ID   CP27B_MOUSE             Reviewed;         507 AA.
AC   O35084;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   16-JUN-2009, entry version 69.
DE   RecName: Full=25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial;
DE            EC=1.14.13.13;
DE   AltName: Full=Cytochrome P450 subfamily XXVIIB polypeptide 1;
DE   AltName: Full=Cytochrome p450 27B1;
DE   AltName: Full=Calcidiol 1-monooxygenase;
DE   AltName: Full=25-OHD-1 alpha-hydroxylase;
DE   AltName: Full=25-hydroxyvitamin D(3) 1-alpha-hydroxylase;
DE            Short=VD3 1A hydroxylase;
DE   AltName: Full=P450C1 alpha;
DE   AltName: Full=P450VD1-alpha;
DE   Flags: Precursor;
GN   Name=Cyp27b1; Synonyms=Cyp27b, Cyp40;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RX   MEDLINE=97442536; PubMed=9295274; DOI=10.1126/science.277.5333.1827;
RA   Takeyama K., Kitanaka S., Sato T., Kobori M., Yanagisawa J., Kato S.;
RT   "25-hydroxyvitamin D3 1alpha-hydroxylase and vitamin D synthesis.";
RL   Science 277:1827-1830(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=129;
RA   Kimmel-Jehan C., DeLuca H.F.;
RT   "Cloning of the mouse 25-hydroxyvitamin D3 1-alpha hydroxylase gene.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   MEDLINE=21024197; PubMed=11149489; DOI=10.1359/jbmr.2001.16.1.46;
RA   Panda D.K., Al-Kawas S., Seldin M.F., Hendy G.N., Goltzman D.;
RT   "25-hydroxyvitamin D 1alpha-hydroxylase: structure of the mouse gene,
RT   chromosomal assignment, and developmental expression.";
RL   J. Bone Miner. Res. 16:46-56(2001).
CC   -!- FUNCTION: Catalyzes the conversion of 25-hydroxyvitamin D3
CC       (25(OH)D) to 1-alpha,25-dihydroxyvitamin D3 (1,25(OH)2D) plays an
CC       important role in normal bone growth, calcium metabolism, and
CC       tissue differentiation.
CC   -!- CATALYTIC ACTIVITY: Calcidiol + NADPH + O(2) = calcitriol +
CC       NADP(+) + H(2)O.
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- PATHWAY: Hormone biosynthesis; cholecalciferol biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane.
CC   -!- TISSUE SPECIFICITY: Kidney.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR   EMBL; AB006034; BAA22434.1; ALT_INIT; mRNA.
DR   EMBL; AF235021; AAK15024.1; -; Genomic_DNA.
DR   EMBL; AF286219; AAG44889.1; -; Genomic_DNA.
DR   IPI; IPI00126549; -.
DR   UniGene; Mm.6216; -.
DR   HSSP; P00189; 1SCC.
DR   Ensembl; ENSMUSG00000006724; Mus musculus.
DR   MGI; MGI:1098274; Cyp27b1.
DR   HOGENOM; O35084; -.
DR   HOVERGEN; O35084; -.
DR   BRENDA; 1.14.13.13; 244.
DR   ArrayExpress; O35084; -.
DR   Bgee; O35084; -.
DR   GermOnline; ENSMUSG00000006724; Mus musculus.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004498; F:calcidiol 1-monooxygenase activity; IDA:UniProtKB.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0033280; P:response to vitamin D; IDA:UniProtKB.
DR   GO; GO:0042369; P:vitamin D catabolic process; IDA:UniProtKB.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017973; Cyt_P450_C.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   Gene3D; G3DSA:1.10.630.10; Cyt_P450; 1.
DR   PANTHER; PTHR19383; Cyt_P450; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Heme; Iron; Membrane; Metal-binding; Mitochondrion; Monooxygenase;
KW   NADP; Oxidoreductase; Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    507       25-hydroxyvitamin D-1 alpha hydroxylase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000003623.
FT   METAL       454    454       Iron (heme axial ligand) (By similarity).
SQ   SEQUENCE   507 AA;  56225 MW;  0669B4478C461B83 CRC64;
     MTQAVKLASR VFHRIHLPLQ LDASLGSRGS ESVLRSLSDI PGPSTLSFLA ELFCKGGLSR
     LHELQVHGAA RYGPIWSGSF GTLRTVYVAD PTLVEQLLRQ ESHCPERCSF SSWAEHRRRH
     QRACGLLTAD GEEWQRLRSL LAPLLLRPQA AAGYAGTLDN VVRDLVRRLR RQRGRGSGLP
     GLVLDVAGEF YKFGLESIGA VLLGSRLGCL EAEVPPDTET FIHAVGSVFV STLLTMAMPN
     WLHHLIPGPW ARLCRDWDQM FAFAQRHVEL REGEAAMRNQ GKPEEDMPSG HHLTHFLFRE
     KVSVQSIVGN VTELLLAGVD TVSNTLSWTL YELSRHPDVQ TALHSEITAG TRGSCAHPHG
     TALSQLPLLK AVIKEVLRLY PVVPGNSRVP DRDIRVGNYV IPQDTLVSLC HYATSRDPTQ
     FPDPNSFNPA RWLGEGPTPH PFASLPFGFG KRSCIGRRLA ELELQMALSQ ILTHFEVLPE
     PGALPIKPMT RTVLVPERSI NLQFVDR
//