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Reviewed, UniProtKB/Swiss-Prot O35132 (CP27B_RAT)

Last modified June 16, 2009. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial
    EC=1.14.13.13
Alternative name(s):
    Cytochrome P450 subfamily XXVIIB polypeptide 1
    Cytochrome p450 27B1
    Calcidiol 1-monooxygenase
    25-OHD-1 alpha-hydroxylase
    25-hydroxyvitamin D(3) 1-alpha-hydroxylase
      Short name=VD3 1A hydroxylase
    P450C1 alpha
    P450VD1-alpha
Gene names
Name: Cyp27b1
Synonyms: Cyp27b
OrganismRattus norvegicus (Rat)
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.

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
O35132-1 [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: 9333115] [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: 9371776] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

AF000139 mRNA. Translation: AAB86461.1.
AB001992 mRNA. Translation: BAA23271.1.
IPIIPI00206228.
RefSeqNP_446215.1.
UniGeneRn.10847

3D structure databases

HSSPHSSP built from PDB template 1SCC based on UniProtKB P00189.
ModBaseSearch...

Genome annotation databases

GeneID114700.
KEGGrno:114700.

Organism-specific databases

RGD69192. Cyp27b1.

Phylogenomic databases

HOVERGENO35132.

Enzyme and pathway databases

BRENDA1.14.13.13. 248.

Family and domain databases

InterProIPR001128. Cyt_P450.
IPR017973. Cyt_P450_C.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
Gene3DG3DSA:1.10.630.10. Cyt_P450. 1 hit.
PANTHERPTHR19383. Cyt_P450. 1 hit.
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00463. EP450I.
PR00385. P450.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

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: June 16, 2009
This is version 67 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents