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   03-AUG-2022, entry version 103.
DE   RecName: Full=Cholesterol side-chain cleavage enzyme, mitochondrial;
DE            EC=1.14.15.6;
DE   AltName: Full=CYPXIA1;
DE   AltName: Full=Cholesterol desmolase;
DE   AltName: Full=Cytochrome P450 11A1;
DE   AltName: Full=Cytochrome P450(scc);
DE   Flags: Precursor;
GN   Name=cyp11a1;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Ovary;
RX   PubMed=8454060; DOI=10.1016/0014-5793(93)80034-r;
RA   Takahashi M., Tanaka M., Sakai N., Adachi S., Miller W.L., 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 cholesterol to
CC       pregnenolone, the precursor of most steroid hormones.
CC       {ECO:0000250|UniProtKB:P05108}.
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:0000250|UniProtKB:P05108};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P05108};
CC   -!- PATHWAY: Lipid metabolism; C21-steroid hormone metabolism.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P14137}; Peripheral membrane protein
CC       {ECO:0000305}. Note=Localizes to the matrix side of the mitochondrion
CC       inner membrane. {ECO:0000250|UniProtKB:P14137}.
CC   -!- TISSUE SPECIFICITY: In the ovary, not found in early vitellogenic
CC       follicles, barely detected in postvitellogenic follicles and abundant
CC       in post-ovulatory follicles. {ECO:0000269|PubMed:8454060}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; S57305; AAB25804.1; -; mRNA.
DR   PIR; S32197; S32197.
DR   AlphaFoldDB; Q07217; -.
DR   SMR; Q07217; -.
DR   PRIDE; Q07217; -.
DR   UniPathway; UPA00229; -.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
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:0006700; P:C21-steroid hormone biosynthetic process; IEA:InterPro.
DR   GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR033283; CYP11A1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24279:SF3; PTHR24279:SF3; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Cholesterol metabolism; Heme; Iron; Lipid metabolism; Membrane;
KW   Metal-binding; Mitochondrion; Mitochondrion inner membrane; Monooxygenase;
KW   Oxidoreductase; Steroid metabolism; Steroidogenesis; Sterol metabolism;
KW   Transit peptide.
FT   TRANSIT         1..39
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250|UniProtKB:P00189"
FT   CHAIN           40..514
FT                   /note="Cholesterol side-chain cleavage enzyme,
FT                   mitochondrial"
FT                   /id="PRO_0000003593"
FT   BINDING         458
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P05108"
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