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Entry: CP51_YEAST
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ID   CP51_YEAST              Reviewed;         530 AA.
AC   P10614; D3DKV1;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   19-MAR-2014, entry version 139.
DE   RecName: Full=Lanosterol 14-alpha demethylase;
DE            EC=1.14.13.70;
DE   AltName: Full=CYPLI;
DE   AltName: Full=Cytochrome P450 51;
DE   AltName: Full=Cytochrome P450-14DM;
DE   AltName: Full=Cytochrome P450-LIA1;
DE   AltName: Full=Sterol 14-alpha demethylase;
GN   Name=ERG11; Synonyms=CYP51; OrderedLocusNames=YHR007C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3322742;
RA   Kalb V.F., Woods C.W., Turi T.G., Dey C.R., Sutter T.R., Loper J.C.;
RT   "Primary structure of the P450 lanosterol demethylase gene from
RT   Saccharomyces cerevisiae.";
RL   DNA 6:529-537(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3046615; DOI=10.1016/S0006-291X(88)81087-8;
RA   Ishida N., Aoyama Y., Hatanaka R., Oyama Y., Imajo S., Ishiguro M.,
RA   Oshima T., Nakazato H., Noguchi T., Maitra U.S., Mohan V.P.,
RA   Sprinson D.B., Yoshida Y.;
RT   "A single amino acid substitution converts cytochrome P450(14DM) to an
RT   inactive form, cytochrome P450SG1: complete primary structures deduced
RT   from cloned DNAS.";
RL   Biochem. Biophys. Res. Commun. 155:317-323(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J.,
RA   Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J.,
RA   Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y.,
RA   Latreille P., Louis E.J., Macri C., Mardis E., Menezes S., Mouser L.,
RA   Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K.,
RA   Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R.,
RA   Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RG   Saccharomyces Genome Database;
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 444-530.
RX   PubMed=3542713; DOI=10.1016/0378-1119(86)90021-1;
RA   Kalb V.F., Loper J.C., Dey C.R., Woods C.W., Sutter T.R.;
RT   "Isolation of a cytochrome P-450 structural gene from Saccharomyces
RT   cerevisiae.";
RL   Gene 45:237-245(1986).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   INTERACTION WITH ERG28.
RX   PubMed=15995173; DOI=10.1194/jlr.M500153-JLR200;
RA   Mo C., Bard M.;
RT   "Erg28p is a key protein in the yeast sterol biosynthetic enzyme
RT   complex.";
RL   J. Lipid Res. 46:1991-1998(2005).
RN   [8]
RP   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA   Kim H., Melen K., Oesterberg M., von Heijne G.;
RT   "A global topology map of the Saccharomyces cerevisiae membrane
RT   proteome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22106047; DOI=10.1002/pmic.201100166;
RA   Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT   "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL   Proteomics 12:236-240(2012).
CC   -!- FUNCTION: Catalyzes C14-demethylation of lanosterol which is
CC       critical for ergosterol biosynthesis. It transforms lanosterol
CC       into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol.
CC   -!- CATALYTIC ACTIVITY: A 14-alpha-methylsteroid + 3 O(2) + 3 NADPH =
CC       a Delta(14)-steroid + formate + 3 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   -!- SUBUNIT: Interacts with ERG28.
CC   -!- INTERACTION:
CC       P53045:ERG25; NbExp=3; IntAct=EBI-5127, EBI-6506;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein.
CC   -!- MISCELLANEOUS: It is the main target for antifungal compounds of
CC       the triazole family like ketoconazole which inhibits by
CC       coordinating the iron atom at the sixth ligand position.
CC   -!- MISCELLANEOUS: Present with 73200 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR   EMBL; M18109; AAA34379.1; -; Genomic_DNA.
DR   EMBL; M15663; AAA34837.1; -; Genomic_DNA.
DR   EMBL; M21483; AAA34546.1; -; Genomic_DNA.
DR   EMBL; M21484; AAA34547.1; -; Genomic_DNA.
DR   EMBL; U10555; AAB68433.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06695.1; -; Genomic_DNA.
DR   PIR; A27491; A27491.
DR   RefSeq; NP_011871.1; NM_001179137.1.
DR   PDB; 4LXJ; X-ray; 1.90 A; A=1-530.
DR   PDBsum; 4LXJ; -.
DR   ProteinModelPortal; P10614; -.
DR   SMR; P10614; 52-525.
DR   BioGrid; 36434; 238.
DR   DIP; DIP-7886N; -.
DR   IntAct; P10614; 68.
DR   MINT; MINT-1325794; -.
DR   STRING; 4932.YHR007C; -.
DR   DrugBank; DB00257; Clotrimazole.
DR   DrugBank; DB01127; Econazole.
DR   DrugBank; DB00196; Fluconazole.
DR   DrugBank; DB01026; Ketoconazole.
DR   DrugBank; DB01263; Posaconazole.
DR   DrugBank; DB01153; Sertaconazole.
DR   DrugBank; DB00251; Terconazole.
DR   DrugBank; DB01007; Tioconazole.
DR   DrugBank; DB00582; Voriconazole.
DR   PaxDb; P10614; -.
DR   PeptideAtlas; P10614; -.
DR   EnsemblFungi; YHR007C; YHR007C; YHR007C.
DR   GeneID; 856398; -.
DR   KEGG; sce:YHR007C; -.
DR   CYGD; YHR007c; -.
DR   SGD; S000001049; ERG11.
DR   eggNOG; COG2124; -.
DR   GeneTree; ENSGT00660000095370; -.
DR   HOGENOM; HOG000042780; -.
DR   KO; K05917; -.
DR   OMA; FRENRAK; -.
DR   OrthoDB; EOG7712HB; -.
DR   BioCyc; MetaCyc:YHR007C-MONOMER; -.
DR   BioCyc; YEAST:YHR007C-MONOMER; -.
DR   UniPathway; UPA00770; UER00754.
DR   NextBio; 981925; -.
DR   PRO; PR:P10614; -.
DR   Genevestigator; P10614; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0008398; F:sterol 14-demethylase activity; IDA:SGD.
DR   GO; GO:0006696; P:ergosterol biosynthetic process; IMP:SGD.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Heme; Iron; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Metal-binding; Monooxygenase; NADP;
KW   Oxidoreductase; Phosphoprotein; Reference proteome;
KW   Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW   Sterol metabolism; Transmembrane; Transmembrane helix.
FT   CHAIN         1    530       Lanosterol 14-alpha demethylase.
FT                                /FTId=PRO_0000052012.
FT   TOPO_DOM      1     20       Extracellular (Potential).
FT   TRANSMEM     21     41       Helical; (Potential).
FT   TOPO_DOM     42    530       Cytoplasmic (Potential).
FT   METAL       470    470       Iron (heme axial ligand) (By similarity).
FT   MOD_RES     458    458       Phosphoserine.
FT   CONFLICT    433    433       K -> N (in Ref. 2; AAA34546/AAA34547).
SQ   SEQUENCE   530 AA;  60720 MW;  646960BBA0E17979 CRC64;
     MSATKSIVGE ALEYVNIGLS HFLALPLAQR ISLIIIIPFI YNIVWQLLYS LRKDRPPLVF
     YWIPWVGSAV VYGMKPYEFF EECQKKYGDI FSFVLLGRVM TVYLGPKGHE FVFNAKLADV
     SAEAAYAHLT TPVFGKGVIY DCPNSRLMEQ KKFVKGALTK EAFKSYVPLI AEEVYKYFRD
     SKNFRLNERT TGTIDVMVTQ PEMTIFTASR SLLGKEMRAK LDTDFAYLYS DLDKGFTPIN
     FVFPNLPLEH YRKRDHAQKA ISGTYMSLIK ERRKNNDIQD RDLIDSLMKN STYKDGVKMT
     DQEIANLLIG VLMGGQHTSA ATSAWILLHL AERPDVQQEL YEEQMRVLDG GKKELTYDLL
     QEMPLLNQTI KETLRMHHPL HSLFRKVMKD MHVPNTSYVI PAGYHVLVSP GYTHLRDEYF
     PNAHQFNIHR WNKDSASSYS VGEEVDYGFG AISKGVSSPY LPFGGGRHRC IGEHFAYCQL
     GVLMSIFIRT LKWHYPEGKT VPPPDFTSMV TLPTGPAKII WEKRNPEQKI
//
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