ID   CP27B_RAT               Reviewed;         501 AA.
AC   O35132; O35076;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   16-JUN-2009, entry version 67.
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;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley;
RX   MEDLINE=97472245; PubMed=9333115; DOI=10.1359/jbmr.1997.12.10.1552;
RA   St Arnaud R., Messerlian S., Moir J.M., Omdahl J.L., Glorieux F.H.;
RT   "The 25-hydroxyvitamin D 1-alpha-hydroxylase gene maps to the
RT   pseudovitamin D-deficiency rickets (PDDR) disease locus.";
RL   J. Bone Miner. Res. 12:1552-1559(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RX   MEDLINE=98058745; PubMed=9371776; DOI=10.1073/pnas.94.24.12920;
RA   Shinki T., Shimada H., Wakino S., Anazawa H., Hayashi M., Saruta T.,
RA   Deluca H.F., Suda T.;
RT   "Cloning and expression of rat 25-hydroxyvitamin D3-1alpha-hydroxylase
RT   cDNA.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:12920-12925(1997).
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; AF000139; AAB86461.1; -; mRNA.
DR   EMBL; AB001992; BAA23271.1; -; mRNA.
DR   IPI; IPI00206228; -.
DR   RefSeq; NP_446215.1; -.
DR   UniGene; Rn.10847; -.
DR   HSSP; P00189; 1SCC.
DR   GeneID; 114700; -.
DR   KEGG; rno:114700; -.
DR   RGD; 69192; Cyp27b1.
DR   HOVERGEN; O35132; -.
DR   BRENDA; 1.14.13.13; 248.
DR   NextBio; 618833; -.
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:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
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         ?    501       25-hydroxyvitamin D-1 alpha hydroxylase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000003624.
FT   METAL       448    448       Iron (heme axial ligand) (By similarity).
FT   CONFLICT     13     13       H -> D (in Ref. 1; AAB86461).
FT   CONFLICT     55     55       H -> D (in Ref. 1; AAB86461).
FT   CONFLICT    103    112       FSSWSEHRRR -> SHLGQSTVAS (in Ref. 1;
FT                                AAB86461).
FT   CONFLICT    119    119       L -> W (in Ref. 1; AAB86461).
FT   CONFLICT    129    144       RLRSLLAPLLLRPQAA -> EAPKSPGPASPPTSSS (in
FT                                Ref. 1; AAB86461).
FT   CONFLICT    201    201       G -> R (in Ref. 1; AAB86461).
FT   CONFLICT    251    251       D -> N (in Ref. 1; AAB86461).
FT   CONFLICT    288    288       H -> D (in Ref. 1; AAB86461).
FT   CONFLICT    305    305       T -> R (in Ref. 1; AAB86461).
FT   CONFLICT    372    374       RLY -> MLD (in Ref. 1; AAB86461).
SQ   SEQUENCE   501 AA;  55369 MW;  B0A85286A219EA0E CRC64;
     MTQAVKLASR VFHRVQLPSQ LGSDSVLRSL SDIPGPSTPS FLAELFCKGG LSRLHELQVH
     GAARYGPIWS GSFGTLRTVY VADPALVEQL LRQESHCPER CSFSSWSEHR RRHQRACGLL
     TADGEEWQRL RSLLAPLLLR PQAAAGYAGT LDSVVSDLVR RLRRQRGRGS GLPDLVLDVA
     GEFYKFGLEG IGAVLLGSRL GCLEAEVPPD TETFIEAVGS VFVSTLLTMA MPSWLHRLIP
     GPWARLCRDW DQMFAFAQKH VEQREGEAAV RNQGKPEEDL PTGHHLTHFL FREKVSVQSI
     VGNVTELLLA GVDTVSNTLS WALYELSRHP EVQSALHSEI TGAVNPGSYA HLQATALSQL
     PLLKAVIKEV LRLYPVVPGN SRVPDRDICV GNYVIPQDTL VSLCHYATSR DPAQFREPNS
     FNPARWLGEG PAPHPFASLP FGFGKRSCIG RRLAELELQM ALAQILTHFE VLPEPGALPV
     KPMTRTVLVP ERSIHLQFVD R
//