"11836339","citationType":"journal article","authors":["Di Cerbo A.","Biason-Lauber A.","Savino M.","Piemontese M.R.","Di Giorgio A.","Perona M.","Savoia A."],"citationCrossReferences":[{"database":"PubMed","id":"11836339"},{"database":"DOI","id":"10.1210/jcem.87.2.8271"}],"title":"Combined 17alpha-hydroxylase/17,20-lyase deficiency caused by Phe93Cys mutation in the CYP17 gene.","publicationDate":"2002","journal":"J. Clin. Endocrinol. Metab.","firstPage":"898","lastPage":"905","volume":"87"},"referencePositions":["VARIANT AH5 CYS-93"]},{"referenceNumber":28,"citation":{"id":"12466376","citationType":"journal article","authors":["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."],"citationCrossReferences":[{"database":"PubMed","id":"12466376"},{"database":"DOI","id":"10.1210/jc.2001-011880"}],"title":"Differential inhibition of 17alpha-hydroxylase and 17,20-lyase activities by three novel missense CYP17 mutations identified in patients with P450c17 deficiency.","publicationDate":"2002","journal":"J. Clin. Endocrinol. Metab.","firstPage":"5714","lastPage":"5721","volume":"87"},"referencePositions":["VARIANTS AH5 VAL-114; VAL-116; CYS-347 AND HIS-347"]},{"referenceNumber":29,"citation":{"id":"14671162","citationType":"journal article","authors":["Martin R.M.","Lin C.J.","Costa E.M.F.","de Oliveira M.L.","Carrilho A.","Villar H.","Longui C.A.","Mendonca B.B."],"citationCrossReferences":[{"database":"PubMed","id":"14671162"},{"database":"DOI","id":"10.1210/jc.2003-030988"}],"title":"P450c17 deficiency in Brazilian patients: biochemical diagnosis through progesterone levels confirmed by CYP17 genotyping.","publicationDate":"2003","journal":"J. Clin. Endocrinol. Metab.","firstPage":"5739","lastPage":"5746","volume":"88"},"referencePositions":["VARIANTS AH5 TRP-96; ASP-329; CYS-362; ARG-406 AND LEU-428"]},{"referenceNumber":30,"citation":{"id":"19793597","citationType":"journal article","authors":["Katsumata N.","Ogawa E.","Fujiwara I.","Fujikura K."],"citationCrossReferences":[{"database":"PubMed","id":"19793597"},{"database":"DOI","id":"10.1016/j.metabol.2009.07.024"}],"title":"Novel CYP17A1 mutation in a Japanese patient with combined 17alpha-hydroxylase/17,20-lyase deficiency.","publicationDate":"2010","journal":"Metabolism","firstPage":"275","lastPage":"278","volume":"59"},"referencePositions":["VARIANTS AH5 PHE-53 DEL AND ASN-373"]},{"referenceNumber":31,"citation":{"id":"24498484","citationType":"journal article","authors":["Mula-Abed W.A.","Pambinezhuth F.B.","Al-Kindi M.K.","Al-Busaidi N.B.","Al-Muslahi H.N.","Al-Lamki M.A."],"citationCrossReferences":[{"database":"PubMed","id":"24498484"},{"database":"DOI","id":"10.5001/omj.2014.12"}],"title":"Congenital adrenal hyperplasia due to 17-alpha-hydoxylase/17,20-lyase deficiency presenting with hypertension and pseudohermaphroditism: first case report from Oman.","publicationDate":"2014","journal":"Oman Med. J.","firstPage":"55","lastPage":"59","volume":"29"},"referencePositions":["VARIANT AH5 GLN-96"]},{"referenceNumber":32,"citation":{"id":"24140098","citationType":"journal article","authors":["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."],"citationCrossReferences":[{"database":"PubMed","id":"24140098"},{"database":"DOI","id":"10.1016/j.metabol.2013.08.015"}],"title":"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.","publicationDate":"2014","journal":"Metabolism","firstPage":"42","lastPage":"49","volume":"63"},"referencePositions":["VARIANTS AH5 GLU-174; LEU-373 AND LEU-406","CHARACTERIZATION OF VARIANT AH5 LEU-406"]},{"referenceNumber":33,"citation":{"id":"25650406","citationType":"journal article","authors":["Rubtsov P.","Nizhnik A.","Dedov I.I.","Kalinchenko N.","Petrov V.","Orekhova A.","Spirin P.","Prassolov V.","Tiulpakov A."],"citationCrossReferences":[{"database":"PubMed","id":"25650406"},{"database":"DOI","id":"10.1530/eje-14-0834"}],"title":"Partial deficiency of 17alpha-hydroxylase/17,20-lyase caused by a novel missense mutation in the canonical cytochrome heme-interacting motif.","publicationDate":"2015","journal":"Eur. J. Endocrinol.","firstPage":"K19","lastPage":"25","volume":"172"},"referencePositions":["VARIANT AH5 ARG-121","CHARACTERIZATION OF VARIANT AH5 ARG-121"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"M14564","properties":[{"key":"ProteinId","value":"AAA52151.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"EMBL","id":"M19489","properties":[{"key":"ProteinId","value":"AAA36405.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"M63871","properties":[{"key":"ProteinId","value":"AAA59984.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"M31153","properties":[{"key":"ProteinId","value":"AAA52140.1"},{"key":"Status","value":"ALT_SEQ"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"M31146","properties":[{"key":"ProteinId","value":"AAA52140.1"},{"key":"Status","value":"JOINED"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"M31147","properties":[{"key":"ProteinId","value":"AAA52140.1"},{"key":"Status","value":"JOINED"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"M31148","properties":[{"key":"ProteinId","value":"AAA52140.1"},{"key":"Status","value":"JOINED"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"M31149","properties":[{"key":"ProteinId","value":"AAA52140.1"},{"key":"Status","value":"JOINED"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"M31150","properties":[{"key":"ProteinId","value":"AAA52140.1"},{"key":"Status","value":"JOINED"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"M31151","properties":[{"key":"ProteinId","value":"AAA52140.1"},{"key":"Status","value":"JOINED"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"M31152","properties":[{"key":"ProteinId","value":"AAA52140.1"},{"key":"Status","value":"JOINED"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"BT020000","properties":[{"key":"ProteinId","value":"AAV38803.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"EMBL","id":"AL358790","properties":[{"key":"ProteinId","value":"-"},{"key":"Status","value":"NOT_ANNOTATED_CDS"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"BC062997","properties":[{"key":"ProteinId","value":"AAH62997.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"EMBL","id":"BC063388","properties":[{"key":"ProteinId","value":"AAH63388.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"CCDS","id":"CCDS7541.1","properties":[{"key":"Description","value":"-"}]},{"database":"PIR","id":"A40921","properties":[{"key":"EntryName","value":"A26366"}]},{"database":"RefSeq","id":"NP_000093.1","properties":[{"key":"NucleotideSequenceId","value":"NM_000102.4"}]},{"database":"PDB","id":"3RUK","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.60 A"},{"key":"Chains","value":"A/B/C/D=24-508"}]},{"database":"PDB","id":"3SWZ","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.40 A"},{"key":"Chains","value":"A/B/C/D=24-508"}]},{"database":"PDB","id":"4NKV","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.65 A"},{"key":"Chains","value":"A/B/C/D=24-508"}]},{"database":"PDB","id":"4NKW","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.50 A"},{"key":"Chains","value":"A/B/C/D=24-508"}]},{"database":"PDB","id":"4NKX","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.79 A"},{"key":"Chains","value":"A/B/C/D=24-508"}]},{"database":"PDB","id":"4NKY","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.55 A"},{"key":"Chains","value":"A/B/C/D=24-508"}]},{"database":"PDB","id":"4NKZ","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"3.00 A"},{"key":"Chains","value":"A/B/C/D=24-508"}]},{"database":"PDB","id":"5IRQ","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.20 A"},{"key":"Chains","value":"A/B/C/D=24-508"}]},{"database":"PDB","id":"5IRV","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"3.10 A"},{"key":"Chains","value":"A/B/C/D=24-508"}]},{"database":"PDB","id":"5UYS","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.39 A"},{"key":"Chains","value":"A/B/C/D=24-508"}]},{"database":"PDB","id":"6CHI","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.70 A"},{"key":"Chains","value":"A/B/C/D=24-508"}]},{"database":"PDB","id":"6CIR","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.65 A"},{"key":"Chains","value":"A/B/C/D=24-508"}]},{"database":"PDB","id":"6CIZ","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.60 A"},{"key":"Chains","value":"A/B/C/D=24-508"}]},{"database":"PDB","id":"6WR0","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.70 A"},{"key":"Chains","value":"A/B/C/D=24-508"}]},{"database":"PDB","id":"6WR1","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.85 A"},{"key":"Chains","value":"A/B=24-508"}]},{"database":"PDB","id":"6WW0","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.01 A"},{"key":"Chains","value":"A/B/C/D=24-508"}]},{"database":"PDB","id":"8FDA","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.20 A"},{"key":"Chains","value":"A/B/C/D=24-508"}]},{"database":"PDBsum","id":"3RUK","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"3SWZ","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"4NKV","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"4NKW","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"4NKX","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"4NKY","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"4NKZ","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"5IRQ","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"5IRV","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"5UYS","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"6CHI","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"6CIR","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"6CIZ","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"6WR0","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"6WR1","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"6WW0","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"8FDA","properties":[{"key":"Description","value":"-"}]},{"database":"AlphaFoldDB","id":"P05093","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P05093","properties":[{"key":"Description","value":"-"}]},{"database":"BioGRID","id":"107958","properties":[{"key":"Interactions","value":"17"}]},{"database":"FunCoup","id":"P05093","properties":[{"key":"Number of interactors","value":"436"}]},{"database":"IntAct","id":"P05093","properties":[{"key":"Interactions","value":"15"}]},{"database":"MINT","id":"P05093","properties":[{"key":"Description","value":"-"}]},{"database":"NDEx","id":"IQUERY-CP-CYP17A1","properties":[{"key":"Evidences","value":"10 NDEx IQuery Curated Pathways"}]},{"database":"STRING","id":"9606.ENSP00000358903","properties":[{"key":"Description","value":"-"}]},{"database":"BindingDB","id":"P05093","properties":[{"key":"Description","value":"-"}]},{"database":"ChEMBL","id":"CHEMBL3522","properties":[{"key":"Description","value":"-"}]},{"database":"DrugBank","id":"DB05812","properties":[{"key":"GenericName","value":"Abiraterone"}]},{"database":"DrugBank","id":"DB04630","properties":[{"key":"GenericName","value":"Aldosterone"}]},{"database":"DrugBank","id":"DB01424","properties":[{"key":"GenericName","value":"Aminophenazone"}]},{"database":"DrugBank","id":"DB09061","properties":[{"key":"GenericName","value":"Cannabidiol"}]},{"database":"DrugBank","id":"DB19193","properties":[{"key":"GenericName","value":"CFG-920"}]},{"database":"DrugBank","id":"DB00882","properties":[{"key":"GenericName","value":"Clomifene"}]},{"database":"DrugBank","id":"DB01234","properties":[{"key":"GenericName","value":"Dexamethasone"}]},{"database":"DrugBank","id":"DB14649","properties":[{"key":"GenericName","value":"Dexamethasone acetate"}]},{"database":"DrugBank","id":"DB08943","properties":[{"key":"GenericName","value":"Isoconazole"}]},{"database":"DrugBank","id":"DB01026","properties":[{"key":"GenericName","value":"Ketoconazole"}]},{"database":"DrugBank","id":"DB05667","properties":[{"key":"GenericName","value":"Levoketoconazole"}]},{"database":"DrugBank","id":"DB14009","properties":[{"key":"GenericName","value":"Medical Cannabis"}]},{"database":"DrugBank","id":"DB14011","properties":[{"key":"GenericName","value":"Nabiximols"}]},{"database":"DrugBank","id":"DB00157","properties":[{"key":"GenericName","value":"NADH"}]},{"database":"DrugBank","id":"DB12066","properties":[{"key":"GenericName","value":"Orteronel"}]},{"database":"DrugBank","id":"DB01708","properties":[{"key":"GenericName","value":"Prasterone"}]},{"database":"DrugBank","id":"DB00396","properties":[{"key":"GenericName","value":"Progesterone"}]},{"database":"DrugBank","id":"DB12275","properties":[{"key":"GenericName","value":"Seviteronel"}]},{"database":"DrugBank","id":"DB02901","properties":[{"key":"GenericName","value":"Stanolone"}]},{"database":"DrugCentral","id":"P05093","properties":[{"key":"Description","value":"-"}]},{"database":"GuidetoPHARMACOLOGY","id":"1361","properties":[{"key":"Description","value":"-"}]},{"database":"SwissLipids","id":"SLP:000001611","properties":[{"key":"Description","value":"-"}]},{"database":"GlyGen","id":"P05093","properties":[{"key":"glycosylation","value":"1 site, 1 O-linked glycan (1 site)"}]},{"database":"iPTMnet","id":"P05093","properties":[{"key":"Description","value":"-"}]},{"database":"PhosphoSitePlus","id":"P05093","properties":[{"key":"Description","value":"-"}]},{"database":"BioMuta","id":"CYP17A1","properties":[{"key":"Description","value":"-"}]},{"database":"DMDM","id":"117283","properties":[{"key":"Description","value":"-"}]},{"database":"MassIVE","id":"P05093","properties":[{"key":"Description","value":"-"}]},{"database":"PaxDb","id":"9606-ENSP00000358903","properties":[{"key":"Description","value":"-"}]},{"database":"PeptideAtlas","id":"P05093","properties":[{"key":"Description","value":"-"}]},{"database":"ProteomicsDB","id":"51789","properties":[{"key":"Description","value":"-"}]},{"database":"Antibodypedia","id":"31491","properties":[{"key":"antibodies","value":"659 antibodies from 42 providers"}]},{"database":"DNASU","id":"1586","properties":[{"key":"Description","value":"-"}]},{"database":"Ensembl","id":"ENST00000369887.4","properties":[{"key":"ProteinId","value":"ENSP00000358903.3"},{"key":"GeneId","value":"ENSG00000148795.8"}]},{"database":"GeneID","id":"1586","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"hsa:1586","properties":[{"key":"Description","value":"-"}]},{"database":"MANE-Select","id":"ENST00000369887.4","properties":[{"key":"ProteinId","value":"ENSP00000358903.3"},{"key":"RefSeqNucleotideId","value":"NM_000102.4"},{"key":"RefSeqProteinId","value":"NP_000093.1"}]},{"database":"AGR","id":"HGNC:2593","properties":[{"key":"Description","value":"-"}]},{"database":"ClinPGx","id":"PA27090","properties":[{"key":"Description","value":"-"}]},{"database":"CTD","id":"1586","properties":[{"key":"Description","value":"-"}]},{"database":"DisGeNET","id":"1586","properties":[{"key":"Description","value":"-"}]},{"database":"GeneCards","id":"CYP17A1","properties":[{"key":"Description","value":"-"}]},{"database":"HGNC","id":"HGNC:2593","properties":[{"key":"GeneName","value":"CYP17A1"}]},{"database":"HPA","id":"ENSG00000148795","properties":[{"key":"ExpressionPatterns","value":"Tissue enriched (adrenal)"}]},{"database":"MalaCards","id":"CYP17A1","properties":[{"key":"Description","value":"-"}]},{"database":"MIM","id":"202110","properties":[{"key":"Type","value":"phenotype"}]},{"database":"MIM","id":"609300","properties":[{"key":"Type","value":"gene"}]},{"database":"OpenTargets","id":"ENSG00000148795","properties":[{"key":"Description","value":"-"}]},{"database":"Orphanet","id":"90796","properties":[{"key":"Disease","value":"46,XY difference of sex development due to isolated 17,20-lyase deficiency"}]},{"database":"Orphanet","id":"90793","properties":[{"key":"Disease","value":"Congenital adrenal hyperplasia due to 17-alpha-hydroxylase deficiency"}]},{"database":"VEuPathDB","id":"HostDB:ENSG00000148795","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"KOG0156","properties":[{"key":"ToxonomicScope","value":"Eukaryota"}]},{"database":"GeneTree","id":"ENSGT00940000155588","properties":[{"key":"Description","value":"-"}]},{"database":"HOGENOM","id":"CLU_001570_22_0_1","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"P05093","properties":[{"key":"Description","value":"-"}]},{"database":"OMA","id":"GPQEAME","properties":[{"key":"Fingerprint","value":"-"}]},{"database":"OrthoDB","id":"1470350at2759","properties":[{"key":"Description","value":"-"}]},{"database":"PAN-GO","id":"P05093","properties":[{"key":"Number of GO annotations","value":"3 GO annotations based on evolutionary models"}]},{"database":"PhylomeDB","id":"P05093","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"MetaCyc:HS07560-MONOMER","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"1.14.14.19","properties":[{"key":"OrganismId","value":"2681"}]},{"database":"BRENDA","id":"1.14.14.32","properties":[{"key":"OrganismId","value":"2681"}]},{"database":"PathwayCommons","id":"P05093","properties":[{"key":"Description","value":"-"}]},{"database":"Reactome","id":"R-HSA-193048","properties":[{"key":"PathwayName","value":"Androgen biosynthesis"}]},{"database":"Reactome","id":"R-HSA-194002","properties":[{"key":"PathwayName","value":"Glucocorticoid biosynthesis"}]},{"database":"Reactome","id":"R-HSA-5579028","properties":[{"key":"PathwayName","value":"Defective CYP17A1 causes AH5"}]},{"database":"SABIO-RK","id":"P05093","properties":[{"key":"Description","value":"-"}]},{"database":"SignaLink","id":"P05093","properties":[{"key":"Description","value":"-"}]},{"database":"SIGNOR","id":"P05093","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00788","properties":[{"key":"RectionId","value":"-"}]},{"database":"Agora","id":"ENSG00000148795","properties":[{"key":"NominatedTarget","value":"-"}]},{"database":"BioGRID-ORCS","id":"1586","properties":[{"key":"hits","value":"16 hits in 1163 CRISPR screens"}]},{"database":"ChiTaRS","id":"CYP17A1","properties":[{"key":"OrganismName","value":"human"}]},{"database":"EvolutionaryTrace","id":"P05093","properties":[{"key":"Description","value":"-"}]},{"database":"GeneWiki","id":"CYP17A1","properties":[{"key":"Description","value":"-"}]},{"database":"GenomeRNAi","id":"1586","properties":[{"key":"Description","value":"-"}]},{"database":"Pharos","id":"P05093","properties":[{"key":"DevelopmentLevel","value":"Tclin"}]},{"database":"PRO","id":"PR:P05093","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000005640","properties":[{"key":"Component","value":"Chromosome 10"}]},{"database":"RNAct","id":"P05093","properties":[{"key":"moleculeType","value":"protein"}]},{"database":"Bgee","id":"ENSG00000148795","properties":[{"key":"ExpressionPatterns","value":"Expressed in right adrenal gland and 97 other cell types or tissues"}]},{"database":"ExpressionAtlas","id":"P05093","properties":[{"key":"ExpressionPatterns","value":"baseline and differential"}]},{"database":"GO","id":"GO:0030424","properties":[{"key":"GoTerm","value":"C:axon"},{"key":"GoEvidenceType","value":"IEA:Ensembl"}]},{"database":"GO","id":"GO:0005783","properties":[{"key":"GoTerm","value":"C:endoplasmic reticulum"},{"key":"GoEvidenceType","value":"NAS:ProtInc"}],"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9326943"}]},{"database":"GO","id":"GO:0005789","properties":[{"key":"GoTerm","value":"C:endoplasmic reticulum membrane"},{"key":"GoEvidenceType","value":"TAS:Reactome"}]},{"database":"GO","id":"GO:0043025","properties":[{"key":"GoTerm","value":"C:neuronal cell body"},{"key":"GoEvidenceType","value":"IEA:Ensembl"}]},{"database":"GO","id":"GO:0020037","properties":[{"key":"GoTerm","value":"F:heme binding"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"22266943"}]},{"database":"GO","id":"GO:0005506","properties":[{"key":"GoTerm","value":"F:iron ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0019825","properties":[{"key":"GoTerm","value":"F:oxygen binding"},{"key":"GoEvidenceType","value":"TAS:ProtInc"}],"evidences":[{"evidenceCode":"ECO:0000304","source":"PubMed","id":"2808364"}]},{"database":"GO","id":"GO:0004508","properties":[{"key":"GoTerm","value":"F:steroid 17-alpha-monooxygenase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"22266943"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"36640554"}]},{"database":"GO","id":"GO:0006702","properties":[{"key":"GoTerm","value":"P:androgen biosynthetic process"},{"key":"GoEvidenceType","value":"TAS:Reactome"}]},{"database":"GO","id":"GO:0034651","properties":[{"key":"GoTerm","value":"P:cortisol biosynthetic process"},{"key":"GoEvidenceType","value":"IDA:UniProt"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"9452426"}]},{"database":"GO","id":"GO:0006704","properties":[{"key":"GoTerm","value":"P:glucocorticoid biosynthetic process"},{"key":"GoEvidenceType","value":"TAS:Reactome"}]},{"database":"GO","id":"GO:0042446","properties":[{"key":"GoTerm","value":"P:hormone biosynthetic process"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"22266943"}]},{"database":"GO","id":"GO:0042448","properties":[{"key":"GoTerm","value":"P:progesterone metabolic process"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"22266943"}]},{"database":"GO","id":"GO:0007548","properties":[{"key":"GoTerm","value":"P:sex differentiation"},{"key":"GoEvidenceType","value":"TAS:ProtInc"}],"evidences":[{"evidenceCode":"ECO:0000304","source":"PubMed","id":"9326943"}]},{"database":"GO","id":"GO:0006694","properties":[{"key":"GoTerm","value":"P:steroid biosynthetic process"},{"key":"GoEvidenceType","value":"TAS:ProtInc"}],"evidences":[{"evidenceCode":"ECO:0000304","source":"PubMed","id":"3500022"}]},{"database":"GO","id":"GO:0008202","properties":[{"key":"GoTerm","value":"P:steroid metabolic process"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"22266943"}]},{"database":"CDD","id":"cd20673","properties":[{"key":"EntryName","value":"CYP17A1"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.630.10:FF:000002","properties":[{"key":"EntryName","value":"Cytochrome P450 1A1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.630.10","properties":[{"key":"EntryName","value":"Cytochrome P450"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001128","properties":[{"key":"EntryName","value":"Cyt_P450"}]},{"database":"InterPro","id":"IPR017972","properties":[{"key":"EntryName","value":"Cyt_P450_CS"}]},{"database":"InterPro","id":"IPR002401","properties":[{"key":"EntryName","value":"Cyt_P450_E_grp-I"}]},{"database":"InterPro","id":"IPR036396","properties":[{"key":"EntryName","value":"Cyt_P450_sf"}]},{"database":"PANTHER","id":"PTHR24289","properties":[{"key":"EntryName","value":"STEROID 17-ALPHA-HYDROXYLASE/17,20 LYASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR24289:SF13","properties":[{"key":"EntryName","value":"STEROID 17-ALPHA-HYDROXYLASE_17,20 LYASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00067","properties":[{"key":"EntryName","value":"p450"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00463","properties":[{"key":"EntryName","value":"EP450I"}]},{"database":"PRINTS","id":"PR00385","properties":[{"key":"EntryName","value":"P450"}]},{"database":"SUPFAM","id":"SSF48264","properties":[{"key":"EntryName","value":"Cytochrome P450"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00086","properties":[{"key":"EntryName","value":"CYTOCHROME_P450"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MWELVALLLLTLAYLFWPKRRCPGAKYPKSLLSLPLVGSLPFLPRHGHMHNNFFKLQKKYGPIYSVRMGTKTTVIVGHHQLAKEVLIKKGKDFSGRPQMATLDIASNNRKGIAFADSGAHWQLHRRLAMATFALFKDGDQKLEKIICQEISTLCDMLATHNGQSIDISFPVFVAVTNVISLICFNTSYKNGDPELNVIQNYNEGIIDNLSKDSLVDLVPWLKIFPNKTLEKLKSHVKIRNDLLNKILENYKEKFRSDSITNMLDTLMQAKMNSDNGNAGPDQDSELLSDNHILTTIGDIFGAGVETTTSVVKWTLAFLLHNPQVKKKLYEEIDQNVGFSRTPTISDRNRLLLLEATIREVLRLRPVAPMLIPHKANVDSSIGEFAVDKGTEVIINLWALHHNEKEWHQPDQFMPERFLNPAGTQLISPSVSYLPFGAGPRSCIGEILARQELFLIMAWLLQRFDLEVPDDGQLPSLEGIPKVVFLIDSFKVKIKVRQAWREAQAEGST","length":508,"molWeight":57371,"crc64":"E5454E9E18F96B0E","md5":"231B3EB8D4F80784D7F2CA693EF88A91"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":10,"COFACTOR":1,"ACTIVITY REGULATION":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"PATHWAY":2,"SUBCELLULAR LOCATION":1,"PTM":1,"DISEASE":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Binding site":2,"Natural variant":31,"Mutagenesis":1,"Helix":26,"Beta strand":18,"Turn":4},"uniParcId":"UPI0000128309"}}