ID   CP11A_HYPAM             Reviewed;         514 AA.
AC   Q92045;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 97.
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; Fragment;
GN   Name=CYP11A1;
OS   Hypanus americanus (Southern stingray) (Dasyatis americana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Batoidea; Myliobatiformes; Dasyatidae; Hypanus.
OX   NCBI_TaxID=2484686;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Interrenal gland;
RX   PubMed=9073075; DOI=10.1016/s0378-1119(96)00734-2;
RA   Nunez S., Trant J.M.;
RT   "Isolation of the putative cDNA encoding cholesterol side chain cleavage
RT   cytochrome P450 (CYP11A) of the southern stingray (Dasyatis americana).";
RL   Gene 187:123-129(1997).
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   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; U63299; AAC60095.1; -; mRNA.
DR   AlphaFoldDB; Q92045; -.
DR   SMR; Q92045; -.
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_0000003592"
FT   BINDING         461
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"
FT   NON_TER         1
SQ   SEQUENCE   514 AA;  59863 MW;  D0F03E25D5534FB2 CRC64;
     SFRLSLSAST YAQRGSFTTP EHDFTLFPHR NHSVTSESRI PSEQTLKSLT DIPGNWRKNW
     LNVYYFWRSN GLNNAHQWML DNFNKYGPIY REKIAYYESI NIINPADAVI MNKSEGPFPK
     RIEMAPWVAY RDLRKENYGV QLLNGENWKR TRLILNNSIF AQSSIQRLVP LFNEVVLDFV
     SMVHKEVEKS RSDYWKTDLT NDLFKLALEV ICYILYGERL DLLQRKYNKA PQKFIDSIAT
     MFHSTPIMLY VPPSLLKSIN SKIWQQHVGS WDNIFEHADT YLKKAYRQFQ QGSKNEHAFP
     GVLTELLLQG ALPFEDIRAS IIDVMSGAID TTSTTVHWMM YELAKHPHIQ KNVRSEIMEA
     HQKTEGDPVK MLKSVPLLKC VVKETLRLYP VAISIQRYLN EDTVLQNYHI PAGTLVQLGL
     YAMGRNPKIF KNPEQYNPER WLKGEDTHFR HLGFGFGPRQ CIGRRIAETQ MVLLMIHMLQ
     NFKIETDPMT EVKSKFSLIL IPDKPINLKF TPIK