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] = (1S)-
CC 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//
