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

 CP17A_PIG               Reviewed;         509 AA.
P19100; Q29553; Q99030;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 3.
25-OCT-2017, entry version 138.
RecName: Full=Steroid 17-alpha-hydroxylase/17,20 lyase;
EC=1.14.14.19 {ECO:0000250|UniProtKB:P05093};
EC=1.14.14.32 {ECO:0000250|UniProtKB:P05093};
AltName: Full=17-alpha-hydroxyprogesterone aldolase;
AltName: Full=CYPXVII;
AltName: Full=Cytochrome P450 17A1;
AltName: Full=Cytochrome P450-C17;
Short=Cytochrome P450c17;
Name=CYP17A1; Synonyms=CYP17;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Adrenal gland, and Testis;
PubMed=3025870; DOI=10.1073/pnas.84.2.407;
Chung B.-C., Picado-Leonard J., Haniu M., Bienkowski M., Hall P.F.,
Shively J.E., Miller W.L.;
"Cytochrome P450c17 (steroid 17 alpha-hydroxylase/17,20 lyase):
cloning of human adrenal and testis cDNAs indicates the same gene is
expressed in both tissues.";
Proc. Natl. Acad. Sci. U.S.A. 84:407-411(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
PubMed=1543750; DOI=10.1016/0167-4781(92)90464-B;
Conley A.J., Graham-Lorence S.E., Kagimoto M., Lorence M.C.,
Murry B.A., Oka K., Sanders D., Mason J.I.;
"Nucleotide sequence of a cDNA encoding porcine testis 17 alpha-
hydroxylase cytochrome P-450.";
Biochim. Biophys. Acta 1130:75-77(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Kidney;
PubMed=1627653; DOI=10.1016/0167-4781(92)90039-3;
Zhang P., Nason T.F., Han X.G., Hall P.F.;
"Gene for 17 alpha-hydroxylase/C (17-20) lyase P-450: complete
nucleotide sequence of the porcine gene and 5' upstream sequence of
the rat gene.";
Biochim. Biophys. Acta 1131:345-348(1992).
[4]
NUCLEOTIDE SEQUENCE.
Conley A.J., Chu X., Corbin C.J.;
Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Conversion of pregnenolone and progesterone to their 17-
alpha-hydroxylated products and subsequently to
dehydroepiandrosterone (DHEA) and androstenedione. Catalyzes both
the 17-alpha-hydroxylation and the 17,20-lyase reaction. Involved
in sexual development during fetal life and at puberty.
-!- CATALYTIC ACTIVITY: A C(21)-steroid + [reduced NADPH--hemoprotein
reductase] + O(2) = a 17-alpha-hydroxy-C(21)-steroid + [oxidized
NADPH--hemoprotein reductase] + H(2)O.
{ECO:0000250|UniProtKB:P05093}.
-!- CATALYTIC ACTIVITY: 17-alpha-hydroxyprogesterone + [reduced
NADPH--hemoprotein reductase] + O(2) = androstenedione + acetate +
[oxidized NADPH--hemoprotein reductase] + H(2)O.
{ECO:0000250|UniProtKB:P05093}.
-!- CATALYTIC ACTIVITY: 17-alpha-hydroxypregnenolone + [reduced
NADPH--hemoprotein reductase] + O(2) = 3-beta-hydroxyandrost-5-en-
17-one + acetate + [oxidized NADPH--hemoprotein reductase] +
H(2)O. {ECO:0000250|UniProtKB:P05093}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Regulated predominantly by intracellular cAMP
levels.
-!- PATHWAY: Lipid metabolism; steroid biosynthesis.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M63507; AAA31008.1; -; mRNA.
EMBL; U41525; AAA84419.1; -; Genomic_DNA.
EMBL; U41519; AAA84419.1; JOINED; Genomic_DNA.
EMBL; U41520; AAA84419.1; JOINED; Genomic_DNA.
EMBL; U41521; AAA84419.1; JOINED; Genomic_DNA.
EMBL; U41522; AAA84419.1; JOINED; Genomic_DNA.
EMBL; U41523; AAA84419.1; JOINED; Genomic_DNA.
EMBL; U41524; AAA84419.1; JOINED; Genomic_DNA.
EMBL; Z11854; CAA77878.1; -; Genomic_DNA.
EMBL; Z11855; CAA77878.1; JOINED; Genomic_DNA.
EMBL; Z11856; CAA77878.1; JOINED; Genomic_DNA.
PIR; S22339; S22339.
RefSeq; NP_999593.1; NM_214428.1.
UniGene; Ssc.51528; -.
ProteinModelPortal; P19100; -.
SMR; P19100; -.
STRING; 9823.ENSSSCP00000011283; -.
PaxDb; P19100; -.
PeptideAtlas; P19100; -.
PRIDE; P19100; -.
Ensembl; ENSSSCT00000011585; ENSSSCP00000011283; ENSSSCG00000010591.
GeneID; 403330; -.
KEGG; ssc:403330; -.
CTD; 1586; -.
eggNOG; KOG0156; Eukaryota.
eggNOG; COG2124; LUCA.
GeneTree; ENSGT00900000140831; -.
HOGENOM; HOG000036991; -.
HOVERGEN; HBG106944; -.
InParanoid; P19100; -.
KO; K00512; -.
OMA; YGPIYSF; -.
OrthoDB; EOG091G0BT8; -.
TreeFam; TF105095; -.
BRENDA; 1.14.99.9; 6170.
Reactome; R-SSC-193048; Androgen biosynthesis.
Reactome; R-SSC-194002; Glucocorticoid biosynthesis.
Reactome; R-SSC-211976; Endogenous sterols.
UniPathway; UPA00062; -.
Proteomes; UP000008227; Chromosome 14.
Bgee; ENSSSCG00000010591; -.
Genevisible; P19100; SS.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0047442; F:17-alpha-hydroxyprogesterone aldolase activity; ISS:UniProtKB.
GO; GO:0020037; F:heme binding; ISS:UniProtKB.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0004508; F:steroid 17-alpha-monooxygenase activity; ISS:UniProtKB.
GO; GO:0006704; P:glucocorticoid biosynthetic process; IEA:Ensembl.
GO; GO:0042446; P:hormone biosynthetic process; ISS:UniProtKB.
GO; GO:0042448; P:progesterone metabolic process; ISS:UniProtKB.
GO; GO:0008202; P:steroid metabolic process; ISS:UniProtKB.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002401; Cyt_P450_E_grp-I.
InterPro; IPR036396; Cyt_P450_sf.
Pfam; PF00067; p450; 1.
PRINTS; PR00463; EP450I.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
2: Evidence at transcript level;
Complete proteome; Heme; Iron; Lyase; Membrane; Metal-binding;
Monooxygenase; Oxidoreductase; Reference proteome; Steroidogenesis.
CHAIN 1 509 Steroid 17-alpha-hydroxylase/17,20 lyase.
/FTId=PRO_0000051940.
METAL 442 442 Iron (heme axial ligand). {ECO:0000250}.
CONFLICT 46 53 RGHQHMNF -> FL (in Ref. 1; no nucleotide
entry). {ECO:0000305}.
CONFLICT 51 51 M -> I (in Ref. 3; CAA77878).
{ECO:0000305}.
CONFLICT 70 70 S -> D (in Ref. 1; no nucleotide entry).
{ECO:0000305}.
CONFLICT 98 98 R -> K (in Ref. 1; no nucleotide entry).
{ECO:0000305}.
CONFLICT 108 116 Missing (in Ref. 3; CAA77878).
{ECO:0000305}.
CONFLICT 117 117 H -> E (in Ref. 1; no nucleotide entry).
{ECO:0000305}.
CONFLICT 126 140 KLALSTFSLFKGGNL -> SLF (in Ref. 1; no
nucleotide entry). {ECO:0000305}.
CONFLICT 161 191 NGESIDLAQPLSLAMTNIVSFICFNFSFKKG -> VIQNAC
EMDRLKEI (in Ref. 1; no nucleotide
entry). {ECO:0000305}.
CONFLICT 196 196 Q -> D (in Ref. 1; no nucleotide entry).
{ECO:0000305}.
CONFLICT 201 210 FNDGILDAVG -> IEEGELT (in Ref. 1; no
nucleotide entry). {ECO:0000305}.
CONFLICT 238 238 M -> E (in Ref. 1; no nucleotide entry).
{ECO:0000305}.
CONFLICT 257 266 NSITNLLDIM -> IL (in Ref. 1; no
nucleotide entry). {ECO:0000305}.
CONFLICT 270 284 Missing (in Ref. 1; no nucleotide entry).
{ECO:0000305}.
CONFLICT 291 303 HMLATVADIFGAG -> AC (in Ref. 1; no
nucleotide entry). {ECO:0000305}.
CONFLICT 292 292 M -> S (in Ref. 3; CAA77878).
{ECO:0000305}.
CONFLICT 308 308 A -> V (in Ref. 1; no nucleotide entry).
{ECO:0000305}.
CONFLICT 311 333 VKWIVAFLLHYPLLRKKIQDAID -> FIWIQEAIE (in
Ref. 1; no nucleotide entry).
{ECO:0000305}.
CONFLICT 319 321 LHY -> ATLC (in Ref. 3; CAA77878).
{ECO:0000305}.
CONFLICT 330 330 D -> E (in Ref. 3; CAA77878).
{ECO:0000305}.
CONFLICT 333 333 D -> E (in Ref. 3; CAA77878).
{ECO:0000305}.
CONFLICT 389 389 D -> A (in Ref. 1; no nucleotide entry).
{ECO:0000305}.
CONFLICT 395 397 NLW -> SLF (in Ref. 1; no nucleotide
entry). {ECO:0000305}.
CONFLICT 407 407 H -> L (in Ref. 2; AAA31008).
{ECO:0000305}.
SEQUENCE 509 AA; 57447 MW; 9497D185A1B446B4 CRC64;
MWVLLVFFLL TLTYLFWPKT KGSGAKYPRS LPVLPVVGSL PFLPRRGHQH MNFFKLQDKY
GPIFSFRLGS KTTVVIGDHQ LAKEVLLKKG KEFSGRPRVM TLDILSDNQK GIAFADHGTS
WQLHRKLALS TFSLFKGGNL KLENIINQEI KVLCDFLATR NGESIDLAQP LSLAMTNIVS
FICFNFSFKK GDPALQAIVN FNDGILDAVG KEILYDMFPG IRILPSQTLE NMKQCVRMRN
ELLREILENR KENYSRNSIT NLLDIMIQAK TNAESNTGGP DHNLKLLSDR HMLATVADIF
GAGVETSASV VKWIVAFLLH YPLLRKKIQD AIDQNIGFNR APSISDRNQL VLLEATIREV
LRFRPVSPTL IPHRAIIDSS IGEFTIDKDT DVVVNLWALH HNEKEWHRPD LFMPERFLDP
TGTQLISPSL SYLPFGAGPR SCVGEMLARQ ELFLFTAGLL QRFDLELPDD GQLPCLVGNP
SLVLQIDPFK VKIKERQAWK EAHTEGSTS


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