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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_RAT               Reviewed;         526 AA.
P14137; Q5FWY8; Q6LDR9;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 1.
28-FEB-2018, entry version 145.
RecName: Full=Cholesterol side-chain cleavage enzyme, mitochondrial;
EC=1.14.15.6;
AltName: Full=CYPXIA1;
AltName: Full=Cholesterol desmolase;
AltName: Full=Cytochrome P450 11A1;
AltName: Full=Cytochrome P450(scc);
Flags: Precursor;
Name=Cyp11a1; Synonyms=Cyp11a, Cyp11a-1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2480959;
Oonk R.B., Krasnow J.S., Beattie W.G., Richards J.S.;
"Cyclic AMP-dependent and -independent regulation of cholesterol side
chain cleavage cytochrome P-450 (P-450scc) in rat ovarian granulosa
cells and corpora lutea. cDNA and deduced amino acid sequence of rat
P-450scc.";
J. Biol. Chem. 264:21934-21942(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2176216;
Oonk R.B., Parker K.L., Gibson J.L., Richards J.S.;
"Rat cholesterol side-chain cleavage cytochrome P-450 (P-450scc) gene.
Structure and regulation by cAMP in vitro.";
J. Biol. Chem. 265:22392-22401(1990).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 344-526, AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Ovary;
PubMed=3123325; DOI=10.1016/0378-1119(87)90170-3;
McMasters K.M., Dickson L.A., Shamy R.V., Robischon K.,
Macdonald G.J., Moyle W.R.;
"Rat cholesterol side-chain cleavage enzyme (P-450scc): use of a cDNA
probe to study the hormonal regulation of P-450scc mRNA levels in
ovarian granulosa cells.";
Gene 57:1-9(1987).
[5]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=3948785; DOI=10.1210/endo-118-4-1353;
Farkash Y., Timberg R., Orly J.;
"Preparation of antiserum to rat cytochrome P-450 cholesterol side
chain cleavage, and its use for ultrastructural localization of the
immunoreactive enzyme by protein A-gold technique.";
Endocrinology 118:1353-1365(1986).
[6]
SUBCELLULAR LOCATION.
PubMed=2170421;
Hanukoglu I., Suh B.S., Himmelhoch S., Amsterdam A.;
"Induction and mitochondrial localization of cytochrome P450scc system
enzymes in normal and transformed ovarian granulosa cells.";
J. Cell Biol. 111:1373-1381(1990).
[7]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=21075169; DOI=10.1016/j.mce.2010.10.020;
Pagotto M.A., Roldan M.L., Pagotto R.M., Lugano M.C., Pisani G.B.,
Rogic G., Molinas S.M., Trumper L., Pignataro O.P., Monasterolo L.A.;
"Localization and functional activity of cytochrome P450 side chain
cleavage enzyme (CYP11A1) in the adult rat kidney.";
Mol. Cell. Endocrinol. 332:253-260(2011).
-!- FUNCTION: Catalyzes the side-chain cleavage reaction of
cholesterol to pregnenolone, the precursor of most steroid
hormones. {ECO:0000250|UniProtKB:P05108}.
-!- CATALYTIC ACTIVITY: Cholesterol + 6 reduced adrenodoxin + 3 O(2) +
6 H(+) = pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin
+ 4 H(2)O. {ECO:0000250|UniProtKB:P05108}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000250|UniProtKB:P05108};
-!- PATHWAY: Lipid metabolism; C21-steroid hormone metabolism.
-!- SUBUNIT: Interacts with FDX1/adrenodoxin. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000269|PubMed:21075169, ECO:0000269|PubMed:2170421,
ECO:0000269|PubMed:3948785}; Peripheral membrane protein
{ECO:0000305}. Note=Localizes to the matrix side of the
mitochondrion inner membrane. {ECO:0000269|PubMed:3948785}.
-!- TISSUE SPECIFICITY: Expressed in the kidney where it localizes to
the distal convoluted tubule and the thick ascending limb of the
loop of Henle (at protein level) (PubMed:21075169). In the ovary,
highly expressed in interstitial cells (at protein level)
(PubMed:3948785). Also expressed in adrenal gland and testis
(PubMed:3123325). {ECO:0000269|PubMed:21075169,
ECO:0000269|PubMed:3123325, ECO:0000269|PubMed:3948785}.
-!- INDUCTION: Induced by FSH or pregnant mare's serum gonadotropin in
ovaries of estrogen-treated immature rats in vivo.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; J05156; AAA40989.1; -; mRNA.
EMBL; M63133; AAA40958.1; -; Genomic_DNA.
EMBL; M63125; AAA40958.1; JOINED; Genomic_DNA.
EMBL; M63126; AAA40958.1; JOINED; Genomic_DNA.
EMBL; M63127; AAA40958.1; JOINED; Genomic_DNA.
EMBL; M63128; AAA40958.1; JOINED; Genomic_DNA.
EMBL; M63129; AAA40958.1; JOINED; Genomic_DNA.
EMBL; M63130; AAA40958.1; JOINED; Genomic_DNA.
EMBL; M63131; AAA40958.1; JOINED; Genomic_DNA.
EMBL; M63132; AAA40958.1; JOINED; Genomic_DNA.
EMBL; BC089100; AAH89100.1; -; mRNA.
EMBL; M22615; AAA62267.1; -; mRNA.
PIR; A34164; A34164.
RefSeq; NP_058982.1; NM_017286.3.
UniGene; Rn.1401; -.
ProteinModelPortal; P14137; -.
SMR; P14137; -.
STRING; 10116.ENSRNOP00000010831; -.
BindingDB; P14137; -.
ChEMBL; CHEMBL5246; -.
iPTMnet; P14137; -.
PhosphoSitePlus; P14137; -.
PaxDb; P14137; -.
PRIDE; P14137; -.
GeneID; 29680; -.
KEGG; rno:29680; -.
UCSC; RGD:69325; rat.
CTD; 1583; -.
RGD; 69325; Cyp11a1.
eggNOG; KOG0159; Eukaryota.
eggNOG; COG2124; LUCA.
HOGENOM; HOG000013161; -.
HOVERGEN; HBG051098; -.
InParanoid; P14137; -.
KO; K00498; -.
OrthoDB; EOG091G04MV; -.
PhylomeDB; P14137; -.
SABIO-RK; P14137; -.
UniPathway; UPA00229; -.
PRO; PR:P14137; -.
Proteomes; UP000002494; Unplaced.
Genevisible; P14137; RN.
GO; GO:0030061; C:mitochondrial crista; IDA:RGD.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:RGD.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0043204; C:perikaryon; IDA:RGD.
GO; GO:0015485; F:cholesterol binding; IMP:RGD.
GO; GO:0008386; F:cholesterol monooxygenase (side-chain-cleaving) activity; IMP:RGD.
GO; GO:0020037; F:heme binding; ISS:UniProtKB.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0018879; P:biphenyl metabolic process; IEP:RGD.
GO; GO:0006700; P:C21-steroid hormone biosynthetic process; IDA:RGD.
GO; GO:0071236; P:cellular response to antibiotic; IEP:RGD.
GO; GO:0071276; P:cellular response to cadmium ion; IEP:RGD.
GO; GO:0071320; P:cellular response to cAMP; IEP:RGD.
GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEP:RGD.
GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IEP:RGD.
GO; GO:0071371; P:cellular response to gonadotropin stimulus; IEP:RGD.
GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEP:RGD.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:RGD.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
GO; GO:0021549; P:cerebellum development; IEP:RGD.
GO; GO:0008203; P:cholesterol metabolic process; ISS:UniProtKB.
GO; GO:0018894; P:dibenzo-p-dioxin metabolic process; IEP:RGD.
GO; GO:0060014; P:granulosa cell differentiation; IEP:RGD.
GO; GO:0021766; P:hippocampus development; IEP:RGD.
GO; GO:0033327; P:Leydig cell differentiation; IEP:RGD.
GO; GO:0008584; P:male gonad development; IEP:RGD.
GO; GO:0060135; P:maternal process involved in female pregnancy; IEP:RGD.
GO; GO:0007617; P:mating behavior; IMP:RGD.
GO; GO:0006082; P:organic acid metabolic process; IEP:RGD.
GO; GO:0018958; P:phenol-containing compound metabolic process; IEP:RGD.
GO; GO:0018963; P:phthalate metabolic process; IEP:RGD.
GO; GO:0043279; P:response to alkaloid; IEP:RGD.
GO; GO:0043200; P:response to amino acid; IEP:RGD.
GO; GO:0046677; P:response to antibiotic; IEP:RGD.
GO; GO:0046686; P:response to cadmium ion; IEP:RGD.
GO; GO:0051591; P:response to cAMP; IEP:RGD.
GO; GO:0051412; P:response to corticosterone; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0043627; P:response to estrogen; IEP:RGD.
GO; GO:0060992; P:response to fungicide; IEP:RGD.
GO; GO:0010332; P:response to gamma radiation; IEP:RGD.
GO; GO:0033595; P:response to genistein; IEP:RGD.
GO; GO:0034698; P:response to gonadotropin; IEP:RGD.
GO; GO:0042542; P:response to hydrogen peroxide; IMP:RGD.
GO; GO:0017085; P:response to insecticide; IEP:RGD.
GO; GO:0010212; P:response to ionizing radiation; IEP:RGD.
GO; GO:0033591; P:response to L-ascorbic acid; IEP:RGD.
GO; GO:0007584; P:response to nutrient; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
GO; GO:0009651; P:response to salt stress; IEP:RGD.
GO; GO:0048545; P:response to steroid hormone; IEP:RGD.
GO; GO:0033197; P:response to vitamin E; IEP:RGD.
GO; GO:0014037; P:Schwann cell differentiation; IEP:RGD.
GO; GO:0006694; P:steroid biosynthetic process; IMP:RGD.
GO; GO:0061370; P:testosterone biosynthetic process; IEP:RGD.
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;
Cholesterol metabolism; Complete proteome; Heme; Iron;
Lipid metabolism; Membrane; Metal-binding; Mitochondrion;
Mitochondrion inner membrane; Monooxygenase; Oxidoreductase;
Reference proteome; Steroid metabolism; Steroidogenesis;
Sterol metabolism; Transit peptide.
TRANSIT 1 36 Mitochondrion.
{ECO:0000250|UniProtKB:P00189}.
CHAIN 37 526 Cholesterol side-chain cleavage enzyme,
mitochondrial.
/FTId=PRO_0000003590.
METAL 459 459 Iron (heme axial ligand).
{ECO:0000250|UniProtKB:P05108}.
SEQUENCE 526 AA; 60586 MW; B2930E40018DC1EE CRC64;
MLAKGLCLRS VLVKSCQPFL SPVWQGPGLA TGNGAGISST NSPRSFNEIP SPGDNGWINL
YHFLRENGTH RIHYHHMQNF QKYGPIYREK LGNMESVYIL DPKDAATLFS CEGPNPERYL
VPPWVAYHQY YQRPIGVLFK SSDAWRKDRI VLNQEVMAPD SIKNFVPLLE GVAQDFIKVL
HRRIKQQNSG KFSGDISDDL FRFAFESITS VVFGERLGML EEIVDPESQR FIDAVYQMFH
TSVPMLNMPP DLFRLFRTKT WKDHAAAWDV IFSKADEYTQ NFYWDLRQKR DFSKYPGVLY
SLLGGNKLPF KNIQANITEM LAGGVDTTSM TLQWNLYEMA HNLKVQEMLR AEVLAARRQA
QGDMAKMVQL VPLLKASIKE TLRLHPISVT LQRYIVNDLV LRNYKIPAKT LVQVASYAMG
RESSFFPNPN KFDPTRWLEK SQNTTHFRYL GFGWGVRQCL GRRIAELEMT IFLINVLENF
RIEVQSIRDV GTKFNLILMP EKPIFFNFQP LKQDLGSTMP RKGDTV


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