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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_HUMAN             Reviewed;         514 AA.
Q07973; Q15807; Q32ML3; Q5I2W7;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
18-OCT-2001, sequence version 2.
26-FEB-2020, entry version 181.
RecName: Full=1,25-dihydroxyvitamin D(3) 24-hydroxylase, mitochondrial {ECO:0000303|PubMed:8506296};
Short=24-OHase;
Short=Vitamin D(3) 24-hydroxylase;
EC=1.14.15.16 {ECO:0000269|PubMed:15574355, ECO:0000269|PubMed:16617161, ECO:0000269|PubMed:21675912, ECO:0000269|PubMed:24893882, ECO:0000269|PubMed:8679605};
AltName: Full=Cytochrome P450 24A1;
AltName: Full=Cytochrome P450-CC24;
Flags: Precursor;
Name=CYP24A1 {ECO:0000312|HGNC:HGNC:2602}; Synonyms=CYP24;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8506296; DOI=10.1073/pnas.90.10.4543;
Chen K.-S., Prahl J.M., Deluca H.F.;
"Isolation and expression of human 1,25-dihydroxyvitamin D3 24-hydroxylase
cDNA.";
Proc. Natl. Acad. Sci. U.S.A. 90:4543-4547(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
PubMed=15788398; DOI=10.1074/jbc.m414522200;
Ren S., Nguyen L., Wu S., Encinas C., Adams J.S., Hewison M.;
"Alternative splicing of vitamin D-24-hydroxylase: a novel mechanism for
the regulation of extrarenal 1,25-dihydroxyvitamin D synthesis.";
J. Biol. Chem. 280:20604-20611(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-104.
PubMed=7632726; DOI=10.1016/0167-4781(95)00060-t;
Chen K.-S., DeLuca H.F.;
"Cloning of the human 1 alpha,25-dihydroxyvitamin D-3 24-hydroxylase gene
promoter and identification of two vitamin D-responsive elements.";
Biochim. Biophys. Acta 1263:1-9(1995).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 258-514 (ISOFORM 1).
PubMed=8266831; DOI=10.1002/jbmr.5650081114;
Labuda M., Lemieux N., Tihy F., Prinster C., Glorieux F.H.;
"Human 25-hydroxyvitamin D 24-hydroxylase cytochrome P450 subunit maps to a
different chromosomal location than that of pseudovitamin D-deficient
rickets.";
J. Bone Miner. Res. 8:1397-1406(1993).
[7]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=8679605; DOI=10.1021/bi960658i;
Beckman M.J., Tadikonda P., Werner E., Prahl J., Yamada S., DeLuca H.F.;
"Human 25-hydroxyvitamin D3-24-hydroxylase, a multicatalytic enzyme.";
Biochemistry 35:8465-8472(1996).
[8]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=11012668; DOI=10.1046/j.1432-1327.2000.01680.x;
Sakaki T., Sawada N., Komai K., Shiozawa S., Yamada S., Yamamoto K.,
Ohyama Y., Inouye K.;
"Dual metabolic pathway of 25-hydroxyvitamin D3 catalyzed by human CYP24.";
Eur. J. Biochem. 267:6158-6165(2000).
[9]
FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
PubMed=15574355; DOI=10.2741/1514;
Sakaki T., Kagawa N., Yamamoto K., Inouye K.;
"Metabolism of vitamin D3 by cytochromes P450.";
Front. Biosci. 10:119-134(2005).
[10]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=16617161; DOI=10.1124/mol.106.023275;
Hamamoto H., Kusudo T., Urushino N., Masuno H., Yamamoto K., Yamada S.,
Kamakura M., Ohta M., Inouye K., Sakaki T.;
"Structure-function analysis of vitamin D 24-hydroxylase (CYP24A1) by site-
directed mutagenesis: amino acid residues responsible for species-based
difference of CYP24A1 between humans and rats.";
Mol. Pharmacol. 70:120-128(2006).
[11]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=24893882; DOI=10.1111/febs.12862;
Tieu E.W., Tang E.K., Tuckey R.C.;
"Kinetic analysis of human CYP24A1 metabolism of vitamin D via the C24-
oxidation pathway.";
FEBS J. 281:3280-3296(2014).
[12]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=25727742; DOI=10.1016/j.jsbmb.2015.02.010;
Tieu E.W., Li W., Chen J., Kim T.K., Ma D., Slominski A.T., Tuckey R.C.;
"Metabolism of 20-hydroxyvitamin D3 and 20,23-dihydroxyvitamin D3 by rat
and human CYP24A1.";
J. Steroid Biochem. Mol. Biol. 149:153-165(2015).
[13]
VARIANTS HCINF1 GLU-143 DEL; GLN-159; LYS-322; TRP-396 AND SER-409,
CHARACTERIZATION OF VARIANTS HCINF1 GLU-143 DEL; GLN-159; LYS-322; TRP-396
AND SER-409, AND CATALYTIC ACTIVITY.
PubMed=21675912; DOI=10.1056/nejmoa1103864;
Schlingmann K.P., Kaufmann M., Weber S., Irwin A., Goos C., John U.,
Misselwitz J., Klaus G., Kuwertz-Broking E., Fehrenbach H., Wingen A.M.,
Guran T., Hoenderop J.G., Bindels R.J., Prosser D.E., Jones G., Konrad M.;
"Mutations in CYP24A1 and idiopathic infantile hypercalcemia.";
N. Engl. J. Med. 365:410-421(2011).
-!- FUNCTION: A cytochrome P450 monooxygenase with a key role in vitamin D
catabolism and calcium homeostasis. Via C24- and C23-oxidation
pathways, 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)) (PubMed:24893882, PubMed:15574355,
PubMed:8679605, PubMed:11012668, PubMed:16617161). 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 (PubMed:24893882,
PubMed:15574355). With initial hydroxylation at C-23 (via C23-oxidation
pathway), catalyzes sequential oxidation of calcidiol leading to the
formation of 25(OH)D3-26,23-lactone as end product (PubMed:11012668,
PubMed:8679605). Preferentially hydroxylates at C-25 other vitamin D
active metabolites, such as CYP11A1-derived secosteroids 20S-
hydroxycholecalciferol and 20S,23-dihydroxycholecalciferol
(PubMed:25727742). 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 (PubMed:8679605).
{ECO:0000269|PubMed:11012668, ECO:0000269|PubMed:15574355,
ECO:0000269|PubMed:16617161, ECO:0000269|PubMed:24893882,
ECO:0000269|PubMed:25727742, ECO:0000269|PubMed:8679605}.
-!- 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:0000269|PubMed:15574355,
ECO:0000269|PubMed:16617161, ECO:0000269|PubMed:21675912,
ECO:0000269|PubMed:24893882, ECO:0000269|PubMed:8679605};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24965;
Evidence={ECO:0000305|PubMed:21675912};
-!- 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:0000269|PubMed:16617161, ECO:0000269|PubMed:21675912,
ECO:0000269|PubMed:24893882};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24973;
Evidence={ECO:0000305|PubMed:21675912};
-!- 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:0000269|PubMed:16617161, ECO:0000269|PubMed:21675912,
ECO:0000269|PubMed:24893882};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24977;
Evidence={ECO:0000305|PubMed:21675912};
-!- 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:0000269|PubMed:21675912, ECO:0000269|PubMed:24893882};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24985;
Evidence={ECO:0000305|PubMed:21675912};
-!- 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:0000269|PubMed:21675912, ECO:0000269|PubMed:24893882};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24989;
Evidence={ECO:0000305|PubMed:21675912};
-!- CATALYTIC ACTIVITY:
Reaction=calcitriol + 2 H(+) + O2 + 2 reduced [adrenodoxin] =
1alpha,23S,25-trihydroxycholecalciferol + H2O + 2 oxidized
[adrenodoxin]; Xref=Rhea:RHEA:49192, 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:90970; Evidence={ECO:0000269|PubMed:16617161,
ECO:0000269|PubMed:24893882};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49193;
Evidence={ECO:0000305|PubMed:16617161};
-!- 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:0000269|PubMed:11012668,
ECO:0000269|PubMed:15574355, ECO:0000269|PubMed:24893882,
ECO:0000269|PubMed:8679605};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24969;
Evidence={ECO:0000305|PubMed:8679605};
-!- 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:0000269|PubMed:11012668,
ECO:0000269|PubMed:24893882, ECO:0000269|PubMed:8679605};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49197;
Evidence={ECO:0000305|PubMed:8679605};
-!- 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:0000269|PubMed:11012668, ECO:0000269|PubMed:24893882,
ECO:0000269|PubMed:8679605};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49269;
Evidence={ECO:0000305|PubMed:8679605};
-!- CATALYTIC ACTIVITY:
Reaction=calcidiol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = (23S)-
23,25-dihydroxycalciol + H2O + 2 oxidized [adrenodoxin];
Xref=Rhea:RHEA:46616, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
ChEBI:CHEBI:17933, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
ChEBI:CHEBI:47214; Evidence={ECO:0000269|PubMed:11012668,
ECO:0000269|PubMed:24893882, ECO:0000269|PubMed:8679605};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46617;
Evidence={ECO:0000305|PubMed:8679605};
-!- 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:0000269|PubMed:25727742};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49213;
Evidence={ECO:0000305|PubMed:25727742};
-!- 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:0000269|PubMed:25727742};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49205;
Evidence={ECO:0000305|PubMed:25727742};
-!- 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:0000269|PubMed:25727742};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49397;
Evidence={ECO:0000305|PubMed:25727742};
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000250|UniProtKB:Q09128};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.16 uM for calcidiol {ECO:0000269|PubMed:11012668};
KM=0.072 uM for calcitriol {ECO:0000269|PubMed:11012668};
KM=0.35 uM for calcitriol {ECO:0000269|PubMed:16617161};
Vmax=0.088 mol/min/mol enzyme toward calcidiol
{ECO:0000269|PubMed:11012668};
Vmax=0.066 mol/min/mol enzyme toward calcitriol
{ECO:0000269|PubMed:11012668};
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q09128}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q07973-1; Sequence=Displayed;
Name=2;
IsoId=Q07973-2; Sequence=VSP_043101;
Name=3; Synonyms=CYP24-SV;
IsoId=Q07973-3; Sequence=VSP_053367, VSP_053368;
-!- DISEASE: Hypercalcemia, infantile, 1 (HCINF1) [MIM:143880]: A disorder
characterized by abnormally high level of calcium in the blood, failure
to thrive, vomiting, dehydration, and nephrocalcinosis.
{ECO:0000269|PubMed:21675912}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- MISCELLANEOUS: [Isoform 3]: Specifically expressed in macrophages.
Lacks the transit peptide. May be a dominant negative-acting isoform
possibly by sequestering vitamin D metabolites. {ECO:0000305}.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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EMBL; L13286; AAA62379.1; -; mRNA.
EMBL; AY858838; AAW50795.1; -; mRNA.
EMBL; AL138805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC109083; AAI09084.1; -; mRNA.
EMBL; BC109084; AAI09085.1; -; mRNA.
EMBL; U60669; AAB03776.1; ALT_SEQ; Genomic_DNA.
EMBL; S67623; AAB29308.1; -; mRNA.
CCDS; CCDS33491.1; -. [Q07973-1]
CCDS; CCDS46616.1; -. [Q07973-2]
PIR; A47436; A47436.
PIR; I55488; I55488.
RefSeq; NP_000773.2; NM_000782.4. [Q07973-1]
RefSeq; NP_001122387.1; NM_001128915.1. [Q07973-2]
RefSeq; XP_005260361.1; XM_005260304.4. [Q07973-1]
RefSeq; XP_016883180.1; XM_017027691.1. [Q07973-1]
RefSeq; XP_016883181.1; XM_017027692.1. [Q07973-1]
RefSeq; XP_016883182.1; XM_017027693.1. [Q07973-2]
SMR; Q07973; -.
BioGrid; 107963; 5.
IntAct; Q07973; 5.
MINT; Q07973; -.
STRING; 9606.ENSP00000216862; -.
BindingDB; Q07973; -.
ChEMBL; CHEMBL4521; -.
DrugBank; DB00146; Calcifediol.
DrugBank; DB02300; Calcipotriol.
DrugBank; DB00136; Calcitriol.
DrugBank; DB01285; Corticotropin.
DrugBank; DB05024; CTA018.
DrugBank; DB00153; Ergocalciferol.
DrugBank; DB00910; Paricalcitol.
DrugCentral; Q07973; -.
GuidetoPHARMACOLOGY; 1365; -.
SwissLipids; SLP:000001269; -.
iPTMnet; Q07973; -.
PhosphoSitePlus; Q07973; -.
BioMuta; CYP24A1; -.
DMDM; 19862747; -.
jPOST; Q07973; -.
MassIVE; Q07973; -.
MaxQB; Q07973; -.
PaxDb; Q07973; -.
PeptideAtlas; Q07973; -.
PRIDE; Q07973; -.
ProteomicsDB; 58564; -. [Q07973-1]
ProteomicsDB; 58565; -. [Q07973-2]
ProteomicsDB; 62973; -.
Ensembl; ENST00000216862; ENSP00000216862; ENSG00000019186. [Q07973-1]
Ensembl; ENST00000395955; ENSP00000379285; ENSG00000019186. [Q07973-2]
Ensembl; ENST00000395954; ENSP00000379284; ENSG00000019186. [Q07973-3]
GeneID; 1591; -.
KEGG; hsa:1591; -.
UCSC; uc002xwu.2; human. [Q07973-1]
CTD; 1591; -.
DisGeNET; 1591; -.
GeneCards; CYP24A1; -.
HGNC; HGNC:2602; CYP24A1.
HPA; HPA022261; -.
HPA; HPA063771; -.
MalaCards; CYP24A1; -.
MIM; 126065; gene.
MIM; 143880; phenotype.
neXtProt; NX_Q07973; -.
OpenTargets; ENSG00000019186; -.
Orphanet; 300547; Autosomal recessive infantile hypercalcemia.
PharmGKB; PA27097; -.
eggNOG; KOG0159; Eukaryota.
eggNOG; COG2124; LUCA.
GeneTree; ENSGT00950000182905; -.
HOGENOM; CLU_001570_28_1_1; -.
InParanoid; Q07973; -.
KO; K07436; -.
OMA; HIGAPCL; -.
OrthoDB; 1231389at2759; -.
PhylomeDB; Q07973; -.
TreeFam; TF105094; -.
BioCyc; MetaCyc:HS00395-MONOMER; -.
BRENDA; 1.14.13.159; 2681.
Reactome; R-HSA-196791; Vitamin D (calciferol) metabolism.
Reactome; R-HSA-211916; Vitamins.
Reactome; R-HSA-5579010; Defective CYP24A1 causes Hypercalcemia, infantile (HCAI).
SABIO-RK; Q07973; -.
SIGNOR; Q07973; -.
ChiTaRS; CYP24A1; human.
GeneWiki; CYP24A1; -.
GenomeRNAi; 1591; -.
Pharos; Q07973; Tchem.
PRO; PR:Q07973; -.
Proteomes; UP000005640; Chromosome 20.
RNAct; Q07973; protein.
Bgee; ENSG00000019186; Expressed in adult mammalian kidney and 94 other tissues.
Genevisible; Q07973; HS.
GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0030342; F:1-alpha,25-dihydroxyvitamin D3 24-hydroxylase activity; IDA:UniProtKB.
GO; GO:0008403; F:25-hydroxycholecalciferol-24-hydroxylase activity; IDA:UniProtKB.
GO; GO:0020037; F:heme binding; TAS:UniProtKB.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0016491; F:oxidoreductase activity; NAS:UniProtKB.
GO; GO:0070643; F:vitamin D 25-hydroxylase activity; IDA:UniProtKB.
GO; GO:0001649; P:osteoblast differentiation; IEP:BHF-UCL.
GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
GO; GO:0033280; P:response to vitamin D; IDA:BHF-UCL.
GO; GO:0042369; P:vitamin D catabolic process; IDA:UniProtKB.
GO; GO:0042359; P:vitamin D metabolic process; TAS:Reactome.
GO; GO:0070561; P:vitamin D receptor signaling pathway; NAS:BHF-UCL.
GO; GO:0006766; P:vitamin metabolic process; TAS:Reactome.
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.
1: Evidence at protein level;
Alternative splicing; Disease mutation; Heme; Iron; Metal-binding;
Mitochondrion; Monooxygenase; Oxidoreductase; Polymorphism;
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_0000003615"
METAL 462
/note="Iron (heme axial ligand)"
/evidence="ECO:0000250|UniProtKB:Q09128"
VAR_SEQ 1..8
/note="MSSPISKS -> MYSCFSHR (in isoform 3)"
/evidence="ECO:0000303|PubMed:15788398"
/id="VSP_053367"
VAR_SEQ 9..150
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:15788398"
/id="VSP_053368"
VAR_SEQ 413..478
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_043101"
VARIANT 143
/note="Missing (in HCINF1; complete loss of function)"
/evidence="ECO:0000269|PubMed:21675912"
/id="VAR_066408"
VARIANT 157
/note="R -> Q (in dbSNP:rs35051736)"
/id="VAR_048464"
VARIANT 159
/note="R -> Q (in HCINF1; complete loss of function;
dbSNP:rs387907322)"
/evidence="ECO:0000269|PubMed:21675912"
/id="VAR_066409"
VARIANT 322
/note="E -> K (in HCINF1; complete loss of function;
dbSNP:rs387907324)"
/evidence="ECO:0000269|PubMed:21675912"
/id="VAR_066410"
VARIANT 374
/note="M -> T (in dbSNP:rs6022990)"
/id="VAR_048465"
VARIANT 396
/note="R -> W (in HCINF1; complete loss of function;
dbSNP:rs114368325)"
/evidence="ECO:0000269|PubMed:21675912"
/id="VAR_066411"
VARIANT 409
/note="L -> S (in HCINF1; retains small but measurable
levels of activity; dbSNP:rs6068812)"
/evidence="ECO:0000269|PubMed:21675912"
/id="VAR_048466"
CONFLICT 68
/note="G -> A (in Ref. 1; AAA62379/AAB03776)"
/evidence="ECO:0000305"
CONFLICT 124..125
/note="AY -> V (in Ref. 1; AAA62379)"
/evidence="ECO:0000305"
CONFLICT 270
/note="D -> G (in Ref. 1; AAA62379)"
/evidence="ECO:0000305"
CONFLICT 365
/note="V -> R (in Ref. 1; AAA62379)"
/evidence="ECO:0000305"
CONFLICT 368
/note="A -> E (in Ref. 1; AAA62379)"
/evidence="ECO:0000305"
CONFLICT 390
/note="S -> G (in Ref. 1; AAA62379)"
/evidence="ECO:0000305"
CONFLICT 511
/note="F -> S (in Ref. 6; AAB29308)"
/evidence="ECO:0000305"
SEQUENCE 514 AA; 58875 MW; 8862F63771981195 CRC64;
MSSPISKSRS LAAFLQQLRS PRQPPRLVTS TAYTSPQPRE VPVCPLTAGG ETQNAAALPG
PTSWPLLGSL LQILWKGGLK KQHDTLVEYH KKYGKIFRMK LGSFESVHLG SPCLLEALYR
TESAYPQRLE IKPWKAYRDY RKEGYGLLIL EGEDWQRVRS AFQKKLMKPG EVMKLDNKIN
EVLADFMGRI DELCDERGHV EDLYSELNKW SFESICLVLY EKRFGLLQKN AGDEAVNFIM
AIKTMMSTFG RMMVTPVELH KSLNTKVWQD HTLAWDTIFK SVKACIDNRL EKYSQQPSAD
FLCDIYHQNR LSKKELYAAV TELQLAAVET TANSLMWILY NLSRNPQVQQ KLLKEIQSVL
PENQVPRAED LRNMPYLKAC LKESMRLTPS VPFTTRTLDK ATVLGEYALP KGTVLMLNTQ
VLGSSEDNFE DSSQFRPERW LQEKEKINPF AHLPFGVGKR MCIGRRLAEL QLHLALCWIV
RKYDIQATDN EPVEMLHSGT LVPSRELPIA FCQR


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