ID   CP51A_BOVIN             Reviewed;         502 AA.
AC   Q4PJW3; A6QPJ2; Q3YM99;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   16-JUN-2009, entry version 33.
DE   RecName: Full=Lanosterol 14-alpha demethylase;
DE            Short=LDM;
DE            EC=1.14.13.70;
DE   AltName: Full=Cytochrome P450 51A1;
DE   AltName: Full=CYPLI;
DE   AltName: Full=P450LI;
DE   AltName: Full=Sterol 14-alpha demethylase;
DE   AltName: Full=P450-14DM;
DE            Short=P45014DM;
GN   Name=CYP51A1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   PubMed=15836952; DOI=10.1016/j.mce.2004.11.009;
RA   Rozman D., Seliskar M., Cotman M., Fink M.;
RT   "Pre-cholesterol precursors in gametogenesis.";
RL   Mol. Cell. Endocrinol. 234:47-56(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16508140; DOI=10.1248/bpb.29.430;
RA   Wang F., Shen Y., Song X., Xia G., Chen X., Zhou B., Lei L.;
RT   "cDNA cloning, genomic structure and expression analysis of the bovine
RT   lanosterol 14alpha-demethylase (CYP51) in gonads.";
RL   Biol. Pharm. Bull. 29:430-436(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal medulla;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes C14-demethylation of lanosterol; it transforms
CC       lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol.
CC   -!- CATALYTIC ACTIVITY: Obtusifoliol + 3 O(2) + 3 NADPH = 4-alpha-
CC       methyl-5-alpha-ergosta-8,14,24(28)-trien-3-beta-ol + formate + 3
CC       NADP(+) + 4 H(2)O.
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol
CC       from lanosterol: step 1/6.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane (By
CC       similarity). Microsome membrane (By similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR   EMBL; DQ078267; AAY82452.1; -; mRNA.
DR   EMBL; DQ085625; AAZ74630.1; -; mRNA.
DR   EMBL; BC149346; AAI49347.1; -; mRNA.
DR   IPI; IPI00705027; -.
DR   RefSeq; NP_001020490.1; -.
DR   UniGene; Bt.49631; -.
DR   Ensembl; ENSBTAG00000001992; Bos taurus.
DR   GeneID; 505060; -.
DR   KEGG; bta:505060; -.
DR   HOVERGEN; Q4PJW3; -.
DR   BRENDA; 1.14.13.70; 251.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005792; C:microsome; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0008398; F:sterol 14-demethylase activity; IEA:EC.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017973; Cyt_P450_C.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR   Gene3D; G3DSA:1.10.630.10; Cyt_P450; 1.
DR   PANTHER; PTHR19383; Cyt_P450; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   PRINTS; PR00385; P450.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Cholesterol biosynthesis; Endoplasmic reticulum; Heme; Iron;
KW   Lipid synthesis; Membrane; Metal-binding; Microsome; Monooxygenase;
KW   NADP; Oxidoreductase; Steroid biosynthesis; Sterol biosynthesis;
KW   Transmembrane.
FT   CHAIN         1    502       Lanosterol 14-alpha demethylase.
FT                                /FTId=PRO_0000051997.
FT   TRANSMEM     22     42       Potential.
FT   METAL       448    448       Iron (heme axial ligand) (By similarity).
SQ   SEQUENCE   502 AA;  56596 MW;  5D1C5AFA43E067A1 CRC64;
     MLDLLQAGGS VLGQAMEQVT GGNLASMLLI ACAFTLSLVY LFRLAVGHLA PPLPTGAKSP
     PYIVSPIPFL GHAIAFGKSP IEFLEDAYEK YGPVFSFTMV GKTFTYLLGS EAAALLFNSK
     NEDLNAEEVY SRLTTPVFGK GVAYDVPNTV FLEQKKMLKS GLNIAHFRQH VSIIEKETKE
     YFKSWGESGE KNLFEALSEL IILTASHCLH GKEIRSQLNE KVAQLYADLD GGFSHAAWLL
     PGWLPLPSFR RRDRAHREIK NIFYKAIQKR RESGEKIDDI LQTLLESTYK DGRPLTDDEV
     AGMLIGLLLA GQHTSSTTSA WMGFFLARDK TLQEKCFLEQ KTVCGENLPP LTYDQLKDLN
     LLDRCIKETL RLRPPIMTMM RLAKTPLTVA GYTIPPGHQV CVSPTVNQRL KDSWVERLDF
     NPDRYLEDSP ASGEKFAYVP FGAGRHRCIG ENFAYVQIKT IWSTMLRLYE FDLIDGYFPT
     VNYTTMIHTP EKPIIRYKRR SK
//