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O46658 (CP2DP_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Vitamin D(3) 25-hydroxylase

EC=1.14.13.15
Alternative name(s):
CYPIID25
Cytochrome P450 2D25
Gene names
Name:CYP2D25
OrganismSus scrofa (Pig) [Complete proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the first step in the metabolic activation of vitamin D3 into 1-alpha,25-dihydroxyvitamin D3, its active, hormonal form.

Catalytic activity

5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol + NADPH + O2 = (25R)-5-beta-cholestane-3-alpha,7-alpha,12-alpha,26-tetraol + NADP+ + H2O.

Cofactor

Heme group By similarity.

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.

Tissue specificity

Found in liver and kidney.

Sequence similarities

Belongs to the cytochrome P450 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1 Ref.2 Ref.3
Chain2 – 500499Vitamin D(3) 25-hydroxylase
PRO_0000051745

Sites

Metal binding4461Iron (heme axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
O46658 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: F1C878A02C44503D

FASTA50056,512
        10         20         30         40         50         60 
MGLLTGDLLG ILALAMVIFL LLVDLMHRRS RWAPRYPPGP MPLPGLGNLL QVNFQDPRLS 

        70         80         90        100        110        120 
FIQLRRRFGD VFSLQQIWRP VVVLNGLAAV REALVSHSHE TSDRPPVFIL EHLGYGPRSE 

       130        140        150        160        170        180 
GVILARYGKA WREQRRFSVS TLRNFGLGKK SLEEWVTQEA SCLCAAFADQ AGRPFSPNNL 

       190        200        210        220        230        240 
LNKAVSNVIA SLTFARRFEY NDPRMLKLLD LVLEGLKEEV GLMRQVLEAM PVLRHIPGLC 

       250        260        270        280        290        300 
AKLFPRQKAF LVMIDELITE HKMTRDLAQP PRDLTDAFLD EMKEAKGNPE SSFNDENLRL 

       310        320        330        340        350        360 
VVAHLFSAGM ITTSTTLAWA LLLMILHPDV QRRVQQEIDE VIGHVRQPEI KDQALMPFTL 

       370        380        390        400        410        420 
AVLHEVQRFG DIVPLGVAHM TSCDIEVQGF LIPKGTTLIT NLTSVLKDET VWKKPFRFYP 

       430        440        450        460        470        480 
EHFLDAQGRF TKQEAFMPFS AGRRSCLGEP LARMELFLFF TTLLQAFSFS VPTGQPCPSD 

       490        500 
HGVFAFLLFP SPYQLCAVPR 

« Hide

References

[1]"Cloning, structure, and expression of a cDNA encoding vitamin D3 25-hydroxylase."
Postlind H., Axen E., Bergman T., Wikvall K.
Biochem. Biophys. Res. Commun. 241:491-497(1997) [PubMed: 9425298] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-57; 249-273 AND 408-430.
Tissue: Liver.
[2]"Purification and characterization of a vitamin D3 25-hydroxylase from pig liver microsomes."
Axen E., Bergman T., Wikvall K.
Biochem. J. 287:725-731(1992) [PubMed: 1445236] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-17.
Tissue: Liver.
[3]"Purification and characterization of cytochrome P-45014DM (lanosterol 14 alpha-demethylase) from pig liver microsomes."
Sono H., Sonoda Y., Sato Y.
Biochim. Biophys. Acta 1078:388-394(1991) [PubMed: 1859829] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-11.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y16417 mRNA. Translation: CAA76205.1.
PIRJC5819.
RefSeqNP_999559.1. NM_214394.1.
UniGeneSsc.55051.

3D structure databases

ProteinModelPortalO46658.
SMRO46658. Positions 37-500.
ModBaseSearch...

Protein-protein interaction databases

STRINGO46658.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID397687.
KEGGssc:397687.

Organism-specific databases

CTD397687.

Phylogenomic databases

HOVERGENHBG015789.
OrthoDBEOG40VVPH.

Family and domain databases

InterProIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
IPR008069. Cyt_P450_E_grp-I_CYP2D-like.
[Graphical view]
Gene3DG3DSA:1.10.630.10. Cyt_P450. 1 hit.
KOK07414.
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00463. EP450I.
PR01686. EP450ICYP2D.
PR00385. P450.
SUPFAMSSF48264. Cytochrome_P450. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCP2DP_PIG
AccessionPrimary (citable) accession number: O46658
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 23, 2007
Last modified: November 16, 2011
This is version 79 of the entry and version 3 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