ID   CP27A_RABIT             Reviewed;         535 AA.
AC   P17177;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   25-NOV-2008, entry version 63.
DE   RecName: Full=Cytochrome P450 27, mitochondrial;
DE            EC=1.14.13.15;
DE   AltName: Full=Cytochrome P-450C27/25;
DE   AltName: Full=Sterol 26-hydroxylase;
DE   AltName: Full=Sterol 27-hydroxylase;
DE   AltName: Full=Vitamin D(3) 25-hydroxylase;
DE   AltName: Full=5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol 27-hydroxylase;
DE   Flags: Precursor;
GN   Name=CYP27A1; Synonyms=CYP27;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=89255259; PubMed=2722778;
RA   Andersson S., Davis D.L., Dahlbaeck H., Joernvall H., Russell D.W.;
RT   "Cloning, structure, and expression of the mitochondrial cytochrome P-
RT   450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme.";
RL   J. Biol. Chem. 264:8222-8229(1989).
CC   -!- FUNCTION: Catalyzes the first step in the oxidation of the side
CC       chain of sterol intermediates; the 27-hydroxylation of 5-beta-
CC       cholestane-3-alpha,7-alpha,12-alpha-triol. Has also a vitamin D3-
CC       25-hydroxylase activity.
CC   -!- CATALYTIC ACTIVITY: 5-beta-cholestane-3-alpha,7-alpha,12-alpha-
CC       triol + NADPH + O(2) = (25R)-5-beta-cholestane-3-alpha,7-alpha,12-
CC       alpha,26-tetraol + NADP(+) + H(2)O.
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- PATHWAY: Hormone biosynthesis; cholecalciferol biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR   EMBL; J04717; AAA31225.1; -; mRNA.
DR   PIR; A33813; A33813.
DR   HSSP; P00189; 1SCC.
DR   Ensembl; ENSOCUG00000003377; Oryctolagus cuniculus.
DR   HOVERGEN; P17177; -.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0047749; F:cholestanetriol 26-monooxygenase activity; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001128; Cyt_P450.
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   Acetylation; Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW   Monooxygenase; NADP; Oxidoreductase; Transit peptide.
FT   TRANSIT       1     32       Mitochondrion (Probable).
FT   CHAIN        33    535       Cytochrome P450 27, mitochondrial.
FT                                /FTId=PRO_0000003620.
FT   REGION      387    401       Sterol-binding (Potential).
FT   METAL       480    480       Iron (heme axial ligand).
FT   MOD_RES     126    126       N6-acetyllysine (By similarity).
FT   MOD_RES     286    286       N6-acetyllysine (By similarity).
SQ   SEQUENCE   535 AA;  60255 MW;  CC44B9820E2FCCC2 CRC64;
     MAALGCARLR WALLGPRVAG CGLCPQGARA KAAIPTALPA DEAAQAPGAG PGDRRRRRSL
     EELPRLGQLR FFYQAFVQGY LLHLHKLQVL NKARYGPMWV SYLGPQLFVN LASAPLVETV
     MRQEGKYPVR NDMQLWKEHR DHQDLAYGVF TTDGHDWYQL RQALNQRLLK PAEAALYTDA
     LNEVIDSFVV RLDQLRAESA SGDQVPDMAD LLYHFALEAI CYILFEKRIG CLEASIPKDT
     ENFIRSVGLM FQNSVYVTFL PKWTRPLLPF WKRYLDGWDT IFSFGKNLID QKLQEVVAQL
     QSAGSDGVQV SGYLHSLLTS GQLSPREALG SLPELLLAGV DTTSNTLTWA LYHLSKNPEI
     QAALRKEVVG VVAAGQVPQH KDFAHMPLLK AVLKETLRLY PVIPANSRII VDKEIEVGGF
     LFPKNTQFVF CHYVTSRDPS TFSEPDTFWP YRWLRKGQPE TSKTQHPFGS VPFGYGVRAC
     LGRRIAELEM QLLLARLIQR YELMLAPETG EVQSVARIVL VPNKKVGLRF LPTQR
//