CP17A_SQUAC
ID CP17A_SQUAC Reviewed; 509 AA.
AC Q92113;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Steroid 17-alpha-hydroxylase/17,20 lyase;
DE EC=1.14.14.19 {ECO:0000250|UniProtKB:P05093};
DE EC=1.14.14.32 {ECO:0000250|UniProtKB:P05093};
DE AltName: Full=17-alpha-hydroxyprogesterone aldolase;
DE AltName: Full=CYPXVII;
DE AltName: Full=Cytochrome P450 17A1;
DE AltName: Full=Cytochrome P450-C17;
DE Short=Cytochrome P450c17;
GN Name=CYP17A1; Synonyms=CYP17;
OS Squalus acanthias (Spiny dogfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Squalomorphii; Squaliformes; Squalidae; Squalus.
OX NCBI_TaxID=7797;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7738515; DOI=10.1002/jez.1402720104;
RA Trant J.M.;
RT "Isolation and characterization of the cDNA encoding the spiny dogfish
RT shark (Squalus acanthias) form of cytochrome P450c17.";
RL J. Exp. Zool. 272:25-33(1995).
CC -!- FUNCTION: Conversion of pregnenolone and progesterone to their 17-
CC alpha-hydroxylated products and subsequently to dehydroepiandrosterone
CC (DHEA) and androstenedione. Catalyzes both the 17-alpha-hydroxylation
CC and the 17,20-lyase reaction.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a C21-steroid + O2 + reduced [NADPH--hemoprotein reductase] =
CC a 17alpha-hydroxy-C21-steroid + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:65760, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:61313, ChEBI:CHEBI:138141; EC=1.14.14.19;
CC Evidence={ECO:0000250|UniProtKB:P05093};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17alpha-hydroxyprogesterone + O2 + reduced [NADPH--hemoprotein
CC reductase] = acetate + androst-4-ene-3,17-dione + 2 H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:14753,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16422,
CC ChEBI:CHEBI:17252, ChEBI:CHEBI:30089, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; EC=1.14.14.32;
CC Evidence={ECO:0000250|UniProtKB:P05093};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17alpha-hydroxypregnenolone + O2 + reduced [NADPH--hemoprotein
CC reductase] = 3beta-hydroxyandrost-5-en-17-one + acetate + 2 H(+) +
CC H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50244,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:28689,
CC ChEBI:CHEBI:28750, ChEBI:CHEBI:30089, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; EC=1.14.14.32;
CC Evidence={ECO:0000250|UniProtKB:P05093};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- PATHWAY: Lipid metabolism; steroid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; S77384; AAB34256.1; -; mRNA.
DR PIR; I51281; I51281.
DR AlphaFoldDB; Q92113; -.
DR SMR; Q92113; -.
DR PRIDE; Q92113; -.
DR UniPathway; UPA00062; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047442; F:17-alpha-hydroxyprogesterone aldolase activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004508; F:steroid 17-alpha-monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0007548; P:sex differentiation; IEA:InterPro.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR033282; CYP17A1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24289:SF7; PTHR24289:SF7; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 2: Evidence at transcript level;
KW Heme; Iron; Lipid metabolism; Lyase; Membrane; Metal-binding;
KW Monooxygenase; Oxidoreductase; Steroidogenesis.
FT CHAIN 1..509
FT /note="Steroid 17-alpha-hydroxylase/17,20 lyase"
FT /id="PRO_0000051947"
FT BINDING 445
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
SQ SEQUENCE 509 AA; 57208 MW; 9D9F1CA18050EF60 CRC64;
MSLMLAALIL TVAFVICSLT GFTQRKLSGG RLPKCLPSFP LIGSLLSLRS DLPPHLLFQK
LQKTYGNLFS LMMGPHYAVV INNHQHAKEV LLKKGKIFAG RPSMVTTDLL SRGGKDIAFG
KYGPAWKFHR KLVLSALHLF GDGSAGIEKM ICQEATSMCS TFERLNNAAH DMMPDVTRAV
TNVICLLCFN STYEKEDPEF QTMRKYSQGI VNTVAKDSLI DIFPWLQFFP NENLHTLKQC
IATRDSILQK KFEDHKANYS SDSANDLFNI LLKAKMNAEN NNSSVHEAGL TDDHMVMTVA
DIFGAGVETS STAFAWMIIY LIHHPEVQKK IQEEIDSNIG FERTPKMSDK GNMNFLNATI
HEILRIQPVS PLLIPHVALA DSSIGDYTIP KGTRVIINLW AIHHDEKEWK NPDAFDPGRF
LDEDGKYVCS SSESYLPFGA GTRVCLGEML ARMELFLFTS WILQRFTVQV PPGYPPPDKE
GKFGIVLQPL KFKVQLKLRK AWENRGLHD
