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Q09128 (CP24A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
1,25-dihydroxyvitamin D(3) 24-hydroxylase, mitochondrial

Short name=24-OHase
Short name=Vitamin D(3) 24-hydroxylase
EC=1.14.13.126
Alternative name(s):
Cytochrome P450 24A1
Cytochrome P450-CC24
Gene names
Name:Cyp24a1
Synonyms:Cyp24
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

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

General annotation (Comments)

Function

Has a role in maintaining calcium homeostasis. Catalyzes the NADPH-dependent 24-hydroxylation of calcidiol (25-hydroxyvitamin D3) and calcitriol (1-alpha,25-dihydroxyvitamin D3). The enzyme can perform up to 6 rounds of hydroxylation of calcitriol leading to calcitroic acid.

Catalytic activity

Calcitriol + NADPH + O2 = calcitetrol + NADP+ + H2O. Ref.5

Calcidiol + NADPH + O2 = secalciferol + NADP+ + H2O. Ref.5

Cofactor

Heme group. Ref.7

Subcellular location

Mitochondrion.

Sequence similarities

Belongs to the cytochrome P450 family.

Biophysicochemical properties

Kinetic parameters:

KM=2.8 µM for calcidiol Ref.5

pH dependence:

Optimum pH is 7.7.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3535Mitochondrion Ref.1 Ref.5
Chain36 – 5144791,25-dihydroxyvitamin D(3) 24-hydroxylase, mitochondrial
PRO_0000003617

Sites

Metal binding4621Iron (heme axial ligand)

Secondary structure

............................................................................. 514
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q09128 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 2E5CC1CCBA3C2B91

FASTA51459,448
        10         20         30         40         50         60 
MSCPIDKRRT LIAFLRRLRD LGQPPRSVTS KASASRAPKE VPLCPLMTDG ETRNVTSLPG 

        70         80         90        100        110        120 
PTNWPLLGSL LEIFWKGGLK KQHDTLAEYH KKYGQIFRMK LGSFDSVHLG SPSLLEALYR 

       130        140        150        160        170        180 
TESAHPQRLE IKPWKAYRDH RNEAYGLMIL EGQEWQRVRS AFQKKLMKPV EIMKLDKKIN 

       190        200        210        220        230        240 
EVLADFLERM DELCDERGRI PDLYSELNKW SFESICLVLY EKRFGLLQKE TEEEALTFIT 

       250        260        270        280        290        300 
AIKTMMSTFG KMMVTPVELH KRLNTKVWQA HTLAWDTIFK SVKPCIDNRL QRYSQQPGAD 

       310        320        330        340        350        360 
FLCDIYQQDH LSKKELYAAV TELQLAAVET TANSLMWILY NLSRNPQAQR RLLQEVQSVL 

       370        380        390        400        410        420 
PDNQTPRAED LRNMPYLKAC LKESMRLTPS VPFTTRTLDK PTVLGEYALP KGTVLTLNTQ 

       430        440        450        460        470        480 
VLGSSEDNFE DSHKFRPERW LQKEKKINPF AHLPFGIGKR MCIGRRLAEL QLHLALCWII 

       490        500        510 
QKYDIVATDN EPVEMLHLGI LVPSRELPIA FRPR 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of cDNA encoding 25-hydroxyvitamin D3 24-hydroxylase."
Ohyama Y., Noshiro M., Okuda K.
FEBS Lett. 278:195-198(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 36-43.
Tissue: Kidney.
[2]"Structural characterization of the gene encoding rat 25-hydroxyvitamin D3 24-hydroxylase."
Ohyama Y., Noshiro M., Eggertsen G., Gotoh O., Kato Y., Bjoerkhem I., Okuda K.
Biochemistry 32:76-82(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[4]"Identification of a vitamin D responsive element in the promoter of the rat cytochrome P450(24) gene."
Hahn C.N., Kerry D.M., Omdahl J.L., May B.K.
Nucleic Acids Res. 22:2410-2416(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-86.
[5]"Isolation and characterization of a cytochrome P-450 from rat kidney mitochondria that catalyzes the 24-hydroxylation of 25-hydroxyvitamin D3."
Ohyama Y., Okuda K.
J. Biol. Chem. 266:8690-8695(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 36-43, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
[6]"Metabolism of vitamin D3 by cytochromes P450."
Sakaki T., Kagawa N., Yamamoto K., Inouye K.
Front. Biosci. 10:119-134(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBSTRATE SPECIFICITY.
[7]"Crystal structure of CYP24A1, a mitochondrial cytochrome P450 involved in vitamin D metabolism."
Annalora A.J., Goodin D.B., Hong W.X., Zhang Q., Johnson E.F., Stout C.D.
J. Mol. Biol. 396:441-451(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 34-514 IN COMPLEX WITH HEME, COFACTOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59506 mRNA. Translation: CAA42093.1.
L04618 expand/collapse EMBL AC list , L04608, L04609, L04610, L04611, L04612, L04613, L04614, L04615, L04616, L04617 Genomic DNA. Translation: AAA42340.1.
BC100059 mRNA. Translation: AAI00060.1.
Z28351 Genomic DNA. Translation: CAA82206.1.
PIRA45228.
RefSeqNP_963966.1. NM_201635.2.
XP_006235734.1. XM_006235672.1.
UniGeneRn.100353.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3K9VX-ray2.50A/B34-514[»]
3K9YX-ray2.80A/B34-514[»]
ProteinModelPortalQ09128.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBQ09128.
ChEMBLCHEMBL3748.

Proteomic databases

PRIDEQ09128.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000046011; ENSRNOP00000043298; ENSRNOG00000013062.
GeneID25279.
KEGGrno:25279.

Organism-specific databases

CTD1591.
RGD2462. Cyp24a1.

Phylogenomic databases

eggNOGCOG2124.
GeneTreeENSGT00750000117435.
HOGENOMHOG000276540.
HOVERGENHBG099053.
InParanoidQ09128.
KOK07436.
OMAQHDTLAE.
OrthoDBEOG7ZGX4B.
PhylomeDBQ09128.
TreeFamTF105094.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14357.
SABIO-RKQ09128.

Gene expression databases

GenevestigatorQ09128.

Family and domain databases

Gene3D1.10.630.10. 1 hit.
InterProIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002949. Cyt_P450_E_CYP24A_mit.
[Graphical view]
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR01238. MITP450CC24.
PR00385. P450.
SUPFAMSSF48264. SSF48264. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ09128.
NextBio605991.
PROQ09128.

Entry information

Entry nameCP24A_RAT
AccessionPrimary (citable) accession number: Q09128
Secondary accession number(s): Q498V4, Q63685
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references