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O35132 (CP27B_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. 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:
25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial

EC=1.14.13.13
Alternative name(s):
25-OHD-1 alpha-hydroxylase
25-hydroxyvitamin D(3) 1-alpha-hydroxylase
Short name=VD3 1A hydroxylase
Calcidiol 1-monooxygenase
Cytochrome P450 subfamily XXVIIB polypeptide 1
Cytochrome P450C1 alpha
Cytochrome P450VD1-alpha
Cytochrome p450 27B1
Gene names
Name:Cyp27b1
Synonyms:Cyp27b
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length501 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (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.

Sequence similarities

Belongs to the cytochrome P450 family.

Ontologies

Keywords
   Cellular componentMembrane
Mitochondrion
   DomainTransit peptide
   LigandHeme
Iron
Metal-binding
NADP
   Molecular functionMonooxygenase
Oxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from direct assay PubMed 3496213. Source: RGD

calcitriol biosynthetic process from calciol

Inferred from direct assay Ref.1Ref.2. Source: GOC

lactation

Inferred from expression pattern PubMed 8333523. Source: RGD

response to cAMP

Inferred from direct assay PubMed 6282936. Source: RGD

response to calcium ion

Inferred from expression pattern PubMed 8333523. Source: RGD

response to copper ion

Inferred from direct assay PubMed 3348368. Source: RGD

response to drug

Inferred from direct assay PubMed 3937586. Source: RGD

response to insulin

Inferred from direct assay PubMed 3295473. Source: RGD

response to peptide hormone

Inferred from expression pattern PubMed 10393981PubMed 17223550. Source: RGD

response to prostaglandin E

Inferred from direct assay PubMed 3937586. Source: RGD

response to vitamin D

Inferred from direct assay PubMed 3000565. Source: RGD

vitamin D catabolic process

Inferred from direct assay Ref.1. Source: BHF-UCL

vitamin D metabolic process

Inferred from direct assay Ref.2. Source: RGD

   Cellular_componentmitochondrial membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 9426217. Source: RGD

   Molecular_functioncalcidiol 1-monooxygenase activity

Inferred from direct assay Ref.1. Source: BHF-UCL

heme binding

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 50125-hydroxyvitamin D-1 alpha hydroxylase, mitochondrialPRO_0000003624

Sites

Metal binding4481Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict131H → D in AAB86461. Ref.1
Sequence conflict551H → D in AAB86461. Ref.1
Sequence conflict103 – 11210FSSWSEHRRR → SHLGQSTVAS in AAB86461. Ref.1
Sequence conflict1191L → W in AAB86461. Ref.1
Sequence conflict129 – 14416RLRSL…RPQAA → EAPKSPGPASPPTSSS in AAB86461. Ref.1
Sequence conflict2011G → R in AAB86461. Ref.1
Sequence conflict2511D → N in AAB86461. Ref.1
Sequence conflict2881H → D in AAB86461. Ref.1
Sequence conflict3051T → R in AAB86461. Ref.1
Sequence conflict372 – 3743RLY → MLD in AAB86461. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O35132 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: B0A85286A219EA0E

FASTA50155,369
        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 

« Hide

References

[1]"The 25-hydroxyvitamin D 1-alpha-hydroxylase gene maps to the pseudovitamin D-deficiency rickets (PDDR) disease locus."
St Arnaud R., Messerlian S., Moir J.M., Omdahl J.L., Glorieux F.H.
J. Bone Miner. Res. 12:1552-1559(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
[2]"Cloning and expression of rat 25-hydroxyvitamin D3-1alpha-hydroxylase cDNA."
Shinki T., Shimada H., Wakino S., Anazawa H., Hayashi M., Saruta T., Deluca H.F., Suda T.
Proc. Natl. Acad. Sci. U.S.A. 94:12920-12925(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF000139 mRNA. Translation: AAB86461.1.
AB001992 mRNA. Translation: BAA23271.1.
RefSeqNP_446215.1. NM_053763.1.
UniGeneRn.10847.

3D structure databases

ProteinModelPortalO35132.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid250405. 1 interaction.

Proteomic databases

PRIDEO35132.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID114700.
KEGGrno:114700.

Organism-specific databases

CTD1594.
RGD69192. Cyp27b1.

Phylogenomic databases

HOVERGENHBG106909.
KOK07438.
PhylomeDBO35132.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14354.
UniPathwayUPA00955.

Gene expression databases

GenevestigatorO35132.

Family and domain databases

Gene3D1.10.630.10. 1 hit.
InterProIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00463. EP450I.
PR00385. P450.
SUPFAMSSF48264. SSF48264. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio618833.

Entry information

Entry nameCP27B_RAT
AccessionPrimary (citable) accession number: O35132
Secondary accession number(s): O35076
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: April 16, 2014
This is version 96 of the entry and version 2 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

PATHWAY comments

Index of metabolic and biosynthesis pathways