ID   CP27A_RAT               Reviewed;         533 AA.
AC   P17178; Q64615; Q64639;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   04-NOV-2026, entry version 176.
DE   RecName: Full=Sterol 26-hydroxylase, mitochondrial {ECO:0000303|PubMed:2175615};
DE            EC=1.14.15.15 {ECO:0000250|UniProtKB:P17177, ECO:0000250|UniProtKB:Q02318};
DE   AltName: Full=5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol 26-hydroxylase;
DE   AltName: Full=Cytochrome P-450C27/25;
DE   AltName: Full=Cytochrome P450 27;
DE   AltName: Full=Sterol 27-hydroxylase {ECO:0000250|UniProtKB:Q02318};
DE   AltName: Full=Vitamin D(3) 25-hydroxylase {ECO:0000303|PubMed:2175615};
DE   Flags: Precursor;
GN   Name=Cyp27a1; Synonyms=Cyp27;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 33-37.
RC   STRAIN=Wistar; TISSUE=Liver;
RX   PubMed=2318307; DOI=10.1016/0014-5793(90)80172-f;
RA   Usui E., Noshiro M., Okuda K.;
RT   "Molecular cloning of cDNA for vitamin D3 25-hydroxylase from rat liver
RT   mitochondria.";
RL   FEBS Lett. 262:135-138(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Liver;
RX   PubMed=2175615; DOI=10.1089/dna.1990.9.657;
RA   Su P., Rennert H., Shayiq R.M., Yamamoto R., Zheng Y.-M., Addya S.,
RA   Strauss J.F. III, Avadhani N.G.;
RT   "A cDNA encoding a rat mitochondrial cytochrome P450 catalyzing both the
RT   26-hydroxylation of cholesterol and 25-hydroxylation of vitamin D3:
RT   gonadotropic regulation of the cognate mRNA in ovaries.";
RL   DNA Cell Biol. 9:657-667(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Liver;
RX   PubMed=1733943; DOI=10.1016/s0021-9258(18)45896-6;
RA   Shayiq R.M., Avadhani N.G.;
RT   "Sequence complementarity between the 5'-terminal regions of mRNAs for rat
RT   mitochondrial cytochrome P-450c27/25 and a growth hormone-inducible serine
RT   protease inhibitor. A possible gene overlap.";
RL   J. Biol. Chem. 267:2421-2428(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7577965; DOI=10.1021/bi00042a003;
RA   Mullick J., Addya S., Sucharov C., Avadhani N.G.;
RT   "Localization of a transcription promoter within the second exon of the
RT   cytochrome P-450c27/25 gene for the expression of the major species of two-
RT   kilobase mRNA.";
RL   Biochemistry 34:13729-13742(1995).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   SUBCELLULAR LOCATION, INTERACTION WITH HSP70, AND TOPOLOGY.
RX   PubMed=19401463; DOI=10.1074/jbc.m109.007492;
RA   Anandatheerthavarada H.K., Sepuri N.B., Avadhani N.G.;
RT   "Mitochondrial targeting of cytochrome P450 proteins containing NH2-
RT   terminal chimeric signals involves an unusual TOM20/TOM22 bypass
RT   mechanism.";
RL   J. Biol. Chem. 284:17352-17363(2009).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase that catalyzes regio- and
CC       stereospecific hydroxylation of cholesterol and its derivatives.
CC       Hydroxylates (with R stereochemistry) the terminal methyl group of
CC       cholesterol side-chain in a three step reaction to yield at first a C26
CC       alcohol, then a C26 aldehyde and finally a C26 acid. Regulates
CC       cholesterol homeostasis by catalyzing the conversion of excess
CC       cholesterol to bile acids via both the 'neutral' (classic) and the
CC       'acid' (alternative) pathways. May also regulate cholesterol
CC       homeostasis via generation of active oxysterols, which act as ligands
CC       for NR1H2 and NR1H3 nuclear receptors, modulating the transcription of
CC       genes involved in lipid metabolism. Catalyzes the conversion of 7-
CC       ketocholesterol (7-oxocholesterol) into 7-keto,27-hydroxycholesterol, a
CC       precursor of 7-keto,27-hydroxycholesterol, an active oxysterol that
CC       activates smoothened (SMO) and the smoothened signaling pathway. Plays
CC       a role in cholestanol metabolism in the cerebellum. Similarly to
CC       cholesterol, hydroxylates cholestanol and may facilitate sterol
CC       diffusion through the blood-brain barrier to the systemic circulation
CC       for further degradation. Also hydroxylates retinal 7-ketocholesterol, a
CC       noxious oxysterol with pro-inflammatory and pro-apoptotic effects, and
CC       may play a role in its elimination from the retinal pigment epithelium.
CC       May play a redundant role in vitamin D biosynthesis (By similarity).
CC       Catalyzes 25-hydroxylation of vitamin D3 that is required for its
CC       conversion to a functionally active form (PubMed:2175615).
CC       {ECO:0000250|UniProtKB:Q02318, ECO:0000250|UniProtKB:Q9DBG1,
CC       ECO:0000269|PubMed:2175615}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5beta-cholestane-3alpha,7alpha,12alpha-triol + 6 reduced
CC         [adrenodoxin] + 3 O2 + 5 H(+) = (25R)-3alpha,7alpha,12alpha-
CC         trihydroxy-5beta-cholestan-26-oate + 6 oxidized [adrenodoxin] + 4
CC         H2O; Xref=Rhea:RHEA:34631, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16496, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC         ChEBI:CHEBI:58734; EC=1.14.15.15;
CC         Evidence={ECO:0000250|UniProtKB:P17177,
CC         ECO:0000250|UniProtKB:Q02318};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34632;
CC         Evidence={ECO:0000250|UniProtKB:Q02318};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cholestanol + 2 reduced [adrenodoxin] + O2 + 2 H(+) = (25R)-
CC         26-hydroxycholestanol + 2 oxidized [adrenodoxin] + H2O;
CC         Xref=Rhea:RHEA:53812, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:86570,
CC         ChEBI:CHEBI:137688; Evidence={ECO:0000250|UniProtKB:Q02318};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53813;
CC         Evidence={ECO:0000250|UniProtKB:Q02318};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(25R)-3beta-hydroxycholest-5-en-7-one-26-al + 2 reduced
CC         [adrenodoxin] + O2 + H(+) = (25R)-3beta-hydroxycholest-5-en-7-one-26-
CC         oate + 2 oxidized [adrenodoxin] + H2O; Xref=Rhea:RHEA:47380,
CC         Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737,
CC         ChEBI:CHEBI:33738, ChEBI:CHEBI:87677, ChEBI:CHEBI:87678;
CC         Evidence={ECO:0000250|UniProtKB:Q02318};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47381;
CC         Evidence={ECO:0000250|UniProtKB:Q02318};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(25R)-3beta,26-dihydroxycholest-5-en-7-one + 2 reduced
CC         [adrenodoxin] + O2 + 2 H(+) = (25R)-3beta-hydroxycholest-5-en-7-one-
CC         26-al + 2 oxidized [adrenodoxin] + 2 H2O; Xref=Rhea:RHEA:47376,
CC         Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737,
CC         ChEBI:CHEBI:33738, ChEBI:CHEBI:87653, ChEBI:CHEBI:87677;
CC         Evidence={ECO:0000250|UniProtKB:Q02318};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47377;
CC         Evidence={ECO:0000250|UniProtKB:Q02318};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-oxocholesterol + 2 reduced [adrenodoxin] + O2 + 2 H(+) =
CC         (25R)-3beta,26-dihydroxycholest-5-en-7-one + 2 oxidized [adrenodoxin]
CC         + H2O; Xref=Rhea:RHEA:47344, Rhea:RHEA-COMP:9998, Rhea:RHEA-
CC         COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:64294,
CC         ChEBI:CHEBI:87653; Evidence={ECO:0000250|UniProtKB:Q02318};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47345;
CC         Evidence={ECO:0000250|UniProtKB:Q02318};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=calciol + 2 reduced [adrenodoxin] + O2 + 2 H(+) = calcidiol +
CC         2 oxidized [adrenodoxin] + H2O; Xref=Rhea:RHEA:46588, Rhea:RHEA-
CC         COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:17933, ChEBI:CHEBI:28940,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738;
CC         Evidence={ECO:0000269|PubMed:2175615};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46589;
CC         Evidence={ECO:0000305};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetrol + 2
CC         reduced [adrenodoxin] + O2 + 2 H(+) = (25R)-3alpha,7alpha,12alpha-
CC         trihydroxy-5beta-cholestan-26-al + 2 oxidized [adrenodoxin] + 2 H2O;
CC         Xref=Rhea:RHEA:40231, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:48939,
CC         ChEBI:CHEBI:48940; Evidence={ECO:0000250|UniProtKB:Q02318};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40232;
CC         Evidence={ECO:0000250|UniProtKB:Q02318};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 reduced [adrenodoxin] + cholesterol + O2 + 2 H(+) = (25R)-
CC         cholest-5-ene-3beta,26-diol + 2 oxidized [adrenodoxin] + H2O;
CC         Xref=Rhea:RHEA:46400, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16113, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC         ChEBI:CHEBI:76591; Evidence={ECO:0000269|PubMed:2175615};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46401;
CC         Evidence={ECO:0000305};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(25R)-3beta,4beta-dihydroxycholest-5-en-26-al + 2 reduced
CC         [adrenodoxin] + O2 + H(+) = (25R)-3beta,4beta-dihydroxycholest-5-en-
CC         26-oate + 2 oxidized [adrenodoxin] + H2O; Xref=Rhea:RHEA:46436,
CC         Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737,
CC         ChEBI:CHEBI:33738, ChEBI:CHEBI:86115, ChEBI:CHEBI:86116;
CC         Evidence={ECO:0000250|UniProtKB:Q02318};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46437;
CC         Evidence={ECO:0000250|UniProtKB:Q02318};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(25R)-4beta,26-dihydroxycholesterol + 2 reduced [adrenodoxin]
CC         + O2 + 2 H(+) = (25R)-3beta,4beta-dihydroxycholest-5-en-26-al + 2
CC         oxidized [adrenodoxin] + 2 H2O; Xref=Rhea:RHEA:46432, Rhea:RHEA-
CC         COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC         ChEBI:CHEBI:86113, ChEBI:CHEBI:86115;
CC         Evidence={ECO:0000250|UniProtKB:Q02318};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46433;
CC         Evidence={ECO:0000250|UniProtKB:Q02318};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4beta-hydroxycholesterol + 2 reduced [adrenodoxin] + O2 + 2
CC         H(+) = (25R)-4beta,26-dihydroxycholesterol + 2 oxidized [adrenodoxin]
CC         + H2O; Xref=Rhea:RHEA:46428, Rhea:RHEA-COMP:9998, Rhea:RHEA-
CC         COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:85778,
CC         ChEBI:CHEBI:86113; Evidence={ECO:0000250|UniProtKB:Q02318};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46429;
CC         Evidence={ECO:0000250|UniProtKB:Q02318};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(25R)-3beta-hydroxy-5-cholesten-26-al + 2 reduced
CC         [adrenodoxin] + O2 + H(+) = (25R)-3beta-hydroxy-5-cholestenoate + 2
CC         oxidized [adrenodoxin] + H2O; Xref=Rhea:RHEA:45236, Rhea:RHEA-
CC         COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC         ChEBI:CHEBI:86096, ChEBI:CHEBI:86098;
CC         Evidence={ECO:0000250|UniProtKB:Q02318};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45237;
CC         Evidence={ECO:0000250|UniProtKB:Q02318};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(25R)-cholest-5-ene-3beta,26-diol + 2 reduced [adrenodoxin] +
CC         O2 + 2 H(+) = (25R)-3beta-hydroxy-5-cholesten-26-al + 2 oxidized
CC         [adrenodoxin] + 2 H2O; Xref=Rhea:RHEA:46092, Rhea:RHEA-COMP:9998,
CC         Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC         ChEBI:CHEBI:76591, ChEBI:CHEBI:86096;
CC         Evidence={ECO:0000250|UniProtKB:Q02318};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46093;
CC         Evidence={ECO:0000250|UniProtKB:Q02318};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al +
CC         2 reduced [adrenodoxin] + O2 + H(+) = (25R)-3alpha,7alpha,12alpha-
CC         trihydroxy-5beta-cholestan-26-oate + 2 oxidized [adrenodoxin] + H2O;
CC         Xref=Rhea:RHEA:34627, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:48940,
CC         ChEBI:CHEBI:58734; Evidence={ECO:0000250|UniProtKB:Q02318};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34628;
CC         Evidence={ECO:0000250|UniProtKB:Q02318};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5beta-cholestane-3alpha,7alpha,12alpha-triol + 2 reduced
CC         [adrenodoxin] + O2 + 2 H(+) = (25R)-5beta-cholestane-
CC         3alpha,7alpha,12alpha,26-tetrol + 2 oxidized [adrenodoxin] + H2O;
CC         Xref=Rhea:RHEA:14373, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16496, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC         ChEBI:CHEBI:48939; Evidence={ECO:0000250|UniProtKB:Q02318};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14374;
CC         Evidence={ECO:0000250|UniProtKB:Q02318};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P17177};
CC   -!- PATHWAY: Hormone biosynthesis; cholecalciferol biosynthesis.
CC       {ECO:0000250|UniProtKB:Q02318}.
CC   -!- PATHWAY: Steroid metabolism; cholesterol degradation.
CC       {ECO:0000250|UniProtKB:Q02318}.
CC   -!- PATHWAY: Lipid metabolism; bile acid biosynthesis.
CC       {ECO:0000250|UniProtKB:Q02318}.
CC   -!- SUBUNIT: Interacts with HSP70; this interaction is required for initial
CC       targeting to mitochondria. {ECO:0000269|PubMed:19401463}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000305|PubMed:19401463}; Peripheral membrane protein
CC       {ECO:0000305|PubMed:19401463}. Note=Post-translationally targeted to
CC       mitochondria. All three of the receptor proteins in the TOM complex,
CC       TOMM70, TOMM20 and TOMM22 are required for the translocation across the
CC       mitochondrial outer membrane. After translocation into the matrix,
CC       associates with the inner membrane as a membrane extrinsic protein.
CC       {ECO:0000305|PubMed:19401463}.
CC   -!- TISSUE SPECIFICITY: Expressed in liver, kidney and ovary.
CC       {ECO:0000269|PubMed:1733943, ECO:0000269|PubMed:2175615}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA86314.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; Y07534; CAA68822.1; -; Genomic_DNA.
DR   EMBL; M38566; AAB02287.1; -; mRNA.
DR   EMBL; M73231; AAA41786.1; -; mRNA.
DR   EMBL; U17375; AAA86314.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U17363; AAA86314.1; JOINED; Genomic_DNA.
DR   EMBL; U17369; AAA86314.1; JOINED; Genomic_DNA.
DR   EMBL; U17370; AAA86314.1; JOINED; Genomic_DNA.
DR   EMBL; U17371; AAA86314.1; JOINED; Genomic_DNA.
DR   EMBL; U17372; AAA86314.1; JOINED; Genomic_DNA.
DR   EMBL; U17373; AAA86314.1; JOINED; Genomic_DNA.
DR   EMBL; U17374; AAA86314.1; JOINED; Genomic_DNA.
DR   EMBL; U17376; AAA86314.1; JOINED; Genomic_DNA.
DR   EMBL; BC061848; AAH61848.1; -; mRNA.
DR   PIR; B42324; B42324.
DR   PIR; S09198; O4RTV3.
DR   RefSeq; NP_849178.2; NM_178847.3.
DR   AlphaFoldDB; P17178; -.
DR   SMR; P17178; -.
DR   BioGRID; 256990; 1.
DR   FunCoup; P17178; 242.
DR   STRING; 10116.ENSRNOP00000023152; -.
DR   PhosphoSitePlus; P17178; -.
DR   PaxDb; 10116-ENSRNOP00000023152; -.
DR   GeneID; 301517; -.
DR   KEGG; rno:301517; -.
DR   UCSC; RGD:727915; rat.
DR   AGR; RGD:727915; -.
DR   CTD; 1593; -.
DR   RGD; 727915; Cyp27a1.
DR   eggNOG; KOG0159; Eukaryota.
DR   HOGENOM; CLU_001570_28_3_1; -.
DR   InParanoid; P17178; -.
DR   OMA; ACPWSSP; -.
DR   OrthoDB; 39818at9989; -.
DR   PhylomeDB; P17178; -.
DR   BioCyc; MetaCyc:MONOMER-14308; -.
DR   BRENDA; 1.14.15.15; 5301.
DR   Reactome; R-RNO-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR   Reactome; R-RNO-193775; Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
DR   Reactome; R-RNO-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
DR   Reactome; R-RNO-211976; Endogenous sterols.
DR   SABIO-RK; P17178; -.
DR   UniPathway; UPA00221; -.
DR   UniPathway; UPA00955; -.
DR   UniPathway; UPA01058; -.
DR   PRO; PR:P17178; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0047748; F:cholestanetetraol 26-dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0031073; F:cholesterol 26-hydroxylase activity; IDA:RGD.
DR   GO; GO:0008123; F:cholesterol 7-alpha-monooxygenase activity; ISS:UniProtKB.
DR   GO; GO:0008386; F:cholesterol monooxygenase (side-chain-cleaving) activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR   GO; GO:0030544; F:Hsp70 protein binding; IDA:UniProtKB.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016716; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, another compound as one donor, and incorporation of one atom of oxygen; ISO:RGD.
DR   GO; GO:0030343; F:vitamin D 25-hydroxylase activity; IDA:RGD.
DR   GO; GO:0006699; P:bile acid biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0008206; P:bile acid metabolic process; ISO:RGD.
DR   GO; GO:0006700; P:C21-steroid hormone biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006707; P:cholesterol catabolic process; ISS:UniProtKB.
DR   GO; GO:0008203; P:cholesterol metabolic process; IDA:RGD.
DR   GO; GO:0045880; P:positive regulation of smoothened signaling pathway; ISO:RGD.
DR   GO; GO:0006706; P:steroid catabolic process; TAS:RGD.
DR   GO; GO:1901755; P:vitamin D3 biosynthetic process; ISO:RGD.
DR   FunFam; 1.10.630.10:FF:000006; Cytochrome P450 302a1, mitochondrial; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR050479; CYP11_CYP27_families.
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; CYTOCHROME P450; 1.
DR   PANTHER; PTHR24279:SF123; CYTOCHROME P450 FAMILY 27 SUBFAMILY A MEMBER 1; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cholesterol metabolism; Direct protein sequencing; Heme; Iron;
KW   Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
KW   Mitochondrion; Mitochondrion inner membrane; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW   Sterol metabolism; Transit peptide.
FT   TRANSIT         1..32
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:2318307"
FT   CHAIN           33..533
FT                   /note="Sterol 26-hydroxylase, mitochondrial"
FT                   /id="PRO_0000003621"
FT   REGION          38..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          386..400
FT                   /note="Sterol-binding"
FT                   /evidence="ECO:0000255"
FT   BINDING         479
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   MOD_RES         142
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DBG1"
FT   MOD_RES         375
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DBG1"
FT   MOD_RES         512
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DBG1"
FT   MOD_RES         523
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DBG1"
FT   CONFLICT        88..96
FT                   /note="Missing (in Ref. 4; AAA86314)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        167..168
FT                   /note="ML -> IV (in Ref. 3; AAA41786 and 4; AAA86314)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        209
FT                   /note="H -> N (in Ref. 3; AAA41786 and 4; AAA86314)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        358
FT                   /note="E -> H (in Ref. 4; AAA86314)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        364
FT                   /note="Missing (in Ref. 4; AAA86314)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        393
FT                   /note="K -> P (in Ref. 4; AAA86314)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        431
FT                   /note="H -> T (in Ref. 2; AAB02287)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   533 AA;  60733 MW;  DC9153BEB6471D63 CRC64;
     MAVLSRMRLR WALLDTRVMG HGLCPQGARA KAAIPAALRD HESTEGPGTG QDRPRLRSLA
     ELPGPGTLRF LFQLFLRGYV LHLHELQALN KAKYGPMWTT TFGTRTNVNL ASAPLLEQVM
     RQEGKYPIRD SMEQWKEHRD HKGLSYGIFI TQGQQWYHLR HSLNQRMLKP AEAALYTDAL
     NEVISDFIAR LDQVRTESAS GDQVPDVAHL LYHLALEAIC YILFEKRVGC LEPSIPEDTA
     TFIRSVGLMF KNSVYVTFLP KWSRPLLPFW KRYMNNWDNI FSFGEKMIHQ KVQEIEAQLQ
     AAGPDGVQVS GYLHFLLTKE LLSPQETVGT FPELILAGVD TTSNTLTWAL YHLSKNPEIQ
     EALHKEVTGV VPFGKVPQNK DFAHMPLLKA VIKETLRLYP VVPTNSRIIT EKETEINGFL
     FPKNTQFVLC HYVVSRDPSV FPEPESFQPH RWLRKREDDN SGIQHPFGSV PFGYGVRSCL
     GRRIAELEMQ LLLSRLIQKY EVVLSPGMGE VKSVSRIVLV PSKKVSLRFL QRQ
//