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Cholesterol side-chain cleavage enzyme, mitochondrial (EC 1.14.15.6) (CYPXIA1) (Cholesterol desmolase) (Cytochrome P450 11A1) (Cytochrome P450(scc))

 CP11A_BOVIN             Reviewed;         520 AA.
P00189; Q28152;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
12-AUG-2020, entry version 144.
RecName: Full=Cholesterol side-chain cleavage enzyme, mitochondrial {ECO:0000303|PubMed:3518802};
EC=1.14.15.6 {ECO:0000269|PubMed:11412116};
AltName: Full=CYPXIA1;
AltName: Full=Cholesterol desmolase;
AltName: Full=Cytochrome P450 11A1;
AltName: Full=Cytochrome P450(scc);
Flags: Precursor;
Name=CYP11A1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Adrenal cortex;
PubMed=6589615; DOI=10.1073/pnas.81.15.4647;
Morohashi K., Fujii-Kuriyama Y., Okada Y., Sogawa K., Hirose T.,
Inayama S., Omura T.;
"Molecular cloning and nucleotide sequence of cDNA for mRNA of
mitochondrial cytochrome P-450(SCC) of bovine adrenal cortex.";
Proc. Natl. Acad. Sci. U.S.A. 81:4647-4651(1984).
[2]
PROTEIN SEQUENCE OF 40-520.
PubMed=3518802; DOI=10.1016/0167-4838(86)90176-7;
Chashchin V.L., Lapko V.N., Adamovich T.B., Lapko A.G., Kuprina N.S.,
Akhrem A.A.;
"Primary structure of the cholesterol side-chain cleavage cytochrome P-450
from bovine adrenocortical mitochondria and some aspects of its functioning
on a structural level.";
Biochim. Biophys. Acta 871:217-223(1986).
[3]
PROTEIN SEQUENCE OF 40-54.
PubMed=6654880;
Ogishima T., Okada Y., Kominami S., Takemori S., Omura T.;
"Partial amino acid sequences of two mitochondrial and two microsomal
cytochrome P-450's from adrenal cortex.";
J. Biochem. 94:1711-1714(1983).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-90.
PubMed=2154474;
Ahlgren R., Simpson E.R., Waterman M.R., Lund J.;
"Characterization of the promoter/regulatory region of the bovine CYP11A
(P-450scc) gene. Basal and cAMP-dependent expression.";
J. Biol. Chem. 265:3313-3319(1990).
[5]
TISSUE SPECIFICITY.
PubMed=3011431; DOI=10.1111/j.1432-1033.1986.tb09633.x;
Hanukoglu I., Hanukoglu Z.;
"Stoichiometry of mitochondrial cytochromes P-450, adrenodoxin and
adrenodoxin reductase in adrenal cortex and corpus luteum. Implications for
membrane organization and gene regulation.";
Eur. J. Biochem. 157:27-31(1986).
[6]
3D-STRUCTURE MODELING OF 40-520.
PubMed=1477100; DOI=10.1016/0167-4838(92)90089-v;
Vijayakumar S., Salerno J.C.;
"Molecular modeling of the 3-D structure of cytochrome P-450scc.";
Biochim. Biophys. Acta 1160:281-286(1992).
[7]
FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF PHE-233, AND PATHWAY.
PubMed=11412116; DOI=10.1021/bi010193i;
Pikuleva I.A., Puchkaev A., Bjoerkhem I.;
"Putative helix F contributes to regioselectivity of hydroxylation in
mitochondrial cytochrome P450 27A1.";
Biochemistry 40:7621-7629(2001).
[8]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 41-520 IN COMPLEX WITH HEME AND
22R-HYDROXYCHOLESTEROL, AND COFACTOR.
PubMed=21159775; DOI=10.1074/jbc.m110.188433;
Mast N., Annalora A.J., Lodowski D.T., Palczewski K., Stout C.D.,
Pikuleva I.A.;
"Structural basis for three-step sequential catalysis by the cholesterol
side chain cleavage enzyme CYP11A1.";
J. Biol. Chem. 286:5607-5613(2011).
-!- FUNCTION: A cytochrome P450 monooxygenase that catalyzes the side-chain
hydroxylation and cleavage of cholesterol to pregnenolone, the
precursor of most steroid hormones (PubMed:11412116). Catalyzes three
sequential oxidation reactions of cholesterol, namely the hydroxylation
at C22 followed with the hydroxylation at C20 to yield 20R,22R-
hydroxycholesterol that is further cleaved between C20 and C22 to yield
the C21-steroid pregnenolone and 4-methylpentanal (PubMed:11412116).
Mechanistically, uses molecular oxygen inserting one oxygen atom into a
substrate and reducing the second into a water molecule. Two electrons
are provided by NADPH via a two-protein mitochondrial transfer system
comprising flavoprotein FDXR (adrenodoxin/ferredoxin reductase) and
nonheme iron-sulfur protein FDX1 or FDX2 (adrenodoxin/ferredoxin)
(PubMed:11412116). {ECO:0000269|PubMed:11412116}.
-!- CATALYTIC ACTIVITY:
Reaction=cholesterol + 6 H(+) + 3 O2 + 6 reduced [adrenodoxin] = 4-
methylpentanal + 4 H2O + 6 oxidized [adrenodoxin] + pregnenolone;
Xref=Rhea:RHEA:35739, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
ChEBI:CHEBI:16113, ChEBI:CHEBI:16581, ChEBI:CHEBI:17998,
ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.14.15.6;
Evidence={ECO:0000269|PubMed:11412116};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35740;
Evidence={ECO:0000305|PubMed:11412116};
-!- CATALYTIC ACTIVITY:
Reaction=cholesterol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = 22R-
hydroxycholesterol + H2O + 2 oxidized [adrenodoxin];
Xref=Rhea:RHEA:34335, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
ChEBI:CHEBI:16113, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
ChEBI:CHEBI:67237; Evidence={ECO:0000269|PubMed:11412116};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34336;
Evidence={ECO:0000305|PubMed:11412116};
-!- CATALYTIC ACTIVITY:
Reaction=22R-hydroxycholesterol + 2 H(+) + O2 + 2 reduced [adrenodoxin]
= (20R,22R)-20,22-dihydroxycholesterol + H2O + 2 oxidized
[adrenodoxin]; Xref=Rhea:RHEA:34339, Rhea:RHEA-COMP:9998, Rhea:RHEA-
COMP:9999, ChEBI:CHEBI:1294, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
ChEBI:CHEBI:67237; Evidence={ECO:0000269|PubMed:11412116};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34340;
Evidence={ECO:0000305|PubMed:11412116};
-!- CATALYTIC ACTIVITY:
Reaction=(20R,22R)-20,22-dihydroxycholesterol + 2 H(+) + O2 + 2 reduced
[adrenodoxin] = 4-methylpentanal + 2 H2O + 2 oxidized [adrenodoxin] +
pregnenolone; Xref=Rhea:RHEA:34343, Rhea:RHEA-COMP:9998, Rhea:RHEA-
COMP:9999, ChEBI:CHEBI:1294, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:15379, ChEBI:CHEBI:16581, ChEBI:CHEBI:17998,
ChEBI:CHEBI:33737, ChEBI:CHEBI:33738;
Evidence={ECO:0000269|PubMed:11412116};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34344;
Evidence={ECO:0000305|PubMed:11412116};
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000269|PubMed:21159775};
-!- PATHWAY: Lipid metabolism; C21-steroid hormone metabolism.
{ECO:0000269|PubMed:11412116}.
-!- PATHWAY: Steroid metabolism; cholesterol metabolism.
{ECO:0000269|PubMed:11412116}.
-!- SUBUNIT: Interacts with FDX1/adrenodoxin.
{ECO:0000250|UniProtKB:P05108}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000250|UniProtKB:P14137}; Peripheral membrane protein
{ECO:0000305}. Note=Localizes to the matrix side of the mitochondrion
inner membrane. {ECO:0000250|UniProtKB:P14137}.
-!- TISSUE SPECIFICITY: Detected in adrenal cortex and corpus luteum (at
protein level). {ECO:0000269|PubMed:3011431}.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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EMBL; K02130; AAA30488.1; -; mRNA.
EMBL; J05245; AAA30681.1; -; Genomic_DNA.
PIR; A00189; O4BOM.
RefSeq; NP_788817.1; NM_176644.2.
PDB; 1SCC; Model; -; A=40-520.
PDB; 2ASA; Model; -; A=87-516.
PDB; 3MZS; X-ray; 2.50 A; A/B/C/D=41-520.
PDBsum; 1SCC; -.
PDBsum; 2ASA; -.
PDBsum; 3MZS; -.
SMR; P00189; -.
STRING; 9913.ENSBTAP00000009106; -.
BindingDB; P00189; -.
ChEMBL; CHEMBL4813; -.
DrugCentral; P00189; -.
PaxDb; P00189; -.
PRIDE; P00189; -.
GeneID; 338048; -.
KEGG; bta:338048; -.
CTD; 1583; -.
eggNOG; KOG0159; Eukaryota.
InParanoid; P00189; -.
KO; K00498; -.
OrthoDB; 561463at2759; -.
BRENDA; 1.14.15.6; 908.
SABIO-RK; P00189; -.
UniPathway; UPA00229; -.
UniPathway; UPA00296; -.
PRO; PR:P00189; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0008386; F:cholesterol monooxygenase (side-chain-cleaving) activity; IDA:UniProtKB.
GO; GO:0020037; F:heme binding; ISS:UniProtKB.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0006700; P:C21-steroid hormone biosynthetic process; IDA:UniProtKB.
GO; GO:0071375; P:cellular response to peptide hormone stimulus; IBA:GO_Central.
GO; GO:0008203; P:cholesterol metabolic process; IDA:UniProtKB.
GO; GO:0034650; P:cortisol metabolic process; IBA:GO_Central.
GO; GO:0006704; P:glucocorticoid biosynthetic process; IBA:GO_Central.
GO; GO:0042359; P:vitamin D metabolic process; IDA:UniProtKB.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR033283; CYP11A1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002401; Cyt_P450_E_grp-I.
InterPro; IPR036396; Cyt_P450_sf.
PANTHER; PTHR24279:SF3; PTHR24279:SF3; 1.
Pfam; PF00067; p450; 1.
PRINTS; PR00463; EP450I.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
1: Evidence at protein level;
3D-structure; Cholesterol metabolism; Direct protein sequencing; Heme;
Iron; Lipid metabolism; Membrane; Metal-binding; Mitochondrion;
Mitochondrion inner membrane; Monooxygenase; Oxidoreductase;
Reference proteome; Steroid metabolism; Steroidogenesis; Sterol metabolism;
Transit peptide.
TRANSIT 1..39
/note="Mitochondrion"
/evidence="ECO:0000269|PubMed:3518802,
ECO:0000269|PubMed:6654880"
CHAIN 40..520
/note="Cholesterol side-chain cleavage enzyme,
mitochondrial"
/id="PRO_0000003582"
METAL 461
/note="Iron (heme axial ligand)"
/evidence="ECO:0000244|PDB:3MZS,
ECO:0000269|PubMed:21159775"
MUTAGEN 233
/note="F->A: Impairs the hydroxylase activity toward
cholesterol; increases the electron leakage from the
electron transfer chain."
/evidence="ECO:0000269|PubMed:11412116"
MUTAGEN 233
/note="F->K: Markedly reduces the hydroxylase activity
toward cholesterol."
/evidence="ECO:0000269|PubMed:11412116"
CONFLICT 22
/note="T -> S (in Ref. 4; AAA30681)"
/evidence="ECO:0000305"
CONFLICT 57
/note="N -> D (in Ref. 2; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 106
/note="D -> N (in Ref. 2; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 197
/note="D -> N (in Ref. 2; AA sequence)"
/evidence="ECO:0000305"
HELIX 48..50
/evidence="ECO:0000244|PDB:3MZS"
HELIX 58..68
/evidence="ECO:0000244|PDB:3MZS"
HELIX 70..72
/evidence="ECO:0000244|PDB:3MZS"
HELIX 74..85
/evidence="ECO:0000244|PDB:3MZS"
STRAND 87..90
/evidence="ECO:0000244|PDB:3MZS"
STRAND 99..101
/evidence="ECO:0000244|PDB:3MZS"
HELIX 104..112
/evidence="ECO:0000244|PDB:3MZS"
HELIX 124..133
/evidence="ECO:0000244|PDB:3MZS"
TURN 139..141
/evidence="ECO:0000244|PDB:3MZS"
HELIX 145..158
/evidence="ECO:0000244|PDB:3MZS"
TURN 161..167
/evidence="ECO:0000244|PDB:3MZS"
HELIX 168..189
/evidence="ECO:0000244|PDB:3MZS"
STRAND 190..192
/evidence="ECO:0000244|PDB:3MZS"
STRAND 194..196
/evidence="ECO:0000244|PDB:3MZS"
HELIX 199..215
/evidence="ECO:0000244|PDB:3MZS"
STRAND 223..225
/evidence="ECO:0000244|PDB:3MZS"
HELIX 229..242
/evidence="ECO:0000244|PDB:3MZS"
HELIX 243..247
/evidence="ECO:0000244|PDB:3MZS"
HELIX 252..254
/evidence="ECO:0000244|PDB:3MZS"
HELIX 255..258
/evidence="ECO:0000244|PDB:3MZS"
HELIX 260..289
/evidence="ECO:0000244|PDB:3MZS"
HELIX 300..306
/evidence="ECO:0000244|PDB:3MZS"
HELIX 312..343
/evidence="ECO:0000244|PDB:3MZS"
HELIX 345..355
/evidence="ECO:0000244|PDB:3MZS"
TURN 356..362
/evidence="ECO:0000244|PDB:3MZS"
HELIX 366..369
/evidence="ECO:0000244|PDB:3MZS"
HELIX 374..386
/evidence="ECO:0000244|PDB:3MZS"
STRAND 389..391
/evidence="ECO:0000244|PDB:3MZS"
STRAND 393..395
/evidence="ECO:0000244|PDB:3MZS"
STRAND 401..408
/evidence="ECO:0000244|PDB:3MZS"
STRAND 414..416
/evidence="ECO:0000244|PDB:3MZS"
HELIX 418..423
/evidence="ECO:0000244|PDB:3MZS"
TURN 425..427
/evidence="ECO:0000244|PDB:3MZS"
STRAND 428..430
/evidence="ECO:0000244|PDB:3MZS"
HELIX 436..440
/evidence="ECO:0000244|PDB:3MZS"
STRAND 446..449
/evidence="ECO:0000244|PDB:3MZS"
HELIX 457..459
/evidence="ECO:0000244|PDB:3MZS"
HELIX 464..479
/evidence="ECO:0000244|PDB:3MZS"
STRAND 485..488
/evidence="ECO:0000244|PDB:3MZS"
STRAND 494..504
/evidence="ECO:0000244|PDB:3MZS"
STRAND 508..510
/evidence="ECO:0000244|PDB:3MZS"
SEQUENCE 520 AA; 60333 MW; 81C84B4AE0E70418 CRC64;
MLARGLPLRS ALVKACPPIL STVGEGWGHH RVGTGEGAGI STKTPRPYSE IPSPGDNGWL
NLYHFWREKG SQRIHFRHIE NFQKYGPIYR EKLGNLESVY IIHPEDVAHL FKFEGSYPER
YDIPPWLAYH RYYQKPIGVL FKKSGTWKKD RVVLNTEVMA PEAIKNFIPL LNPVSQDFVS
LLHKRIKQQG SGKFVGDIKE DLFHFAFESI TNVMFGERLG MLEETVNPEA QKFIDAVYKM
FHTSVPLLNV PPELYRLFRT KTWRDHVAAW DTIFNKAEKY TEIFYQDLRR KTEFRNYPGI
LYCLLKSEKM LLEDVKANIT EMLAGGVNTT SMTLQWHLYE MARSLNVQEM LREEVLNARR
QAEGDISKML QMVPLLKASI KETLRLHPIS VTLQRYPESD LVLQDYLIPA KTLVQVAIYA
MGRDPAFFSS PDKFDPTRWL SKDKDLIHFR NLGFGWGVRQ CVGRRIAELE MTLFLIHILE
NFKVEMQHIG DVDTIFNLIL TPDKPIFLVF RPFNQDPPQA


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Pathways :
WP1274: cytochrome P450
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WP1502: Mitochondrial biogenesis
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WP1077: cytochrome P450
WP958: cytochrome P450
WP696: Benzo(a)pyrene metabolism
WP1194: cytochrome P450
WP43: cytochrome P450
WP1633: Bisphenol A degradation
WP1634: Butanoate metabolism
WP132: Cholesterol Biosynthesis
WP952: Cholesterol Biosynthesis
WP1070: Cholesterol Biosynthesis
WP1186: Cholesterol Biosynthesis
WP2011: SREBF and miR33 in cholesterol and lipid homeostasis
WP1573: Phase I, non P450
WP461: Cholesterol Biosynthesis
WP103: Cholesterol Biosynthesis
WP1652: Fructose and mannose metabolism
WP1666: Linoleic acid metabolism
WP626: Abscisic Acid Biosynthesis
WP136: Phase I, non P450

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Bibliography :
[31917682] Long-term outcome of partial P450 side-chain cleavage enzyme deficiency in three brothers: the importance of early diagnosis.
[31398249] Sex Differences in Adrenal Bmal1 Deletion-Induced Augmentation of Glucocorticoid Responses to Stress and ACTH in Mice.
[31051467] Deficient pregnenolone synthesis associated with congenital adrenal hyperplasia and organelle dysfunction.
[30348838] Inner Mitochondrial Translocase Tim50 Is Central in Adrenal and Testicular Steroid Synthesis.
[29995203] Heterozygous mutations in the cholesterol side-chain cleavage enzyme gene (CYP11A1) can cause transient adrenal insufficiency and life-threatening failure to thrive.
[27855232] Novel SCC mutation in a patient of Mexican descent with sex reversal, salt-losing crisis and adrenal failure.
[26995740] MCL1 is a key regulator of steroidogenesis in mouse Leydig cells.
[25318172] Cyp11A1 canola plants under short time heat stress conditions.
[24404170] Targeting of GFP-Cre to the mouse Cyp11a1 locus both drives cre recombinase expression in steroidogenic cells and permits generation of Cyp11a1 knock out mice.
[23330251] Genetic defects in pregnenolone synthesis.