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Details on Person UniProt:P05093 CYP17A1

Class:Id	ReferenceGeneProduct:52716
_chainChangeLog	chain:1-508 added on Sat February 7 2015
_displayName	UniProt:P05093 CYP17A1
_timestamp	2025-02-21 18:45:30
chain	chain:1-508
checksum	E5454E9E18F96B0E
comment	FUNCTION 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).CATALYTIC ACTIVITY a C21-steroid + reduced [NADPH--hemoprotein reductase] + O2 = a 17alpha-hydroxy-C21-steroid + oxidized [NADPH--hemoprotein reductase] + H2O + H(+)CATALYTIC ACTIVITY progesterone + reduced [NADPH--hemoprotein reductase] + O2 = 17alpha-hydroxyprogesterone + oxidized [NADPH--hemoprotein reductase] + H2O + H(+)CATALYTIC ACTIVITY pregnenolone + reduced [NADPH--hemoprotein reductase] + O2 = 17alpha-hydroxypregnenolone + oxidized [NADPH--hemoprotein reductase] + H2O + H(+)CATALYTIC ACTIVITY 17alpha-hydroxyprogesterone + reduced [NADPH--hemoprotein reductase] + O2 = androst-4-ene-3,17-dione + acetate + oxidized [NADPH--hemoprotein reductase] + H2O + 2 H(+)CATALYTIC ACTIVITY 17alpha-hydroxyprogesterone + reduced [NADPH--hemoprotein reductase] + O2 = 16alpha,17alpha-dihydroxyprogesterone + oxidized [NADPH--hemoprotein reductase] + H2O + H(+)CATALYTIC ACTIVITY 16alpha,17alpha-dihydroxyprogesterone + reduced [NADPH--hemoprotein reductase] + O2 = 6beta,16alpha,17alpha-trihydroxyprogesterone + oxidized [NADPH--hemoprotein reductase] + H2O + H(+)CATALYTIC ACTIVITY 17alpha-hydroxypregnenolone + reduced [NADPH--hemoprotein reductase] + O2 = 3beta-hydroxyandrost-5-en-17-one + acetate + oxidized [NADPH--hemoprotein reductase] + H2O + 2 H(+)CATALYTIC ACTIVITY 16alpha,17alpha-dihydroxypregnenolone + reduced [NADPH--hemoprotein reductase] + O2 = 3beta,16alpha-dihydroxy-androst-5-en-17-one + acetate + oxidized [NADPH--hemoprotein reductase] + H2O + 2 H(+)CATALYTIC ACTIVITY 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(+)CATALYTIC ACTIVITY androst-4-ene-3,17-dione + reduced [NADPH--hemoprotein reductase] + O2 = 16alpha-hydroxyandrost-4-ene-3,17-dione + oxidized [NADPH--hemoprotein reductase] + H2O + H(+)COFACTOR 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).BIOPHYSICOCHEMICAL PROPERTIES 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.PATHWAY Steroid hormone biosynthesis.PATHWAY Steroid biosynthesis; glucocorticoid biosynthesis.SUBCELLULAR LOCATION Phosphorylation is necessary for 17,20-lyase, but not for 17-alpha-hydroxylase activity.DISEASE The disease is caused by variants affecting the gene represented in this entry.SIMILARITY Belongs to the cytochrome P450 family.
description	recommendedName: fullName evidence="27"Steroid 17-alpha-hydroxylase/17,20 lyase ecNumber evidence="10 13 15"1.14.14.19 alternativeName: 17-alpha-hydroxyprogesterone aldolase ecNumber evidence="10 13 15"1.14.14.32 alternativeName: CYPXVII alternativeName: fullName evidence="26"Cytochrome P450 17A1 alternativeName: Cytochrome P450-C17 shortName evidence="28"Cytochrome P450c17 alternativeName: Steroid 17-alpha-monooxygenase
geneName	CYP17A1 CYP17 S17AH
identifier	P05093
isSequenceChanged	FALSE
keyword	3D-structure Congenital adrenal hyperplasia Disease variant Endoplasmic reticulum Heme Iron Lipid metabolism Lyase Membrane Metal-binding Microsome Monooxygenase Oxidoreductase Phosphoprotein Proteomics identification Reference proteome Steroidogenesis
modified	[InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9862192] Weiser, Joel, 2024-02-26 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21
name	CYP17A1
referenceDatabase	[ReferenceDatabase:2] UniProt
referenceGene	[ReferenceDNASequence:8995920] ENSEMBL:ENSG00000148795 CYP17A1 [Homo sapiens]
secondaryIdentifier	CP17A_HUMAN Q5TZV7
sequenceLength	508
species	[Species:48887] Homo sapiens
(referenceEntity)	[EntityWithAccessionedSequence:193119] CYP17A1 [endoplasmic reticulum membrane] [Homo sapiens] [EntityWithAccessionedSequence:5601756] CYP17A1 R96Q [endoplasmic reticulum membrane] [Homo sapiens] [EntityWithAccessionedSequence:5601769] CYP17A1 S106P [endoplasmic reticulum membrane] [Homo sapiens] [EntityWithAccessionedSequence:5601786] CYP17A1 R347H [endoplasmic reticulum membrane] [Homo sapiens] [EntityWithAccessionedSequence:5601794] CYP17A1 R362C [endoplasmic reticulum membrane] [Homo sapiens] [EntityWithAccessionedSequence:5601803] CYP17A1 R96W [endoplasmic reticulum membrane] [Homo sapiens] [EntityWithAccessionedSequence:5601823] CYP17A1 R358Q [endoplasmic reticulum membrane] [Homo sapiens] [EntityWithAccessionedSequence:5601826] CYP17A1 W406R [endoplasmic reticulum membrane] [Homo sapiens] [EntityWithAccessionedSequence:5601860] CYP17A1 W17* [endoplasmic reticulum membrane] [Homo sapiens]
(referenceSequence)	[ReplacedResidue:5601757] L-arginine 96 replaced with L-glutamine [ReplacedResidue:5601778] L-arginine 358 replaced with L-glutamine [ReplacedResidue:5601782] L-arginine 362 replaced with L-cysteine [ReplacedResidue:5601789] L-serine 106 replaced with L-proline [ReplacedResidue:5601790] L-arginine 347 replaced with L-histidine [ReplacedResidue:5601797] L-tryptophan 406 replaced with L-arginine [ReplacedResidue:5601827] L-arginine 96 replaced with L-tryptophan [NonsenseMutation:5601863] Nonsense mutation at L-tryptophan 17
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No pathways have been reviewed or authored by UniProt:P05093 CYP17A1 (52716)