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Reviewed, UniProtKB/Swiss-Prot Q07973 (CP24A_HUMAN)

Last modified July 22, 2008. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    1,25-dihydroxyvitamin D(3) 24-hydroxylase, mitochondrial
      Short name=Vitamin D(3) 24-hydroxylase
      Short name=24-OHase
    EC=1.14.13.n4
Alternative name(s):
    Cytochrome P450 24A1
    P450-CC24
Gene names
Name: CYP24A1
Synonyms: CYP24
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length514 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Has a role in maintaining calcium homeostasis. Catalyzes the NADPH-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.

Catalytic activity

Calcitriol + NADPH + O(2) = calcitetrol + NADP(+) + H(2)O.

Calcidiol + NADPH + O(2) = secalciferol + NADP(+) + H(2)O.

Cofactor

Heme group By similarity.

Subcellular location

Mitochondrion.

Sequence similarities

Belongs to the cytochrome P450 family.

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Ontologies

Keywords

   Cellular componentMitochondrion
   DomainTransit peptide
   LigandHeme
Iron
Metal-binding
NADP
   Molecular functionMonooxygenase
Oxidoreductase

Gene Ontology (GO)

   Biological processoxidation reduction Ref.1 Ref.3

Inferred from direct assay. Source: UniProtKB

   Molecular function1-alpha,25-dihydroxyvitamin D3 (1,25-(OH)2D3) 24-hydroxylase activity Ref.1

Inferred from direct assay. Source: UniProtKB

heme binding Ref.1

Traceable author statement. Source: UniProtKB

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Transit peptide1 – 3535Mitochondrion By similarity
Chain36 – 5144791,25-dihydroxyvitamin D(3) 24-hydroxylase, mitochondrial

Sites

Metal binding4621Iron (heme axial ligand) Potential

Experimental info

Sequence conflict681G → A in AAA62379 and AAB03776. Ref.1
Sequence conflict124 – 1252AY → V in AAA62379. Ref.1
Sequence conflict2701D → G in AAA62379. Ref.1
Sequence conflict3651V → R in AAA62379. Ref.1
Sequence conflict3681A → E in AAA62379. Ref.1
Sequence conflict3901S → G in AAA62379. Ref.1
Sequence conflict5111F → S in AAB29308. Ref.4

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Sequences

Sequence LengthMass (Da)Tools
Q07973-1 [UniParc].

Last modified October 18, 2001. Version 2.
Checksum: 8862F63771981195

FASTA51458,875
        10         20         30         40         50         60 
MSSPISKSRS LAAFLQQLRS PRQPPRLVTS TAYTSPQPRE VPVCPLTAGG ETQNAAALPG 

        70         80         90        100        110        120 
PTSWPLLGSL LQILWKGGLK KQHDTLVEYH KKYGKIFRMK LGSFESVHLG SPCLLEALYR 

       130        140        150        160        170        180 
TESAYPQRLE IKPWKAYRDY RKEGYGLLIL EGEDWQRVRS AFQKKLMKPG EVMKLDNKIN 

       190        200        210        220        230        240 
EVLADFMGRI DELCDERGHV EDLYSELNKW SFESICLVLY EKRFGLLQKN AGDEAVNFIM 

       250        260        270        280        290        300 
AIKTMMSTFG RMMVTPVELH KSLNTKVWQD HTLAWDTIFK SVKACIDNRL EKYSQQPSAD 

       310        320        330        340        350        360 
FLCDIYHQNR LSKKELYAAV TELQLAAVET TANSLMWILY NLSRNPQVQQ KLLKEIQSVL 

       370        380        390        400        410        420 
PENQVPRAED LRNMPYLKAC LKESMRLTPS VPFTTRTLDK ATVLGEYALP KGTVLMLNTQ 

       430        440        450        460        470        480 
VLGSSEDNFE DSSQFRPERW LQEKEKINPF AHLPFGVGKR MCIGRRLAEL QLHLALCWIV 

       490        500        510 
RKYDIQATDN EPVEMLHSGT LVPSRELPIA FCQR

« Hide

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References

« Hide 'large scale' references
[1]"Isolation and expression of human 1,25-dihydroxyvitamin D3 24-hydroxylase cDNA."
Chen K.-S., Prahl J.M., Deluca H.F.
Proc. Natl. Acad. Sci. U.S.A. 90:4543-4547(1993) [PubMed: 8506296] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The DNA sequence and comparative analysis of human chromosome 20."
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. expand/collapse author list , 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.
Nature 414:865-871(2001) [PubMed: 11780052] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Cloning of the human 1 alpha,25-dihydroxyvitamin D-3 24-hydroxylase gene promoter and identification of two vitamin D-responsive elements."
Chen K.-S., DeLuca H.F.
Biochim. Biophys. Acta 1263:1-9(1995) [PubMed: 7632726] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-104.
[4]"Human 25-hydroxyvitamin D 24-hydroxylase cytochrome P450 subunit maps to a different chromosomal location than that of pseudovitamin D-deficient rickets."
Labuda M., Lemieux N., Tihy F., Prinster C., Glorieux F.H.
J. Bone Miner. Res. 8:1397-1406(1993) [PubMed: 8266831] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 258-514.
[5]"Metabolism of vitamin D3 by cytochromes P450."
Sakaki T., Kagawa N., Yamamoto K., Inouye K.
Front. Biosci. 10:119-134(2005) [PubMed: 15574355] [Abstract]
Cited for: SUBSTRATE SPECIFICITY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

L13286 mRNA. Translation: AAA62379.1.
AL138805 Genomic DNA. Translation: CAB91829.1.
U60669 Genomic DNA. Translation: AAB03776.1. Sequence problems.
S67623 mRNA. Translation: AAB29308.1.
PIRA47436.
I55488.
RefSeqNP_000773.2.
UniGeneHs.89663

3D structure databases

HSSPHSSP built from PDB template 1JPZ based on UniProtKB P14779.
ModBaseSearch...

PTM databases

PhosphoSiteQ07973.

Genome annotation databases

EnsemblENSG00000019186. Homo sapiens. [Contig view]
GeneID1591.
KEGGhsa:1591.

Organism-specific databases

HGNCHGNC:2602. CYP24A1.
MIM126065. gene.
PharmGKBPA27097.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMQ07973.
HOVERGENQ07973.

Gene expression databases

ArrayExpressQ07973.
CleanExHS_CYP24A1.
GermOnlineENSG00000019186. Homo sapiens.

Family and domain databases

InterProIPR001128. Cyt_P450.
IPR002949. Cyt_P450_E_CYP24A_mit.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
Gene3DG3DSA:1.10.630.10. Cyt_P450. 1 hit.
PANTHERPTHR19383. Cyt_P450. 1 hit.
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00463. EP450I.
PR01238. MITP450CC24.
PR00385. P450.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProDomQ07973.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

DrugBankDB00146. Calcidiol.
DB00136. Calcitriol.
DB00169. Cholecalciferol.
DB00153. Ergocalciferol.
DB00910. Paricalcitol.
SOURCESearch...
ProtoNetSearch...

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Entry information

Entry nameCP24A_HUMAN
AccessionPrimary (citable) accession number: Q07973
Secondary accession number(s): Q15807
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 18, 2001
Last modified: July 22, 2008
This is version 71 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents