ID   CP11A_ONCMY             Reviewed;         514 AA.
AC   Q07217;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   26-MAY-2009, entry version 56.
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   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei;
OC   Protacanthopterygii; Salmoniformes; Salmonidae; Salmoninae;
OC   Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   MEDLINE=93202273; PubMed=8454060; DOI=10.1016/0014-5793(93)80034-R;
RA   Takahashi M., Tanaka M., Sakai N., Adachi S., Miller W.L.,
RA   Nagahama Y.;
RT   "Rainbow trout ovarian cholesterol side-chain cleavage cytochrome P450
RT   (P450scc). cDNA cloning and mRNA expression during oogenesis.";
RL   FEBS Lett. 319:45-48(1993).
CC   -!- FUNCTION: Catalyzes the side-chain cleavage reaction of
CC       cholesterol to pregnenolone. Increased amounts during final oocyte
CC       maturation may be responsible for the rapid increase in the
CC       follicular production of maturation-inducing hormone 17-alpha,20-
CC       beta-DP.
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   -!- TISSUE SPECIFICITY: Not found in early vitellogenic follicles,
CC       barely detected in postvitellogenic follicles and abundant in post
CC       ovulatory follicles.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR   EMBL; S57305; AAB25804.1; -; mRNA.
DR   PIR; S32197; S32197.
DR   HSSP; P00189; 1SCC.
DR   HOVERGEN; Q07217; -.
DR   BRENDA; 1.14.15.6; 3435.
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   2: Evidence at transcript level;
KW   Cholesterol metabolism; Heme; Iron; Lipid metabolism; Membrane;
KW   Metal-binding; Mitochondrion; Monooxygenase; Oxidoreductase;
KW   Steroid metabolism; Steroidogenesis; Transit peptide.
FT   TRANSIT       1     39       Mitochondrion (Potential).
FT   CHAIN        40    514       Cholesterol side-chain cleavage enzyme,
FT                                mitochondrial.
FT                                /FTId=PRO_0000003593.
FT   METAL       458    458       Iron (heme axial ligand) (By similarity).
SQ   SEQUENCE   514 AA;  59137 MW;  0C6F49ECE8FF38FD CRC64;
     MMVSWSVCRS SLALPACGLP SARHNSSMPV VRQALSPDNS STVQNFSEIP GLWRNGLANL
     YSFWKLDGFR NIHRVMVHNF NTFGPIYREK IGYYDSVNII KPEMPAILFK AEGHYPKRLT
     VEAWTSYRDY RNRKYGVLLK NGEDWRSNRV ILNREVISPK VLGNFVPLLD EVGQDFVARV
     HKKIERSGQD KWTTDLSQEL FKYALESVGS VLYGERLGLM LDYINPEAQH FIDCISLMFK
     TTSPMLYIPP AMLRRVGAKI WRDHVEAWDG IFNQADRCIQ NIYRTMRQDT NTHGKYPGVL
     ASLLMLDKLS IEDIKASVTE LMAGGVDTTS ITLLWTLYEL ARHPDLQEEL RAEVAVARQS
     TQGDMLQMLK MIPLVKGALK ETLRLHPVAV SLQRYITEEI VIQNYHIPCG TLVQLGLYAM
     GRDPDVFPRP EKYLPSRWLR TENQYFRSLG FGFGPRQCLG RRIAETEMQL FLIHMLENFR
     VDKQRQVEVH STFELILLPE KPILLTLKPL KSGQ
//