CP27A_RAT
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 03-AUG-2022, entry version 162.
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. Plays a role in cholestanol
CC metabolism in the cerebellum. Similarly to cholesterol, hydroxylates
CC cholestanol and may facilitate sterol diffusion through the blood-brain
CC barrier to the systemic circulation for further degradation. Also
CC hydroxylates retinal 7-ketocholesterol, a noxious oxysterol with pro-
CC inflammatory and pro-apoptotic effects, and may play a role in its
CC elimination from the retinal pigment epithelium. May play a redundant
CC role in vitamin D biosynthesis (By similarity). Catalyzes 25-
CC hydroxylation of vitamin D3 that is required for its conversion to a
CC functionally active form (PubMed:2175615).
CC {ECO:0000250|UniProtKB:Q02318, ECO:0000269|PubMed:2175615}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5beta-cholestane-3alpha,7alpha,12alpha-triol + 5 H(+) + 3 O2 +
CC 6 reduced [adrenodoxin] = (25R)-3alpha,7alpha,12alpha-trihydroxy-
CC 5beta-cholestan-26-oate + 4 H2O + 6 oxidized [adrenodoxin];
CC 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 H(+) + O2 + 2 reduced [adrenodoxin] = (25R)-
CC 26-hydroxycholestanol + H2O + 2 oxidized [adrenodoxin];
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 + H(+) + O2 + 2
CC reduced [adrenodoxin] = (25R)-3beta-hydroxycholest-5-en-7-one-26-oate
CC + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:47380, 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: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 H(+) + O2 + 2
CC reduced [adrenodoxin] = (25R)-3beta-hydroxycholest-5-en-7-one-26-al +
CC 2 H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:47376, 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: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 H(+) + O2 + 2 reduced [adrenodoxin] =
CC (25R)-3beta,26-dihydroxycholest-5-en-7-one + H2O + 2 oxidized
CC [adrenodoxin]; 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 H(+) + O2 + 2 reduced [adrenodoxin] = calcidiol +
CC H2O + 2 oxidized [adrenodoxin]; 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 H(+) + O2 + 2 reduced [adrenodoxin] = (25R)-3alpha,7alpha,12alpha-
CC trihydroxy-5beta-cholestan-26-al + 2 H2O + 2 oxidized [adrenodoxin];
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=cholesterol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = (25R)-
CC cholest-5-ene-3beta,26-diol + H2O + 2 oxidized [adrenodoxin];
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 + H(+) + O2 + 2
CC reduced [adrenodoxin] = (25R)-3beta,4beta-dihydroxycholest-5-en-26-
CC oate + H2O + 2 oxidized [adrenodoxin]; 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 H(+) + O2 + 2 reduced
CC [adrenodoxin] = (25R)-3beta,4beta-dihydroxycholest-5-en-26-al + 2 H2O
CC + 2 oxidized [adrenodoxin]; 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 H(+) + O2 + 2 reduced
CC [adrenodoxin] = (25R)-4beta,26-dihydroxycholesterol + H2O + 2
CC oxidized [adrenodoxin]; Xref=Rhea:RHEA:46428, 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:85778, ChEBI:CHEBI:86113;
CC 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 + H(+) + O2 + 2 reduced
CC [adrenodoxin] = (25R)-3beta-hydroxy-5-cholestenoate + H2O + 2
CC oxidized [adrenodoxin]; Xref=Rhea:RHEA:45236, 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: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 H(+) + O2 + 2 reduced
CC [adrenodoxin] = (25R)-3beta-hydroxy-5-cholesten-26-al + 2 H2O + 2
CC oxidized [adrenodoxin]; 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 H(+) + O2 + 2 reduced [adrenodoxin] = (25R)-3alpha,7alpha,12alpha-
CC trihydroxy-5beta-cholestan-26-oate + H2O + 2 oxidized [adrenodoxin];
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 H(+) + O2 + 2
CC reduced [adrenodoxin] = (25R)-5beta-cholestane-
CC 3alpha,7alpha,12alpha,26-tetrol + H2O + 2 oxidized [adrenodoxin];
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 STRING; 10116.ENSRNOP00000023152; -.
DR PaxDb; P17178; -.
DR PRIDE; P17178; -.
DR GeneID; 301517; -.
DR KEGG; rno:301517; -.
DR UCSC; RGD:727915; rat.
DR CTD; 1593; -.
DR RGD; 727915; Cyp27a1.
DR eggNOG; KOG0159; Eukaryota.
DR HOGENOM; CLU_001570_28_3_1; -.
DR InParanoid; P17178; -.
DR OrthoDB; 871849at2759; -.
DR PhylomeDB; P17178; -.
DR TreeFam; TF105094; -.
DR BioCyc; MetaCyc:MON-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 Genevisible; P17178; RN.
DR GO; GO:0005740; C:mitochondrial envelope; IDA:RGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0047103; F:3-alpha,7-alpha,12-alpha-trihydroxycholestan-26-al 26-oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0047748; F:cholestanetetraol 26-dehydrogenase activity; IEA:RHEA.
DR GO; GO:0047749; F:cholestanetriol 26-monooxygenase 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:0030343; F:vitamin D3 25-hydroxylase activity; IDA:RGD.
DR GO; GO:0006699; P:bile acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006700; P:C21-steroid hormone biosynthetic process; ISS:UniProtKB.
DR GO; GO:0036378; P:calcitriol biosynthetic process from calciol; ISO:RGD.
DR GO; GO:0006707; P:cholesterol catabolic process; ISS:UniProtKB.
DR GO; GO:0008203; P:cholesterol metabolic process; IDA:RGD.
DR GO; GO:0006706; P:steroid catabolic process; TAS:RGD.
DR Gene3D; 1.10.630.10; -; 1.
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 Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 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
