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UniProtKB/Swiss-Prot entry O35084

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CP27B_MOUSE
Primary accession number O35084
Secondary accession numbers None
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on July 15, 1998 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 62)
Name and origin of the protein
Protein name 25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial [Precursor]
Synonyms 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, Cyp40
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
DOI=10.1126/science.277.5333.1827; PubMed=9295274 [NCBI, ExPASy, EBI, Israel, Japan]
Takeyama K., Kitanaka S., Sato T., Kobori M., Yanagisawa J., Kato S.;
"25-Hydroxyvitamin D3 1alpha-hydroxylase and vitamin D synthesis.";
Science 277:1827-1827(1997).
[2]
 NUCLEOTIDE SEQUENCE.
STRAIN=129;
Kimmel-Jehan C., DeLuca H.F.;
"Cloning of the mouse 25-hydroxyvitamin D3 1-alpha hydroxylase gene.";
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[3]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/SvJ;
PubMed=11149489 [NCBI, ExPASy, EBI, Israel, Japan]
Panda D.K., Al-Kawas S., Seldin M.F., Hendy G.N., Goltzman D.;
"25-hydroxyvitamin D 1alpha-hydroxylase: structure of the mouse gene, chromosomal assignment, and developmental expression.";
J. Bone Miner. Res. 16:46-56(2001).
Comments
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
AB006034; BAA22434.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF235021; AAK15024.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF286219; AAG44889.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
UniGene Mm.6216
3D structure databases
HSSP P00189; 1SCC. [HSSP ENTRY / PDB]
ModBase O35084.
Organism-specific databases
MGI MGI:1098274; Cyp27b1.
Gene expression databases
ArrayExpress O35084; -.
GermOnline ENSMUSG00000006724; Mus musculus.
Ontologies
GO
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).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037; Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0006816; Biological process: calcium ion transport (inferred from mutant phenotype from MGI).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.
Genome annotation databases
Ensembl ENSMUSG00000006724; Mus musculus. [Contig view]
Phylogenomic databases
HOGENOM O35084; -.
HOVERGEN O35084; -.
Other
SOURCE Cyp27b1; Mus musculus.
ProtoNet O35084.
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
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1     ?        Mitochondrion (Potential). 
CHAIN   ?   507        25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial. PRO_0000003623
METAL   454   454        Iron (heme axial ligand) (By similarity). 
Sequence information
Length: 507 AA [This is the length of the unprocessed precursor] Molecular weight: 56225 Da [This is the MW of the unprocessed precursor] CRC64: 0669B4478C461B83 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTQAVKLASR VFHRIHLPLQ LDASLGSRGS ESVLRSLSDI PGPSTLSFLA ELFCKGGLSR 

        70         80         90        100        110        120 
LHELQVHGAA RYGPIWSGSF GTLRTVYVAD PTLVEQLLRQ ESHCPERCSF SSWAEHRRRH 

       130        140        150        160        170        180 
QRACGLLTAD GEEWQRLRSL LAPLLLRPQA AAGYAGTLDN VVRDLVRRLR RQRGRGSGLP 

       190        200        210        220        230        240 
GLVLDVAGEF YKFGLESIGA VLLGSRLGCL EAEVPPDTET FIHAVGSVFV STLLTMAMPN 

       250        260        270        280        290        300 
WLHHLIPGPW ARLCRDWDQM FAFAQRHVEL REGEAAMRNQ GKPEEDMPSG HHLTHFLFRE 

       310        320        330        340        350        360 
KVSVQSIVGN VTELLLAGVD TVSNTLSWTL YELSRHPDVQ TALHSEITAG TRGSCAHPHG 

       370        380        390        400        410        420 
TALSQLPLLK AVIKEVLRLY PVVPGNSRVP DRDIRVGNYV IPQDTLVSLC HYATSRDPTQ 

       430        440        450        460        470        480 
FPDPNSFNPA RWLGEGPTPH PFASLPFGFG KRSCIGRRLA ELELQMALSQ ILTHFEVLPE 

       490        500 
PGALPIKPMT RTVLVPERSI NLQFVDR
O35084 in FASTA format

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