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1,25-dihydroxyvitamin D(3) 24-hydroxylase, mitochondrial (24-OHase) (Vitamin D(3) 24-hydroxylase) (EC 1 14 15 16) (Cytochrome P450 24A1) (Cytochrome P450-CC24)

 CP24A_MOUSE             Reviewed;         514 AA.
Q64441;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
26-FEB-2020, entry version 149.
RecName: Full=1,25-dihydroxyvitamin D(3) 24-hydroxylase, mitochondrial;
Short=24-OHase;
Short=Vitamin D(3) 24-hydroxylase;
EC=1.14.15.16 {ECO:0000250|UniProtKB:Q09128};
AltName: Full=Cytochrome P450 24A1;
AltName: Full=Cytochrome P450-CC24;
Flags: Precursor;
Name=Cyp24a1 {ECO:0000312|MGI:MGI:88593}; Synonyms=Cyp-24, Cyp24;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J; TISSUE=Kidney;
PubMed=7578252; DOI=10.1016/0167-4781(95)00147-9;
Itoh S., Yoshimura T., Iemura O., Yamada E., Tsujikawa K., Kohama Y.,
Mimura T.;
"Molecular cloning of 25-hydroxyvitamin D-3 24-hydroxylase (Cyp-24) from
mouse kidney: its inducibility by vitamin D-3.";
Biochim. Biophys. Acta 1264:26-28(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=ddY; TISSUE=Kidney;
PubMed=9165006; DOI=10.1210/endo.138.6.5170;
Akeno N., Saikatsu S., Kawane T., Horiuchi N.;
"Mouse vitamin D-24-hydroxylase: molecular cloning, tissue distribution,
and transcriptional regulation by 1alpha,25-dihydroxyvitamin D3.";
Endocrinology 138:2233-2240(1997).
[3]
INDUCTION.
PubMed=14528024; DOI=10.1210/me.2003-0048;
Tsujikawa H., Kurotaki Y., Fujimori T., Fukuda K., Nabeshima Y.;
"Klotho, a gene related to a syndrome resembling human premature aging,
functions in a negative regulatory circuit of vitamin D endocrine system.";
Mol. Endocrinol. 17:2393-2403(2003).
-!- FUNCTION: A cytochrome P450 monooxygenase with a key role in vitamin D
catabolism and calcium homeostasis. Via C24-oxidation pathway,
catalyzes the inactivation of both the vitamin D precursor calcidiol
(25-hydroxyvitamin D(3)) and the active hormone calcitriol (1-alpha,25-
dihydroxyvitamin D(3)). With initial hydroxylation at C-24 (via C24-
oxidation pathway), performs a sequential 6-step oxidation of
calcitriol leading to the formation of the biliary metabolite
calcitroic acid. Hydroxylates at C-24 or C-25 other vitamin D active
metabolites, such as CYP11A1-derived secosteroids 20S-
hydroxycholecalciferol and 20S,23-dihydroxycholecalciferol.
Mechanistically, uses molecular oxygen inserting one oxygen atom into a
substrate, and reducing the second into a water molecule, with two
electrons provided by NADPH via FDXR/adrenodoxin reductase and
FDX1/adrenodoxin. {ECO:0000250|UniProtKB:Q09128}.
-!- CATALYTIC ACTIVITY:
Reaction=calcitriol + 2 H(+) + O2 + 2 reduced [adrenodoxin] =
calcitetrol + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:24964,
Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17823,
ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:47799;
EC=1.14.15.16; Evidence={ECO:0000250|UniProtKB:Q09128};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24965;
Evidence={ECO:0000250|UniProtKB:Q09128};
-!- CATALYTIC ACTIVITY:
Reaction=calcitetrol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = (1S)-
1,25-dihydroxy-24-oxocalciol + 2 H2O + 2 oxidized [adrenodoxin];
Xref=Rhea:RHEA:24972, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:47799,
ChEBI:CHEBI:47812; EC=1.14.15.16;
Evidence={ECO:0000250|UniProtKB:Q09128};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24973;
Evidence={ECO:0000250|UniProtKB:Q09128};
-!- CATALYTIC ACTIVITY:
Reaction=(1S)-1,25-dihydroxy-24-oxocalciol + 2 H(+) + O2 + 2 reduced
[adrenodoxin] = (1S)-1,23,25-trihydroxy-24-oxocalciol + H2O + 2
oxidized [adrenodoxin]; Xref=Rhea:RHEA:24976, Rhea:RHEA-COMP:9998,
Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
ChEBI:CHEBI:47812, ChEBI:CHEBI:47813; EC=1.14.15.16;
Evidence={ECO:0000250|UniProtKB:Q09128};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24977;
Evidence={ECO:0000250|UniProtKB:Q09128};
-!- CATALYTIC ACTIVITY:
Reaction=(1S)-1,23-dihydroxy-24,25,26,27-tetranorcalciol + 2 H(+) + O2
+ 2 reduced [adrenodoxin] = (1S)-1-hydroxy-23-oxo-24,25,26,27-
tetranorcalciol + 2 H2O + 2 oxidized [adrenodoxin];
Xref=Rhea:RHEA:24984, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:47818,
ChEBI:CHEBI:47820; EC=1.14.15.16;
Evidence={ECO:0000250|UniProtKB:Q09128};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24985;
Evidence={ECO:0000250|UniProtKB:Q09128};
-!- CATALYTIC ACTIVITY:
Reaction=(1S)-1-hydroxy-23-oxo-24,25,26,27-tetranorcalciol + H(+) + O2
+ 2 reduced [adrenodoxin] = calcitroate + H2O + 2 oxidized
[adrenodoxin]; Xref=Rhea:RHEA:24988, Rhea:RHEA-COMP:9998, Rhea:RHEA-
COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:47820,
ChEBI:CHEBI:58715; EC=1.14.15.16;
Evidence={ECO:0000250|UniProtKB:Q09128};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24989;
Evidence={ECO:0000250|UniProtKB:Q09128};
-!- CATALYTIC ACTIVITY:
Reaction=calcidiol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = H2O + 2
oxidized [adrenodoxin] + secalciferol; Xref=Rhea:RHEA:24968,
Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17933,
ChEBI:CHEBI:28818, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738;
EC=1.14.15.16; Evidence={ECO:0000250|UniProtKB:Q09128};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24969;
Evidence={ECO:0000250|UniProtKB:Q09128};
-!- CATALYTIC ACTIVITY:
Reaction=2 H(+) + O2 + 2 reduced [adrenodoxin] + secalciferol = 25-
hydroxy-24-oxocalciol + 2 H2O + 2 oxidized [adrenodoxin];
Xref=Rhea:RHEA:49196, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
ChEBI:CHEBI:28818, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
ChEBI:CHEBI:47805; Evidence={ECO:0000250|UniProtKB:Q09128};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49197;
Evidence={ECO:0000250|UniProtKB:Q09128};
-!- CATALYTIC ACTIVITY:
Reaction=25-hydroxy-24-oxocalciol + 2 H(+) + O2 + 2 reduced
[adrenodoxin] = 23S,25-dihydroxy-24-oxocholecalciferol + H2O + 2
oxidized [adrenodoxin]; Xref=Rhea:RHEA:49268, Rhea:RHEA-COMP:9998,
Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
ChEBI:CHEBI:47805, ChEBI:CHEBI:90980;
Evidence={ECO:0000250|UniProtKB:Q09128};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49269;
Evidence={ECO:0000250|UniProtKB:Q09128};
-!- CATALYTIC ACTIVITY:
Reaction=20S,23-dihydroxycholecalciferol + 2 H(+) + O2 + 2 reduced
[adrenodoxin] = 20S,23,25-trihydroxycholecalciferol + H2O + 2
oxidized [adrenodoxin]; Xref=Rhea:RHEA:49396, Rhea:RHEA-COMP:9998,
Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
ChEBI:CHEBI:91306, ChEBI:CHEBI:91308;
Evidence={ECO:0000250|UniProtKB:Q09128};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49397;
Evidence={ECO:0000250|UniProtKB:Q09128};
-!- CATALYTIC ACTIVITY:
Reaction=20S,23-dihydroxycholecalciferol + 2 H(+) + O2 + 2 reduced
[adrenodoxin] = 20S,23,24-trihydroxycholecalciferol + H2O + 2
oxidized [adrenodoxin]; Xref=Rhea:RHEA:49392, Rhea:RHEA-COMP:9998,
Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
ChEBI:CHEBI:91306, ChEBI:CHEBI:91307;
Evidence={ECO:0000250|UniProtKB:Q09128};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49393;
Evidence={ECO:0000250|UniProtKB:Q09128};
-!- CATALYTIC ACTIVITY:
Reaction=20S-hydroxycholecalciferol + 2 H(+) + O2 + 2 reduced
[adrenodoxin] = 20S,25-dihydroxycholecalciferol + H2O + 2 oxidized
[adrenodoxin]; Xref=Rhea:RHEA:49212, Rhea:RHEA-COMP:9998, Rhea:RHEA-
COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:90983,
ChEBI:CHEBI:90984; Evidence={ECO:0000250|UniProtKB:Q09128};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49213;
Evidence={ECO:0000250|UniProtKB:Q09128};
-!- CATALYTIC ACTIVITY:
Reaction=20S-hydroxycholecalciferol + 2 H(+) + O2 + 2 reduced
[adrenodoxin] = 20S,24S-dihydroxycholecalciferol + H2O + 2 oxidized
[adrenodoxin]; Xref=Rhea:RHEA:49208, Rhea:RHEA-COMP:9998, Rhea:RHEA-
COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:90983,
ChEBI:CHEBI:90986; Evidence={ECO:0000250|UniProtKB:Q09128};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49209;
Evidence={ECO:0000250|UniProtKB:Q09128};
-!- CATALYTIC ACTIVITY:
Reaction=20S-hydroxycholecalciferol + 2 H(+) + O2 + 2 reduced
[adrenodoxin] = 20S,24R-dihydroxycholecalciferol + H2O + 2 oxidized
[adrenodoxin]; Xref=Rhea:RHEA:49204, Rhea:RHEA-COMP:9998, Rhea:RHEA-
COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:90983,
ChEBI:CHEBI:90985; Evidence={ECO:0000250|UniProtKB:Q09128};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49205;
Evidence={ECO:0000250|UniProtKB:Q09128};
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000250|UniProtKB:Q09128};
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q09128}.
-!- INDUCTION: By 1,25-dihydroxyvitamin D(3) in kidney.
{ECO:0000269|PubMed:14528024}.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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EMBL; D49438; BAA08416.1; -; mRNA.
EMBL; D89669; BAA21843.1; -; mRNA.
CCDS; CCDS17122.1; -.
PIR; S60033; S60033.
RefSeq; NP_034126.1; NM_009996.4.
SMR; Q64441; -.
STRING; 10090.ENSMUSP00000047954; -.
iPTMnet; Q64441; -.
PhosphoSitePlus; Q64441; -.
EPD; Q64441; -.
PaxDb; Q64441; -.
PRIDE; Q64441; -.
Ensembl; ENSMUST00000038824; ENSMUSP00000047954; ENSMUSG00000038567.
GeneID; 13081; -.
KEGG; mmu:13081; -.
UCSC; uc008ocb.1; mouse.
CTD; 1591; -.
MGI; MGI:88593; Cyp24a1.
eggNOG; KOG0159; Eukaryota.
eggNOG; COG2124; LUCA.
GeneTree; ENSGT00950000182905; -.
HOGENOM; CLU_001570_28_1_1; -.
InParanoid; Q64441; -.
KO; K07436; -.
OMA; HIGAPCL; -.
OrthoDB; 1273535at2759; -.
PhylomeDB; Q64441; -.
TreeFam; TF105094; -.
Reactome; R-MMU-196791; Vitamin D (calciferol) metabolism.
Reactome; R-MMU-211916; Vitamins.
PRO; PR:Q64441; -.
Proteomes; UP000000589; Chromosome 2.
RNAct; Q64441; protein.
Bgee; ENSMUSG00000038567; Expressed in metanephros and 41 other tissues.
ExpressionAtlas; Q64441; baseline and differential.
Genevisible; Q64441; MM.
GO; GO:0005739; C:mitochondrion; HDA:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0030342; F:1-alpha,25-dihydroxyvitamin D3 24-hydroxylase activity; ISS:UniProtKB.
GO; GO:0008403; F:25-hydroxycholecalciferol-24-hydroxylase activity; IMP:MGI.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0070576; F:vitamin D 24-hydroxylase activity; ISS:UniProtKB.
GO; GO:0070643; F:vitamin D 25-hydroxylase activity; ISS:UniProtKB.
GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
GO; GO:0055114; P:oxidation-reduction process; ISO:MGI.
GO; GO:0033280; P:response to vitamin D; ISO:MGI.
GO; GO:0042369; P:vitamin D catabolic process; ISS:UniProtKB.
GO; GO:0042359; P:vitamin D metabolic process; IMP:MGI.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002401; Cyt_P450_E_grp-I.
InterPro; IPR036396; Cyt_P450_sf.
Pfam; PF00067; p450; 1.
PRINTS; PR00463; EP450I.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
2: Evidence at transcript level;
Heme; Iron; Metal-binding; Mitochondrion; Monooxygenase; Oxidoreductase;
Reference proteome; Transit peptide.
TRANSIT 1..35
/note="Mitochondrion"
/evidence="ECO:0000250|UniProtKB:Q09128"
CHAIN 36..514
/note="1,25-dihydroxyvitamin D(3) 24-hydroxylase,
mitochondrial"
/id="PRO_0000003616"
METAL 462
/note="Iron (heme axial ligand)"
/evidence="ECO:0000250|UniProtKB:Q09128"
SEQUENCE 514 AA; 59453 MW; 3D38BA9235177A42 CRC64;
MSCPIDKRRP LIAFLRRLRD LGQPPRSVTS KAHVKRAPKE VPLCPLMTDG ETRNVTSLPG
PTNWPLLGSL LEIFWKGGLK KQHDTLAEYH KKYGQIFRMK LGSFDSVHLG SPSLLEALYR
TESAHPQRLE IKPWKAYRDH RNEAYGLMIL EGQEWQRVRS AFQKKLMKPV EIMKLDKKIN
EVLADFMGQI DELRDERGRI QDLYSELNKW SFESICLVLY EKRFGLLQKD TEEEALTFIA
AIKTMMSTFG KMMVTPVELH KRLNTKVWQA HTLAWDTIFK SVKPCIDHRL ERYSQQPGAD
FLCDIYQQDH LSKKELYAAV TELQLAAVET TANSLMWILY NLSRNPQVQQ RLLREIQSVL
PDNQTPRAED VRNMPYLKAC LKESMRLTPS VPFTTRTLDK PTVLGEYTLP KGTVLTLNTQ
VLGSSEDNFE DADKFRPERW LEKEKKINPF AHLPFGVGKR MCIGRRLAEL QLHLALCWII
QKYNIVATDS EPVEMLHLGI LVPSRELPIA FCPR


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