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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.
05-DEC-2018, entry version 171.
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:0000269|PubMed:15574355};
AltName: Full=Cytochrome P450 24A1;
AltName: Full=Cytochrome P450-CC24;
Flags: Precursor;
Name=CYP24A1; 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;
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, 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).
[8]
VARIANTS HCINF1 GLU-143 DEL; GLN-159; LYS-322; TRP-396 AND SER-409,
AND CHARACTERIZATION OF VARIANTS HCINF1 GLU-143 DEL; GLN-159; LYS-322;
TRP-396 AND SER-409.
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: Has a role in maintaining calcium homeostasis. Catalyzes
the adrenodoxin-dependent 24-hydroxylation of calcidiol (25-
hydroxyvitamin D(3)) and calcitriol (1-alpha,25-dihydroxyvitamin
D(3)). The enzyme can perform up to 6 rounds of hydroxylation of
calcitriol leading to calcitroic acid. It also shows 23-
hydroxylating activity leading to 1-alpha,25-dihydroxyvitamin
D(3)-26,23-lactone as end product. {ECO:0000269|PubMed:15574355}.
-!- 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};
-!- 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:15574355};
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
-!- SUBCELLULAR LOCATION: Mitochondrion.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q07973-1; Sequence=Displayed;
Name=2;
IsoId=Q07973-2; Sequence=VSP_043101;
Note=No experimental confirmation available.;
Name=3; Synonyms=CYP24-SV;
IsoId=Q07973-3; Sequence=VSP_053367, VSP_053368;
Note=Specifically expressed in macrophages. Lacks the transit
peptide. May be a dominant negative-acting isoform possibly by
sequestering vitamin D metabolites.;
-!- 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.
-!- 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]
UniGene; Hs.89663; -.
ProteinModelPortal; Q07973; -.
SMR; Q07973; -.
BioGrid; 107963; 5.
IntAct; Q07973; 2.
MINT; Q07973; -.
STRING; 9606.ENSP00000216862; -.
BindingDB; Q07973; -.
ChEMBL; CHEMBL4521; -.
DrugBank; DB00146; Calcidiol.
DrugBank; DB02300; Calcipotriol.
DrugBank; DB00136; Calcitriol.
DrugBank; DB01285; Corticotropin.
DrugBank; DB05024; CTA018.
DrugBank; DB00153; Ergocalciferol.
DrugBank; DB00910; Paricalcitol.
GuidetoPHARMACOLOGY; 1365; -.
SwissLipids; SLP:000001269; -.
iPTMnet; Q07973; -.
PhosphoSitePlus; Q07973; -.
BioMuta; CYP24A1; -.
DMDM; 19862747; -.
MaxQB; Q07973; -.
PaxDb; Q07973; -.
PeptideAtlas; Q07973; -.
PRIDE; Q07973; -.
ProteomicsDB; 58564; -.
ProteomicsDB; 58565; -. [Q07973-2]
Ensembl; ENST00000216862; ENSP00000216862; ENSG00000019186. [Q07973-1]
Ensembl; ENST00000395954; ENSP00000379284; ENSG00000019186. [Q07973-3]
Ensembl; ENST00000395955; ENSP00000379285; ENSG00000019186. [Q07973-2]
GeneID; 1591; -.
KEGG; hsa:1591; -.
UCSC; uc002xwu.2; human. [Q07973-1]
CTD; 1591; -.
DisGeNET; 1591; -.
EuPathDB; HostDB:ENSG00000019186.9; -.
GeneCards; CYP24A1; -.
H-InvDB; HIX0040564; -.
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; ENSGT00940000153297; -.
HOGENOM; HOG000276540; -.
HOVERGEN; HBG099053; -.
InParanoid; Q07973; -.
KO; K07436; -.
OMA; EILWKGG; -.
OrthoDB; EOG091G0MI3; -.
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; -.
PRO; PR:Q07973; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000019186; Expressed in 95 organ(s), highest expression level in adult mammalian kidney.
CleanEx; HS_CYP24A1; -.
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:0005634; C:nucleus; 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; IEA:Ensembl.
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: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; NAS:BHF-UCL.
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; Complete proteome; Disease mutation; Heme; Iron;
Metal-binding; Mitochondrion; Monooxygenase; Oxidoreductase;
Polymorphism; Reference proteome; Transit peptide.
TRANSIT 1 35 Mitochondrion. {ECO:0000250}.
CHAIN 36 514 1,25-dihydroxyvitamin D(3) 24-
hydroxylase, mitochondrial.
/FTId=PRO_0000003615.
METAL 462 462 Iron (heme axial ligand). {ECO:0000250}.
VAR_SEQ 1 8 MSSPISKS -> MYSCFSHR (in isoform 3).
{ECO:0000303|PubMed:15788398}.
/FTId=VSP_053367.
VAR_SEQ 9 150 Missing (in isoform 3).
{ECO:0000303|PubMed:15788398}.
/FTId=VSP_053368.
VAR_SEQ 413 478 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_043101.
VARIANT 143 143 Missing (in HCINF1; complete loss of
function). {ECO:0000269|PubMed:21675912}.
/FTId=VAR_066408.
VARIANT 157 157 R -> Q (in dbSNP:rs35051736).
/FTId=VAR_048464.
VARIANT 159 159 R -> Q (in HCINF1; complete loss of
function; dbSNP:rs387907322).
{ECO:0000269|PubMed:21675912}.
/FTId=VAR_066409.
VARIANT 322 322 E -> K (in HCINF1; complete loss of
function; dbSNP:rs387907324).
{ECO:0000269|PubMed:21675912}.
/FTId=VAR_066410.
VARIANT 374 374 M -> T (in dbSNP:rs6022990).
/FTId=VAR_048465.
VARIANT 396 396 R -> W (in HCINF1; complete loss of
function; dbSNP:rs114368325).
{ECO:0000269|PubMed:21675912}.
/FTId=VAR_066411.
VARIANT 409 409 L -> S (in HCINF1; retains small but
measurable levels of activity;
dbSNP:rs6068812).
{ECO:0000269|PubMed:21675912}.
/FTId=VAR_048466.
CONFLICT 68 68 G -> A (in Ref. 1; AAA62379/AAB03776).
{ECO:0000305}.
CONFLICT 124 125 AY -> V (in Ref. 1; AAA62379).
{ECO:0000305}.
CONFLICT 270 270 D -> G (in Ref. 1; AAA62379).
{ECO:0000305}.
CONFLICT 365 365 V -> R (in Ref. 1; AAA62379).
{ECO:0000305}.
CONFLICT 368 368 A -> E (in Ref. 1; AAA62379).
{ECO:0000305}.
CONFLICT 390 390 S -> G (in Ref. 1; AAA62379).
{ECO:0000305}.
CONFLICT 511 511 F -> S (in Ref. 6; AAB29308).
{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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E0988Rb ELISA 4-nitrophenol 2-hydroxylase,CYP2E,CYP2E1,CYPIIE1,Cytochrome P450 2E1,Cytochrome P450 isozyme 3A,Cytochrome P450 LM3A,Cytochrome P450-ALC,Oryctolagus cuniculus,Rabbit 96T


 

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