EC 1.14.13.13
Cytochrome P450 subfamily XXVIIB polypeptide 1
Cytochrome p450 27B1
Calcidiol 1-monooxygenase
25-OHD-1 alpha-hydroxylase
25-hydroxyvitamin D(3) 1-alpha-hydroxylase
VD3 1A hydroxylase
P450C1 alpha
P450VD1-alpha

Gene name

	Name:	Cyp27b1
	Synonyms:	Cyp27b

From

Rattus norvegicus (Rat)

[TaxID: 10116]

Taxonomy

Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.

Protein existence

2: Evidence at transcript level;

References

[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Sprague-Dawley; PubMed=9333115 [NCBI, ExPASy, EBI, Israel, Japan] St Arnaud R., Messerlian S., Moir J.M., Omdahl J.L., Glorieux F.H.; "The 25-hydroxyvitamin D 1-alpha-hydroxylase gene maps to the pseudovitamin D-deficiency rickets (PDDR) disease locus."; J. Bone Miner. Res. 12:1552-1559(1997).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Kidney; DOI=10.1073/pnas.94.24.12920; PubMed=9371776 [NCBI, ExPASy, EBI, Israel, Japan] Shinki T., Shimada H., Wakino S., Anazawa H., Hayashi M., Saruta T., Deluca H.F., Suda T.; "Cloning and expression of rat 25-hydroxyvitamin D3-1alpha-hydroxylase cDNA."; Proc. Natl. Acad. Sci. U.S.A. 94:12920-12925(1997).

Comments

FUNCTION: Catalyzes the conversion of 25-hydroxyvitamin D3 (25(OH)D) to 1-alpha,25-dihydroxyvitamin D3 (1,25(OH)2D) plays an important role in normal bone growth, calcium metabolism, and tissue differentiation.
CATALYTIC ACTIVITY: Calcidiol + NADPH + O₂ = calcitriol + NADP⁺ + H₂O.
COFACTOR: Heme group (By similarity).
PATHWAY: Hormone biosynthesis; cholecalciferol biosynthesis .
SUBCELLULAR LOCATION: Mitochondrion membrane.
TISSUE SPECIFICITY: Kidney.
SIMILARITY: Belongs to the cytochrome P450 family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF000139; AAB86461.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB001992; BAA23271.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_446215.1; -.

UniGene

Rn.10847

3D structure databases

HSSP

P00189; 1SCC. [HSSP ENTRY / PDB]

ModBase

O35132.

Organism-specific databases

RGD

69192; Cyp27b1.

Ontologies

GO:0031966;	Cellular component: mitochondrial membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004498;	Molecular function: calcidiol 1-monooxygenase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR001128; Cyt_P450.
IPR002401; Cyt_P450_E_grp-I.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.630.10; Cyt_P450; 1.

PANTHER

PTHR19383; Cyt_P450; 1.

Pfam

PF00067; p450; 1.
Pfam graphical view of domain structure.

PRINTS

PR00463; EP450I.
PR00385; P450.

PROSITE

PS00086; CYTOCHROME_P450; 1.

BLOCKS

O35132.

Genome annotation databases

GeneID

114700; -.

KEGG

rno:114700; -.

Phylogenomic databases

HOVERGEN

O35132; -.

Other

ProtoNet

O35132.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Heme; Iron; Membrane; Metal-binding; Mitochondrion; Monooxygenase; NADP; Oxidoreductase; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 ?`		`Mitochondrion (Potential).`
`CHAIN`	`? 501`		`25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial.`	`PRO_0000003624`
`METAL`	`448 448`		`Iron (heme axial ligand) (By similarity).`
`CONFLICT`	`13 13`		`H -> D (in Ref. 1; AAB86461).`
`CONFLICT`	`55 55`		`H -> D (in Ref. 1; AAB86461).`
`CONFLICT`	`103 112`		`FSSWSEHRRR -> SHLGQSTVAS (in Ref. 1; AAB86461).`
`CONFLICT`	`119 119`		`L -> W (in Ref. 1; AAB86461).`
`CONFLICT`	`129 144`		`RLRSLLAPLLLRPQAA -> EAPKSPGPASPPTSSS (in Ref. 1; AAB86461).`
`CONFLICT`	`201 201`		`G -> R (in Ref. 1; AAB86461).`
`CONFLICT`	`251 251`		`D -> N (in Ref. 1; AAB86461).`
`CONFLICT`	`288 288`		`H -> D (in Ref. 1; AAB86461).`
`CONFLICT`	`305 305`		`T -> R (in Ref. 1; AAB86461).`
`CONFLICT`	`372 374`		`RLY -> MLD (in Ref. 1; AAB86461).`

Sequence information

Length: 501 AA [This is the length of the unprocessed precursor]

Molecular weight: 55369 Da [This is the MW of the unprocessed precursor]

CRC64: B0A85286A219EA0E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTQAVKLASR VFHRVQLPSQ LGSDSVLRSL SDIPGPSTPS FLAELFCKGG LSRLHELQVH 

        70         80         90        100        110        120 
GAARYGPIWS GSFGTLRTVY VADPALVEQL LRQESHCPER CSFSSWSEHR RRHQRACGLL 

       130        140        150        160        170        180 
TADGEEWQRL RSLLAPLLLR PQAAAGYAGT LDSVVSDLVR RLRRQRGRGS GLPDLVLDVA 

       190        200        210        220        230        240 
GEFYKFGLEG IGAVLLGSRL GCLEAEVPPD TETFIEAVGS VFVSTLLTMA MPSWLHRLIP 

       250        260        270        280        290        300 
GPWARLCRDW DQMFAFAQKH VEQREGEAAV RNQGKPEEDL PTGHHLTHFL FREKVSVQSI 

       310        320        330        340        350        360 
VGNVTELLLA GVDTVSNTLS WALYELSRHP EVQSALHSEI TGAVNPGSYA HLQATALSQL 

       370        380        390        400        410        420 
PLLKAVIKEV LRLYPVVPGN SRVPDRDICV GNYVIPQDTL VSLCHYATSR DPAQFREPNS 

       430        440        450        460        470        480 
FNPARWLGEG PAPHPFASLP FGFGKRSCIG RRLAELELQM ALAQILTHFE VLPEPGALPV 

       490        500 
KPMTRTVLVP ERSIHLQFVD R

O35132 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools