ID   CP24A_RAT               Reviewed;         514 AA.
AC   Q09128; Q498V4; Q63685;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 156.
DE   RecName: Full=1,25-dihydroxyvitamin D(3) 24-hydroxylase, mitochondrial;
DE            Short=24-OHase;
DE            Short=Vitamin D(3) 24-hydroxylase;
DE            EC=1.14.15.16 {ECO:0000269|PubMed:2026586};
DE   AltName: Full=Cytochrome P450 24A1;
DE   AltName: Full=Cytochrome P450-CC24;
DE   Flags: Precursor;
GN   Name=Cyp24a1; Synonyms=Cyp24;
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 [MRNA], AND PROTEIN SEQUENCE OF 36-43.
RC   TISSUE=Kidney;
RX   PubMed=1991512; DOI=10.1016/0014-5793(91)80115-j;
RA   Ohyama Y., Noshiro M., Okuda K.;
RT   "Cloning and expression of cDNA encoding 25-hydroxyvitamin D3 24-
RT   hydroxylase.";
RL   FEBS Lett. 278:195-198(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8418863; DOI=10.1021/bi00052a011;
RA   Ohyama Y., Noshiro M., Eggertsen G., Gotoh O., Kato Y., Bjoerkhem I.,
RA   Okuda K.;
RT   "Structural characterization of the gene encoding rat 25-hydroxyvitamin D3
RT   24-hydroxylase.";
RL   Biochemistry 32:76-82(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-86.
RX   PubMed=8036172; DOI=10.1093/nar/22.12.2410;
RA   Hahn C.N., Kerry D.M., Omdahl J.L., May B.K.;
RT   "Identification of a vitamin D responsive element in the promoter of the
RT   rat cytochrome P450(24) gene.";
RL   Nucleic Acids Res. 22:2410-2416(1994).
RN   [5]
RP   PROTEIN SEQUENCE OF 36-43, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP   SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RX   PubMed=2026586; DOI=10.1016/s0021-9258(18)31501-1;
RA   Ohyama Y., Okuda K.;
RT   "Isolation and characterization of a cytochrome P-450 from rat kidney
RT   mitochondria that catalyzes the 24-hydroxylation of 25-hydroxyvitamin D3.";
RL   J. Biol. Chem. 266:8690-8695(1991).
RN   [6]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=10231362; DOI=10.1046/j.1432-1327.1999.00375.x;
RA   Sakaki T., Sawada N., Nonaka Y., Ohyama Y., Inouye K.;
RT   "Metabolic studies using recombinant escherichia coli cells producing rat
RT   mitochondrial CYP24 CYP24 can convert 1alpha,25-dihydroxyvitamin D3 to
RT   calcitroic acid.";
RL   Eur. J. Biochem. 262:43-48(1999).
RN   [7]
RP   SUBSTRATE SPECIFICITY.
RX   PubMed=15574355; DOI=10.2741/1514;
RA   Sakaki T., Kagawa N., Yamamoto K., Inouye K.;
RT   "Metabolism of vitamin D3 by cytochromes P450.";
RL   Front. Biosci. 10:119-134(2005).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   MUTAGENESIS OF THR-416 AND ILE-500.
RX   PubMed=16617161; DOI=10.1124/mol.106.023275;
RA   Hamamoto H., Kusudo T., Urushino N., Masuno H., Yamamoto K., Yamada S.,
RA   Kamakura M., Ohta M., Inouye K., Sakaki T.;
RT   "Structure-function analysis of vitamin D 24-hydroxylase (CYP24A1) by site-
RT   directed mutagenesis: amino acid residues responsible for species-based
RT   difference of CYP24A1 between humans and rats.";
RL   Mol. Pharmacol. 70:120-128(2006).
RN   [9]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=25727742; DOI=10.1016/j.jsbmb.2015.02.010;
RA   Tieu E.W., Li W., Chen J., Kim T.K., Ma D., Slominski A.T., Tuckey R.C.;
RT   "Metabolism of 20-hydroxyvitamin D3 and 20,23-dihydroxyvitamin D3 by rat
RT   and human CYP24A1.";
RL   J. Steroid Biochem. Mol. Biol. 149:153-165(2015).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 34-514 IN COMPLEX WITH HEME, AND
RP   COFACTOR.
RX   PubMed=19961857; DOI=10.1016/j.jmb.2009.11.057;
RA   Annalora A.J., Goodin D.B., Hong W.X., Zhang Q., Johnson E.F., Stout C.D.;
RT   "Crystal structure of CYP24A1, a mitochondrial cytochrome P450 involved in
RT   vitamin D metabolism.";
RL   J. Mol. Biol. 396:441-451(2010).
CC   -!- FUNCTION: A cytochrome P450 monooxygenase with a key role in vitamin D
CC       catabolism and calcium homeostasis. Via C24-oxidation pathway,
CC       catalyzes the inactivation of both the vitamin D precursor calcidiol
CC       (25-hydroxyvitamin D(3)) and the active hormone calcitriol (1-alpha,25-
CC       dihydroxyvitamin D(3)) (PubMed:2026586, PubMed:16617161,
CC       PubMed:10231362). With initial hydroxylation at C-24 (via C24-oxidation
CC       pathway), performs a sequential 6-step oxidation of calcitriol leading
CC       to the formation of the biliary metabolite calcitroic acid
CC       (PubMed:10231362, PubMed:16617161). Hydroxylates at C-24 or C-25 other
CC       vitamin D active metabolites, such as CYP11A1-derived secosteroids 20S-
CC       hydroxycholecalciferol and 20S,23-dihydroxycholecalciferol
CC       (PubMed:25727742). Mechanistically, uses molecular oxygen inserting one
CC       oxygen atom into a substrate, and reducing the second into a water
CC       molecule, with two electrons provided by NADPH via FDXR/adrenodoxin
CC       reductase and FDX1/adrenodoxin (PubMed:2026586).
CC       {ECO:0000269|PubMed:10231362, ECO:0000269|PubMed:16617161,
CC       ECO:0000269|PubMed:2026586, ECO:0000269|PubMed:25727742}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=calcitriol + 2 H(+) + O2 + 2 reduced [adrenodoxin] =
CC         calcitetrol + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:24964,
CC         Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17823,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:47799;
CC         EC=1.14.15.16; Evidence={ECO:0000269|PubMed:10231362,
CC         ECO:0000269|PubMed:16617161, ECO:0000269|PubMed:2026586};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24965;
CC         Evidence={ECO:0000305|PubMed:2026586};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=calcitetrol + 2 H(+) + O2 + 2 reduced [adrenodoxin] =
CC         (1S)-1,25-dihydroxy-24-oxocalciol + 2 H2O + 2 oxidized [adrenodoxin];
CC         Xref=Rhea:RHEA:24972, 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:47799,
CC         ChEBI:CHEBI:47812; EC=1.14.15.16;
CC         Evidence={ECO:0000269|PubMed:10231362, ECO:0000269|PubMed:16617161};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24973;
CC         Evidence={ECO:0000305|PubMed:16617161};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(1S)-1,25-dihydroxy-24-oxocalciol + 2 H(+) + O2 + 2 reduced
CC         [adrenodoxin] = (1S)-1,23,25-trihydroxy-24-oxocalciol + H2O + 2
CC         oxidized [adrenodoxin]; Xref=Rhea:RHEA:24976, 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:47812, ChEBI:CHEBI:47813; EC=1.14.15.16;
CC         Evidence={ECO:0000269|PubMed:10231362, ECO:0000269|PubMed:16617161};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24977;
CC         Evidence={ECO:0000305|PubMed:16617161};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(1S)-1,23-dihydroxy-24,25,26,27-tetranorcalciol + 2 H(+) + O2
CC         + 2 reduced [adrenodoxin] = (1S)-1-hydroxy-23-oxo-24,25,26,27-
CC         tetranorcalciol + 2 H2O + 2 oxidized [adrenodoxin];
CC         Xref=Rhea:RHEA:24984, 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:47818,
CC         ChEBI:CHEBI:47820; EC=1.14.15.16;
CC         Evidence={ECO:0000269|PubMed:10231362};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24985;
CC         Evidence={ECO:0000305|PubMed:10231362};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(1S)-1-hydroxy-23-oxo-24,25,26,27-tetranorcalciol + H(+) + O2
CC         + 2 reduced [adrenodoxin] = calcitroate + H2O + 2 oxidized
CC         [adrenodoxin]; Xref=Rhea:RHEA:24988, 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:47820,
CC         ChEBI:CHEBI:58715; EC=1.14.15.16;
CC         Evidence={ECO:0000269|PubMed:10231362};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24989;
CC         Evidence={ECO:0000305|PubMed:10231362};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=calcidiol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = H2O + 2
CC         oxidized [adrenodoxin] + secalciferol; Xref=Rhea:RHEA:24968,
CC         Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17933,
CC         ChEBI:CHEBI:28818, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738;
CC         EC=1.14.15.16; Evidence={ECO:0000269|PubMed:10231362,
CC         ECO:0000269|PubMed:2026586};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24969;
CC         Evidence={ECO:0000305|PubMed:2026586};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + O2 + 2 reduced [adrenodoxin] + secalciferol = 25-
CC         hydroxy-24-oxocalciol + 2 H2O + 2 oxidized [adrenodoxin];
CC         Xref=Rhea:RHEA:49196, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:28818, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC         ChEBI:CHEBI:47805; Evidence={ECO:0000269|PubMed:10231362};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49197;
CC         Evidence={ECO:0000305|PubMed:10231362};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=25-hydroxy-24-oxocalciol + 2 H(+) + O2 + 2 reduced
CC         [adrenodoxin] = 23S,25-dihydroxy-24-oxocholecalciferol + H2O + 2
CC         oxidized [adrenodoxin]; Xref=Rhea:RHEA:49268, 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:47805, ChEBI:CHEBI:90980;
CC         Evidence={ECO:0000269|PubMed:10231362};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49269;
CC         Evidence={ECO:0000305|PubMed:10231362};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=20S,23-dihydroxycholecalciferol + 2 H(+) + O2 + 2 reduced
CC         [adrenodoxin] = 20S,23,25-trihydroxycholecalciferol + H2O + 2
CC         oxidized [adrenodoxin]; Xref=Rhea:RHEA:49396, 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:91306, ChEBI:CHEBI:91308;
CC         Evidence={ECO:0000269|PubMed:25727742};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49397;
CC         Evidence={ECO:0000305|PubMed:25727742};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=20S,23-dihydroxycholecalciferol + 2 H(+) + O2 + 2 reduced
CC         [adrenodoxin] = 20S,23,24-trihydroxycholecalciferol + H2O + 2
CC         oxidized [adrenodoxin]; Xref=Rhea:RHEA:49392, 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:91306, ChEBI:CHEBI:91307;
CC         Evidence={ECO:0000269|PubMed:25727742};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49393;
CC         Evidence={ECO:0000305|PubMed:25727742};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=20S-hydroxycholecalciferol + 2 H(+) + O2 + 2 reduced
CC         [adrenodoxin] = 20S,25-dihydroxycholecalciferol + H2O + 2 oxidized
CC         [adrenodoxin]; Xref=Rhea:RHEA:49212, 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:90983,
CC         ChEBI:CHEBI:90984; Evidence={ECO:0000269|PubMed:25727742};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49213;
CC         Evidence={ECO:0000305|PubMed:25727742};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=20S-hydroxycholecalciferol + 2 H(+) + O2 + 2 reduced
CC         [adrenodoxin] = 20S,24S-dihydroxycholecalciferol + H2O + 2 oxidized
CC         [adrenodoxin]; Xref=Rhea:RHEA:49208, 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:90983,
CC         ChEBI:CHEBI:90986; Evidence={ECO:0000269|PubMed:25727742};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49209;
CC         Evidence={ECO:0000305|PubMed:25727742};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=20S-hydroxycholecalciferol + 2 H(+) + O2 + 2 reduced
CC         [adrenodoxin] = 20S,24R-dihydroxycholecalciferol + H2O + 2 oxidized
CC         [adrenodoxin]; Xref=Rhea:RHEA:49204, 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:90983,
CC         ChEBI:CHEBI:90985; Evidence={ECO:0000269|PubMed:25727742};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49205;
CC         Evidence={ECO:0000305|PubMed:25727742};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000269|PubMed:19961857};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.8 uM for calcidiol {ECO:0000269|PubMed:2026586};
CC         KM=0.19 uM for calcitriol {ECO:0000269|PubMed:16617161};
CC       pH dependence:
CC         Optimum pH is 7.7. {ECO:0000269|PubMed:2026586};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:2026586}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; X59506; CAA42093.1; -; mRNA.
DR   EMBL; L04618; AAA42340.1; -; Genomic_DNA.
DR   EMBL; L04608; AAA42340.1; JOINED; Genomic_DNA.
DR   EMBL; L04609; AAA42340.1; JOINED; Genomic_DNA.
DR   EMBL; L04610; AAA42340.1; JOINED; Genomic_DNA.
DR   EMBL; L04611; AAA42340.1; JOINED; Genomic_DNA.
DR   EMBL; L04612; AAA42340.1; JOINED; Genomic_DNA.
DR   EMBL; L04613; AAA42340.1; JOINED; Genomic_DNA.
DR   EMBL; L04614; AAA42340.1; JOINED; Genomic_DNA.
DR   EMBL; L04615; AAA42340.1; JOINED; Genomic_DNA.
DR   EMBL; L04616; AAA42340.1; JOINED; Genomic_DNA.
DR   EMBL; L04617; AAA42340.1; JOINED; Genomic_DNA.
DR   EMBL; BC100059; AAI00060.1; -; mRNA.
DR   EMBL; Z28351; CAA82206.1; -; Genomic_DNA.
DR   PIR; A45228; A45228.
DR   RefSeq; NP_963966.1; NM_201635.3.
DR   PDB; 3K9V; X-ray; 2.50 A; A/B=34-514.
DR   PDB; 3K9Y; X-ray; 2.80 A; A/B=34-514.
DR   PDBsum; 3K9V; -.
DR   PDBsum; 3K9Y; -.
DR   AlphaFoldDB; Q09128; -.
DR   SMR; Q09128; -.
DR   STRING; 10116.ENSRNOP00000043298; -.
DR   BindingDB; Q09128; -.
DR   ChEMBL; CHEMBL3748; -.
DR   DrugCentral; Q09128; -.
DR   SwissLipids; SLP:000001482; -.
DR   PhosphoSitePlus; Q09128; -.
DR   PaxDb; 10116-ENSRNOP00000043298; -.
DR   Ensembl; ENSRNOT00000046011.3; ENSRNOP00000043298.2; ENSRNOG00000013062.6.
DR   GeneID; 25279; -.
DR   KEGG; rno:25279; -.
DR   AGR; RGD:2462; -.
DR   CTD; 1591; -.
DR   RGD; 2462; Cyp24a1.
DR   eggNOG; KOG0159; Eukaryota.
DR   GeneTree; ENSGT00950000182905; -.
DR   HOGENOM; CLU_001570_28_1_1; -.
DR   InParanoid; Q09128; -.
DR   OMA; VLMINTH; -.
DR   OrthoDB; 2658719at2759; -.
DR   PhylomeDB; Q09128; -.
DR   TreeFam; TF105094; -.
DR   BioCyc; MetaCyc:MONOMER-14357; -.
DR   BRENDA; 1.14.15.16; 5301.
DR   Reactome; R-RNO-196791; Vitamin D (calciferol) metabolism.
DR   Reactome; R-RNO-211916; Vitamins.
DR   SABIO-RK; Q09128; -.
DR   EvolutionaryTrace; Q09128; -.
DR   PRO; PR:Q09128; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000013062; Expressed in kidney and 2 other cell types or tissues.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0062181; F:1-alpha,25-dihydroxyvitamin D3 23-hydroxylase activity; ISO:RGD.
DR   GO; GO:0030342; F:1-alpha,25-dihydroxyvitamin D3 24-hydroxylase activity; IDA:UniProtKB.
DR   GO; GO:0062180; F:25-hydroxycholecalciferol-23-hydroxylase activity; ISO:RGD.
DR   GO; GO:0008403; F:25-hydroxycholecalciferol-24-hydroxylase activity; IDA:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0070576; F:vitamin D 24-hydroxylase activity; IDA:UniProtKB.
DR   GO; GO:0070643; F:vitamin D 25-hydroxylase activity; IDA:UniProtKB.
DR   GO; GO:0071305; P:cellular response to vitamin D; IEP:RGD.
DR   GO; GO:0001649; P:osteoblast differentiation; ISO:RGD.
DR   GO; GO:0033280; P:response to vitamin D; ISO:RGD.
DR   GO; GO:0042369; P:vitamin D catabolic process; IDA:UniProtKB.
DR   GO; GO:0042359; P:vitamin D metabolic process; IDA:RGD.
DR   CDD; cd20645; CYP24A1; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002949; Cyt_P450_E_CYP24A_mit.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24279; -; 1.
DR   PANTHER; PTHR24279:SF120; CYTOCHROME P450 FAMILY 24 SUBFAMILY A MEMBER 1; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR01238; MITP450CC24.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Heme; Iron; Lipid metabolism;
KW   Metal-binding; Mitochondrion; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..35
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:1991512,
FT                   ECO:0000269|PubMed:2026586"
FT   CHAIN           36..514
FT                   /note="1,25-dihydroxyvitamin D(3) 24-hydroxylase,
FT                   mitochondrial"
FT                   /id="PRO_0000003617"
FT   BINDING         462
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:0007744|PDB:3K9V, ECO:0007744|PDB:3K9Y"
FT   MUTAGEN         416
FT                   /note="T->F: Increases the C23:C24 hydroxylation ratio from
FT                   0.01 to 0.12."
FT                   /evidence="ECO:0000269|PubMed:16617161"
FT   MUTAGEN         416
FT                   /note="T->I: Increases the C23:C24 hydroxylation ratio from
FT                   0.01 to 0.19."
FT                   /evidence="ECO:0000269|PubMed:16617161"
FT   MUTAGEN         416
FT                   /note="T->M: Increases the C23:C24 hydroxylation ratio from
FT                   0.01 to 0.08."
FT                   /evidence="ECO:0000269|PubMed:16617161"
FT   MUTAGEN         416
FT                   /note="T->V: Increases the C23:C24 hydroxylation ratio from
FT                   0.01 to 0.16."
FT                   /evidence="ECO:0000269|PubMed:16617161"
FT   MUTAGEN         500
FT                   /note="I->A: Increases the C23:C24 hydroxylation ratio from
FT                   0.01 to 0.15."
FT                   /evidence="ECO:0000269|PubMed:16617161"
FT   MUTAGEN         500
FT                   /note="I->T,L: Increases the C23:C24 hydroxylation ratio
FT                   from 0.01 to 0.16."
FT                   /evidence="ECO:0000269|PubMed:16617161"
FT   MUTAGEN         500
FT                   /note="I->V: Increases the C23:C24 hydroxylation ratio from
FT                   0.01 to 0.13."
FT                   /evidence="ECO:0000269|PubMed:16617161"
FT   HELIX           55..57
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   TURN            65..67
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   HELIX           70..75
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   HELIX           79..81
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   HELIX           82..93
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   STRAND          95..101
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   STRAND          104..109
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   HELIX           112..120
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   HELIX           132..141
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   TURN            147..149
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   HELIX           152..166
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   HELIX           169..172
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   HELIX           173..175
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   HELIX           176..193
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   STRAND          196..198
FT                   /evidence="ECO:0007829|PDB:3K9Y"
FT   HELIX           203..220
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   STRAND          226..228
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   HELIX           236..246
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   HELIX           249..252
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   STRAND          253..255
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   HELIX           257..263
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   HELIX           266..292
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   TURN            293..295
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   HELIX           301..308
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   HELIX           313..343
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   HELIX           346..359
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   HELIX           368..373
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   HELIX           375..387
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   STRAND          393..397
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   STRAND          402..404
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   STRAND          407..409
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   STRAND          414..418
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   HELIX           421..424
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   TURN            426..428
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   STRAND          432..434
FT                   /evidence="ECO:0007829|PDB:3K9Y"
FT   HELIX           437..440
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   HELIX           449..451
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   HELIX           465..482
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   STRAND          483..488
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   STRAND          495..506
FT                   /evidence="ECO:0007829|PDB:3K9V"
FT   STRAND          509..513
FT                   /evidence="ECO:0007829|PDB:3K9V"
SQ   SEQUENCE   514 AA;  59448 MW;  2E5CC1CCBA3C2B91 CRC64;
     MSCPIDKRRT LIAFLRRLRD LGQPPRSVTS KASASRAPKE VPLCPLMTDG ETRNVTSLPG
     PTNWPLLGSL LEIFWKGGLK KQHDTLAEYH KKYGQIFRMK LGSFDSVHLG SPSLLEALYR
     TESAHPQRLE IKPWKAYRDH RNEAYGLMIL EGQEWQRVRS AFQKKLMKPV EIMKLDKKIN
     EVLADFLERM DELCDERGRI PDLYSELNKW SFESICLVLY EKRFGLLQKE TEEEALTFIT
     AIKTMMSTFG KMMVTPVELH KRLNTKVWQA HTLAWDTIFK SVKPCIDNRL QRYSQQPGAD
     FLCDIYQQDH LSKKELYAAV TELQLAAVET TANSLMWILY NLSRNPQAQR RLLQEVQSVL
     PDNQTPRAED LRNMPYLKAC LKESMRLTPS VPFTTRTLDK PTVLGEYALP KGTVLTLNTQ
     VLGSSEDNFE DSHKFRPERW LQKEKKINPF AHLPFGIGKR MCIGRRLAEL QLHLALCWII
     QKYDIVATDN EPVEMLHLGI LVPSRELPIA FRPR
//