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CP17A_BOVIN
ID   CP17A_BOVIN             Reviewed;         509 AA.
AC   P05185; Q2YDL3;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Steroid 17-alpha-hydroxylase/17,20 lyase;
DE            EC=1.14.14.19 {ECO:0000250|UniProtKB:P05093};
DE   AltName: Full=17-alpha-hydroxyprogesterone aldolase;
DE            EC=1.14.14.32 {ECO:0000250|UniProtKB:P05093};
DE   AltName: Full=CYPXVII;
DE   AltName: Full=Cytochrome P450 17A1;
DE   AltName: Full=Cytochrome P450-C17;
DE            Short=Cytochrome P450c17;
DE   AltName: Full=Steroid 17-alpha-monooxygenase;
GN   Name=CYP17A1; Synonyms=CYP17;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3003117; DOI=10.1016/s0021-9258(17)35959-8;
RA   Zuber M.X., John M.E., Okamura T., Simpson E.R., Waterman M.R.;
RT   "Bovine adrenocortical cytochrome P-450(17 alpha). Regulation of gene
RT   expression by ACTH and elucidation of primary sequence.";
RL   J. Biol. Chem. 261:2475-2482(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2543297; DOI=10.1016/0003-9861(89)90298-1;
RA   Bhasker C.R., Adler B.S., Dee A., John M.E., Kagimoto M., Zuber M.X.,
RA   Ahlgren R., Wang X.D., Simpson E.R., Waterman M.R.;
RT   "Structural characterization of the bovine CYP17 (17 alpha-hydroxylase)
RT   gene.";
RL   Arch. Biochem. Biophys. 271:479-487(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: A cytochrome P450 monooxygenase involved in corticoid and
CC       androgen biosynthesis. Catalyzes 17-alpha hydroxylation of C21
CC       steroids, which is common for both pathways. A second oxidative step,
CC       required only for androgen synthesis, involves an acyl-carbon cleavage.
CC       The 17-alpha hydroxy intermediates, as part of adrenal glucocorticoids
CC       biosynthesis pathway, are precursors of cortisol. Hydroxylates steroid
CC       hormones, pregnenolone and progesterone to form 17-alpha hydroxy
CC       metabolites, followed by the cleavage of the C17-C20 bond to form C19
CC       steroids, dehydroepiandrosterone (DHEA) and androstenedione. Has 16-
CC       alpha hydroxylase activity. Catalyzes 16-alpha hydroxylation of 17-
CC       alpha hydroxy pregnenolone, followed by the cleavage of the C17-C20
CC       bond to form 16-alpha-hydroxy DHEA. Also 16-alpha hydroxylates
CC       androgens, relevant for estriol synthesis. Mechanistically, uses
CC       molecular oxygen inserting one oxygen atom into a substrate, and
CC       reducing the second into a water molecule, with two electrons provided
CC       by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein
CC       reductase). {ECO:0000250|UniProtKB:P05093}.
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       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65761;
CC         Evidence={ECO:0000250|UniProtKB:P05093};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + progesterone + reduced [NADPH--hemoprotein reductase] =
CC         17alpha-hydroxyprogesterone + H(+) + H2O + oxidized [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:46308, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:17026, ChEBI:CHEBI:17252,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.19;
CC         Evidence={ECO:0000250|UniProtKB:P05093};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46309;
CC         Evidence={ECO:0000250|UniProtKB:P05093};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + pregnenolone + reduced [NADPH--hemoprotein reductase] =
CC         17alpha-hydroxypregnenolone + H(+) + H2O + oxidized [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:50236, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16581, ChEBI:CHEBI:28750,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.19;
CC         Evidence={ECO:0000250|UniProtKB:P05093};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50237;
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       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14754;
CC         Evidence={ECO:0000250|UniProtKB:P05093};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17alpha-hydroxyprogesterone + O2 + reduced [NADPH--hemoprotein
CC         reductase] = 16alpha,17alpha-dihydroxyprogesterone + H(+) + H2O +
CC         oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53216,
CC         Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:763,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:17252, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000250|UniProtKB:P05093};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53217;
CC         Evidence={ECO:0000250|UniProtKB:P05093};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=16alpha,17alpha-dihydroxyprogesterone + O2 + reduced [NADPH--
CC         hemoprotein reductase] = 6beta,16alpha,17alpha-trihydroxyprogesterone
CC         + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC         Xref=Rhea:RHEA:53220, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC         ChEBI:CHEBI:763, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:137046; Evidence={ECO:0000250|UniProtKB:P05093};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53221;
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       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50245;
CC         Evidence={ECO:0000250|UniProtKB:P05093};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=16alpha,17alpha-dihydroxypregnenolone + O2 + reduced [NADPH--
CC         hemoprotein reductase] = 3beta,16alpha-dihydroxy-androst-5-en-17-one
CC         + acetate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC         Xref=Rhea:RHEA:53224, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:27771, ChEBI:CHEBI:30089, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:137049;
CC         Evidence={ECO:0000250|UniProtKB:P05093};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53225;
CC         Evidence={ECO:0000250|UniProtKB:P05093};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3beta-hydroxyandrost-5-en-17-one + O2 + reduced [NADPH--
CC         hemoprotein reductase] = 3beta,16alpha-dihydroxy-androst-5-en-17-one
CC         + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC         Xref=Rhea:RHEA:47220, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:27771, ChEBI:CHEBI:28689, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P05093};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47221;
CC         Evidence={ECO:0000250|UniProtKB:P05093};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=androst-4-ene-3,17-dione + O2 + reduced [NADPH--hemoprotein
CC         reductase] = 16alpha-hydroxyandrost-4-ene-3,17-dione + H(+) + H2O +
CC         oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53228,
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:27582, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000250|UniProtKB:P05093};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53229;
CC         Evidence={ECO:0000250|UniProtKB:P05093};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P05093};
CC   -!- ACTIVITY REGULATION: Regulated predominantly by intracellular cAMP
CC       levels. The 17,20-lyase activity is stimulated by cytochrome b5, which
CC       acts as an allosteric effector increasing the Vmax of the lyase
CC       activity. {ECO:0000250|UniProtKB:P05093}.
CC   -!- PATHWAY: Steroid hormone biosynthesis. {ECO:0000250|UniProtKB:P05093}.
CC   -!- PATHWAY: Steroid biosynthesis; glucocorticoid biosynthesis.
CC       {ECO:0000250|UniProtKB:P05093}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P05093}. Microsome membrane
CC       {ECO:0000250|UniProtKB:P05093}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; M12547; AAA30485.1; -; mRNA.
DR   EMBL; BC110169; AAI10170.1; -; mRNA.
DR   PIR; S04346; S04346.
DR   RefSeq; NP_776729.1; NM_174304.2.
DR   AlphaFoldDB; P05185; -.
DR   SMR; P05185; -.
DR   STRING; 9913.ENSBTAP00000019061; -.
DR   BindingDB; P05185; -.
DR   PaxDb; P05185; -.
DR   PRIDE; P05185; -.
DR   Ensembl; ENSBTAT00000019061; ENSBTAP00000019061; ENSBTAG00000014335.
DR   Ensembl; ENSBTAT00000087082; ENSBTAP00000069265; ENSBTAG00000054516.
DR   GeneID; 281739; -.
DR   KEGG; bta:281739; -.
DR   CTD; 1586; -.
DR   VEuPathDB; HostDB:ENSBTAG00000014335; -.
DR   VEuPathDB; HostDB:ENSBTAG00000054516; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   GeneTree; ENSGT00940000155588; -.
DR   InParanoid; P05185; -.
DR   OMA; HEFIDDR; -.
DR   OrthoDB; 702827at2759; -.
DR   UniPathway; UPA00788; -.
DR   Proteomes; UP000009136; Chromosome 26.
DR   Bgee; ENSBTAG00000014335; Expressed in dorsal thalamus and 43 other tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0047442; F:17-alpha-hydroxyprogesterone aldolase activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004508; F:steroid 17-alpha-monooxygenase activity; ISS:UniProtKB.
DR   GO; GO:0006704; P:glucocorticoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0042446; P:hormone biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0042448; P:progesterone metabolic process; ISS:UniProtKB.
DR   GO; GO:0008202; P:steroid metabolic process; ISS:UniProtKB.
DR   Gene3D; 1.10.630.10; -; 1.
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   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   Endoplasmic reticulum; Heme; Iron; Lipid metabolism; Lyase; Membrane;
KW   Metal-binding; Microsome; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Steroidogenesis.
FT   CHAIN           1..509
FT                   /note="Steroid 17-alpha-hydroxylase/17,20 lyase"
FT                   /id="PRO_0000051926"
FT   BINDING         202
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P05093"
FT   BINDING         442
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"
FT   CONFLICT        240
FT                   /note="N -> K (in Ref. 3; AAI10170)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        423
FT                   /note="T -> A (in Ref. 2; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        458
FT                   /note="R -> W (in Ref. 2; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        509
FT                   /note="P -> S (in Ref. 2; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   509 AA;  57244 MW;  64B0E5537A474BB7 CRC64;
     MWLLLAVFLL TLAYLFWPKT KHSGAKYPRS LPSLPLVGSL PFLPRRGQQH KNFFKLQEKY
     GPIYSFRLGS KTTVMIGHHQ LAREVLLKKG KEFSGRPKVA TLDILSDNQK GIAFADHGAH
     WQLHRKLALN AFALFKDGNL KLEKIINQEA NVLCDFLATQ HGEAIDLSEP LSLAVTNIIS
     FICFNFSFKN EDPALKAIQN VNDGILEVLS KEVLLDIFPV LKIFPSKAME KMKGCVQTRN
     ELLNEILEKC QENFSSDSIT NLLHILIQAK VNADNNNAGP DQDSKLLSNR HMLATIGDIF
     GAGVETTTSV IKWIVAYLLH HPSLKKRIQD DIDQIIGFNR TPTISDRNRL VLLEATIREV
     LRIRPVAPTL IPHKAVIDSS IGDLTIDKGT DVVVNLWALH HSEKEWQHPD LFMPERFLDP
     TGTQLISPSL SYLPFGAGPR SCVGEMLARQ ELFLFMSRLL QRFNLEIPDD GKLPSLEGHA
     SLVLQIKPFK VKIEVRQAWK EAQAEGSTP
 
 
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