ID   CP11A_SHEEP             Reviewed;         520 AA.
AC   P79202;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   26-MAY-2009, entry version 58.
DE   RecName: Full=Cholesterol side-chain cleavage enzyme, mitochondrial;
DE            EC=1.14.15.6;
DE   AltName: Full=Cytochrome P450 11A1;
DE   AltName: Full=CYPXIA1;
DE   AltName: Full=P450(SCC);
DE   AltName: Full=Cholesterol desmolase;
DE   Flags: Precursor;
GN   Name=CYP11A1;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Adrenal cortex;
RX   MEDLINE=96244421; PubMed=8645627; DOI=10.1016/0960-0760(95)00263-4;
RA   Okuyama E., Okazaki T., Furukawa A., Wu R.-F., Ichikawa Y.;
RT   "Molecular cloning and nucleotide sequences of cDNA clones of sheep
RT   and goat adrenocortical cytochromes P450scc (CYP11A1).";
RL   J. Steroid Biochem. Mol. Biol. 57:179-185(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 40-62.
RC   TISSUE=Adrenal cortex;
RX   MEDLINE=95035073; PubMed=7948001; DOI=10.1016/0005-2760(94)90108-2;
RA   Miyatake A., Tsubaki M., Hori H., Ichikawa Y.;
RT   "Purification and comparative characterization of cytochrome P-450scc
RT   (CYP XIA1) from sheep adrenocortical mitochondria.";
RL   Biochim. Biophys. Acta 1215:176-182(1994).
CC   -!- FUNCTION: Catalyzes the side-chain cleavage reaction of
CC       cholesterol to pregnenolone.
CC   -!- CATALYTIC ACTIVITY: Cholesterol + reduced adrenal ferredoxin +
CC       O(2) = pregnenolone + 4-methylpentanal + oxidized adrenal
CC       ferredoxin + H(2)O.
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- PATHWAY: Lipid metabolism; C21-steroid hormone metabolism.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR   EMBL; D50057; BAA08775.1; -; mRNA.
DR   RefSeq; NP_001087258.1; -.
DR   UniGene; Oar.5829; -.
DR   HSSP; P00189; 1SCC.
DR   GeneID; 100048994; -.
DR   HOVERGEN; P79202; -.
DR   BRENDA; 1.14.15.6; 271.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008386; F:cholesterol monooxygenase (side-chain-cleav...; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006700; P:C21-steroid hormone biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017973; Cyt_P450_C.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   Gene3D; G3DSA:1.10.630.10; Cyt_P450; 1.
DR   PANTHER; PTHR19383; Cyt_P450; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Cholesterol metabolism; Direct protein sequencing; Heme; Iron;
KW   Lipid metabolism; Membrane; Metal-binding; Mitochondrion;
KW   Monooxygenase; Oxidoreductase; Steroid metabolism; Steroidogenesis;
KW   Transit peptide.
FT   TRANSIT       1     39       Mitochondrion.
FT   CHAIN        40    520       Cholesterol side-chain cleavage enzyme,
FT                                mitochondrial.
FT                                /FTId=PRO_0000003591.
FT   METAL       461    461       Iron (heme axial ligand) (By similarity).
SQ   SEQUENCE   520 AA;  60357 MW;  DF8989FB8A87E8AE CRC64;
     MLARGLPFRS ALVKACPPLL NTGREGWGHH RVGTGEGAGI STRTPRPYSE IPSPGDNGWI
     NLYHFWRKKG SQRIHFHHIE NFQKYGPIYR EKLGNLESVY IIHPEGVAHL FKFEGSYPQR
     YDIPPWLAYH RYYQKPIGVL FKKSGAWKKD RVVLNTEVMA PEAIKNFIPL LNPVSQDFVS
     LLHKRIKQQG SGKFVGDIKE DLFRFAFESI TNVMFGERLG MLEDTVDTEA QKFIDAVYKM
     FHTSVPLLNL PPELYRLFRT KTWRDHVAAW DTIFNKAEKY TEIFYQDLRQ KTEFRNYPGI
     LYHLLKSEKM LLEDVKANIT EMLAGGVDTT SMTLQWHLYE MARSLNVQEM LRKEVLNARR
     QAEGDISKML QMVPLLKASI KETLRLHPIS VTLQRYPESD LVLQDYLIPA KTLVQVAIYA
     MGRDPAFFSN PDKFDPTRWL GKDKDLIHFR NLGFGWGVRQ CVGRRIAELE MTLFLIHILE
     NFRVEMQQIG DVNTIFNLIL TPDKPIFLVF RPFNQGPPQA
//