Vitamin D(3) 25-hydroxylase - Sus scrofa (Pig)

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Reviewed, UniProtKB/Swiss-Prot O46658 (CP2DP_PIG)

Last modified January 19, 2010. Version 67. History...

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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 names

Recommended name:
    Vitamin D(3) 25-hydroxylase
    EC=1.14.13.15
Alternative name(s):
    Cytochrome P450 2D25
    CYPIID25

Gene names

Name:

CYP2D25

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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Protein attributes

Sequence length	500 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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.

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Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Ligand	Heme Iron Metal-binding NADP
Molecular function	Monooxygenase Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microsome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	cholestanetriol 26-monooxygenase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.1 Ref.2 Ref.3

Chain

2 – 500

499

Vitamin D(3) 25-hydroxylase

PRO_0000051745

Sites

Metal binding

446

Iron (heme axial ligand) By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

O46658-1 [UniParc].

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

500

56,512

        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

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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.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	Y16417 mRNA. Translation: CAA76205.1.
PIR	JC5819.
RefSeq	NP_999559.1.
UniGene	Ssc.55051
3D structure databases
SMR	O46658. Positions 37-500.
ModBase	Search...
Genome annotation databases
Ensembl	ENSSSCT00000000050; ENSSSCP00000000050; ENSSSCG00000000046; Sus scrofa. [Genome view]
GeneID	397687.
KEGG	ssc:397687.
Organism-specific databases
CTD	397687.
Phylogenomic databases
HOVERGEN	O46658.
Family and domain databases
InterPro	IPR001128. Cyt_P450. IPR017973. Cyt_P450_C. IPR017972. Cyt_P450_CS. IPR002401. Cyt_P450_E_grp-I. IPR008069. Cyt_P450_E_grp-I_CYP2D-like. [Graphical view]
Gene3D	G3DSA:1.10.630.10. Cyt_P450. 1 hit.
PANTHER	PTHR19383. Cyt_P450. 1 hit.
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00463. EP450I. PR01686. EP450ICYP2D. PR00385. P450.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

CP2DP_PIG

Accession

Primary (citable) accession number: O46658

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	January 23, 2007
Last modified:	January 19, 2010
This is version 67 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents