ID A0JCJ2_COTJA Unreviewed; 242 AA.
AC A0JCJ2;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Cholesterol side-chain cleavage enzyme, mitochondrial {ECO:0000256|ARBA:ARBA00019844, ECO:0000256|RuleBase:RU364077};
DE EC=1.14.15.6 {ECO:0000256|ARBA:ARBA00012764, ECO:0000256|RuleBase:RU364077};
DE AltName: Full=Cholesterol desmolase {ECO:0000256|RuleBase:RU364077};
DE Flags: Fragment;
GN Name=P-450scc {ECO:0000313|EMBL:BAF36702.1};
OS Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Perdicinae; Coturnix.
OX NCBI_TaxID=93934 {ECO:0000313|EMBL:BAF36702.1};
RN [1] {ECO:0000313|EMBL:BAF36702.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Ovary {ECO:0000313|EMBL:BAF36702.1};
RX PubMed=20211759; DOI=10.1016/j.cbpc.2010.03.002;
RA Kamata R., Shiraishi F., Takahashi S., Shimizu A., Shiraishi H.;
RT "Reevaluation of the developmental toxicity of dieldrin by the use of
RT fertilized Japanese quail eggs.";
RL Comp. Biochem. Physiol. C Toxicol. Pharmacol. 152:84-90(2010).
CC -!- FUNCTION: A cytochrome P450 monooxygenase that catalyzes the side-chain
CC hydroxylation and cleavage of cholesterol to pregnenolone, the
CC precursor of most steroid hormones. Catalyzes three sequential
CC oxidation reactions of cholesterol, namely the hydroxylation at C22
CC followed with the hydroxylation at C20 to yield 20R,22R-
CC hydroxycholesterol that is further cleaved between C20 and C22 to yield
CC the C21-steroid pregnenolone and 4-methylpentanal. Mechanistically,
CC uses molecular oxygen inserting one oxygen atom into a substrate and
CC reducing the second into a water molecule. Two electrons are provided
CC by NADPH via a two-protein mitochondrial transfer system comprising
CC flavoprotein FDXR (adrenodoxin/ferredoxin reductase) and nonheme iron-
CC sulfur protein FDX1 or FDX2 (adrenodoxin/ferredoxin).
CC {ECO:0000256|RuleBase:RU364077}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesterol + 6 H(+) + 3 O2 + 6 reduced [adrenodoxin] = 4-
CC methylpentanal + 4 H2O + 6 oxidized [adrenodoxin] + pregnenolone;
CC Xref=Rhea:RHEA:35739, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16113, ChEBI:CHEBI:16581, ChEBI:CHEBI:17998,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.14.15.6;
CC Evidence={ECO:0000256|RuleBase:RU364077};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|RuleBase:RU364077};
CC -!- PATHWAY: Lipid metabolism; C21-steroid hormone metabolism.
CC {ECO:0000256|ARBA:ARBA00005108, ECO:0000256|RuleBase:RU364077}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|RuleBase:RU364077}; Peripheral membrane protein
CC {ECO:0000256|RuleBase:RU364077}. Note=Localizes to the matrix side of
CC the mitochondrion inner membrane. {ECO:0000256|RuleBase:RU364077}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU364077}.
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DR EMBL; AB281616; BAF36702.1; -; mRNA.
DR UniPathway; UPA00229; -.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008386; F:cholesterol monooxygenase (side-chain-cleaving) activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0008207; P:C21-steroid hormone metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24279; -; 1.
DR PANTHER; PTHR24279:SF3; CHOLESTEROL SIDE-CHAIN CLEAVAGE ENZYME, MITOCHONDRIAL; 1.
DR Pfam; PF00067; p450; 1.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
PE 2: Evidence at transcript level;
KW Cholesterol metabolism {ECO:0000256|RuleBase:RU364077};
KW Heme {ECO:0000256|RuleBase:RU364077}; Iron {ECO:0000256|RuleBase:RU364077};
KW Lipid metabolism {ECO:0000256|RuleBase:RU364077};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364077};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU364077};
KW Mitochondrion {ECO:0000256|RuleBase:RU364077};
KW Monooxygenase {ECO:0000256|RuleBase:RU364077};
KW Oxidoreductase {ECO:0000256|RuleBase:RU364077};
KW Steroid metabolism {ECO:0000256|RuleBase:RU364077};
KW Steroidogenesis {ECO:0000256|RuleBase:RU364077};
KW Sterol metabolism {ECO:0000256|RuleBase:RU364077};
KW Transit peptide {ECO:0000256|RuleBase:RU364077}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAF36702.1"
FT NON_TER 242
FT /evidence="ECO:0000313|EMBL:BAF36702.1"
SQ SEQUENCE 242 AA; 27700 MW; 2B20D1D3324262E5 CRC64;
DYRNKPYGVL LKTGEAWRSD RLTLNXEVLS PQVVGSFVPL LNQVSEDFVR RAQAQVQKSG
REHWTADFSH ELFRFALESV CHVLYGERLG LLQDFVDPEA QQFIDAVTLM FHTTSPMLYV
PPALLRHLNT KTWRDHVHAW DAIFTQADKC IQNVYRDIRL QRKSTEEHTG ILFSLLVQDK
LPLDDIKASV TEMMAGGVXT TSMTLQWAML ELARSPGIQE RIRAEVLAAK QEAQGDRVKM
LK
//
