ID   CP51A_PIG               Reviewed;         503 AA.
AC   O46420;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   16-JUN-2009, entry version 66.
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; Synonyms=CYP51;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Kojima M., Morozumi T., Hamasima N., Okamoto T.;
RT   "Cloning of a pig lanosterol 14-demethylase cDNA.";
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=20250839; PubMed=10788789;
RA   Kojima M., Morozumi T., Onishi A., Mitsuhashi T.;
RT   "Structure of the pig sterol 14 alpha-demethylase (CYP51) gene and its
RT   expression in the testis and other tissues.";
RL   J. Biochem. 127:805-811(2000).
CC   -!- FUNCTION: Catalyzes C14-demethylation of lanosterol; it transforms
CC       lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol
CC       (By similarity).
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 (Potential).
CC       Microsome membrane (Potential).
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR   EMBL; AB009988; BAA24134.1; -; mRNA.
DR   EMBL; AB042982; BAA96092.1; -; Genomic_DNA.
DR   PIR; JC7243; JC7243.
DR   RefSeq; NP_999597.1; -.
DR   UniGene; Ssc.5712; -.
DR   HSSP; P77901; 1E9X.
DR   GeneID; 403334; -.
DR   KEGG; ssc:403334; -.
DR   HOVERGEN; O46420; -.
DR   BRENDA; 1.14.13.70; 249.
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    503       Lanosterol 14-alpha demethylase.
FT                                /FTId=PRO_0000051999.
FT   TRANSMEM     24     44       Potential.
FT   METAL       449    449       Iron (heme axial ligand) (By similarity).
SQ   SEQUENCE   503 AA;  56867 MW;  0302949CE461AFD6 CRC64;
     MVLLGLLQAG GSVLGQAMEQ VTGVNLLSSL LLACAFTLIL VYLFRQAIGH LAPLPAGAKS
     PPYIFSPIPF LGHAIAFGKS PIEFLENAYE KYGPVFSFTM VGKTFTYLLG SDAAALLFNS
     KNEDLNAEDV YSRLTTPVFG KGVAYDVPNP VFLEQKKMLK SGLNIAHFRQ HVSIIEKETK
     EYFQSWGESG ERNLFEALSE LIILTASHCL HGKEIRSQLN EKVAQLYADL DGGFSHAAWL
     LPGWLPLPSF RRRDRAHREI KNIFYKAIQK RRQSEEKIDD ILQTLLDSTY KDGRPLTDDE
     VAGMLIGLLL AGQHTSSTTS AWMGFFLARD KTLQEKCYLE QKTVCGEDLP PLTYDQLKDL
     NLLDRCIKET LRLRPPIMTM MRMAKTPQTV AGYTIPPGHQ VCVSPTVNQR LKDSWVERLD
     FNPDRYLQDN PASGEKFAYV PFGAGRHRCI GENFAYVQIK TIWSTMLRLY EFDLIDGYFP
     TVNYTTMIHT PENPVIRYKR RSK
//