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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   29-OCT-2014, entry version 144.
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; DOI=10.1089/dna.1987.6.529;
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;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
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. {ECO:0000250}.
CC   -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol
CC       from lanosterol: step 1/6.
CC   -!- SUBUNIT: Interacts with ERG28. {ECO:0000269|PubMed:15995173}.
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. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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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; 6-530.
DR   BioGrid; 36434; 239.
DR   DIP; DIP-7886N; -.
DR   IntAct; P10614; 68.
DR   MINT; MINT-1325794; -.
DR   STRING; 4932.YHR007C; -.
DR   MaxQB; P10614; -.
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   InParanoid; P10614; -.
DR   KO; K05917; -.
DR   OMA; DFTSMVT; -.
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:0070988; P:demethylation; IDA:GOC.
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. {ECO:0000255}.
FT   TRANSMEM     21     41       Helical. {ECO:0000255}.
FT   TOPO_DOM     42    530       Cytoplasmic. {ECO:0000255}.
FT   METAL       470    470       Iron (heme axial ligand). {ECO:0000250}.
FT   MOD_RES     458    458       Phosphoserine.
FT                                {ECO:0000269|PubMed:17330950}.
FT   CONFLICT    433    433       K -> N (in Ref. 2; AAA34546/AAA34547).
FT                                {ECO:0000305}.
FT   HELIX         9     23
FT   HELIX        27     49
FT   STRAND       53     55
FT   TURN         64     66
FT   HELIX        69     74
FT   HELIX        76     87
FT   STRAND       89     95
FT   STRAND       98    103
FT   HELIX       105    113
FT   TURN        117    119
FT   HELIX       122    134
FT   HELIX       144    155
FT   HELIX       160    180
FT   TURN        182    184
FT   TURN        186    188
FT   STRAND      190    195
FT   HELIX       196    212
FT   HELIX       215    220
FT   HELIX       225    234
FT   HELIX       238    242
FT   HELIX       249    274
FT   STRAND      280    282
FT   HELIX       283    289
FT   HELIX       301    331
FT   HELIX       334    347
FT   HELIX       349    351
FT   HELIX       357    360
FT   HELIX       364    376
FT   STRAND      383    387
FT   STRAND      405    408
FT   HELIX       410    413
FT   TURN        417    419
FT   TURN        421    424
FT   HELIX       428    431
FT   STRAND      444    449
FT   STRAND      451    454
FT   HELIX       466    468
FT   HELIX       473    490
FT   STRAND      491    494
FT   STRAND      507    510
FT   STRAND      518    525
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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