ID   CP51_SCHPO              Reviewed;         495 AA.
AC   Q09736;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   16-JUN-2009, entry version 70.
DE   RecName: Full=Lanosterol 14-alpha demethylase erg11;
DE            EC=1.14.13.70;
DE   AltName: Full=Cytochrome P450 51;
DE   AltName: Full=CYPLI;
DE   AltName: Full=P450-LIA1;
DE   AltName: Full=Sterol 14-alpha demethylase erg11;
DE   AltName: Full=P450-14DM;
DE   Flags: Precursor;
GN   Name=erg11; Synonyms=cyp51; ORFNames=SPAC13A11.02c;
OS   Schizosaccharomyces pombe (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   INDUCTION.
RX   PubMed=16537923; DOI=10.1128/MCB.26.7.2817-2831.2006;
RA   Todd B.L., Stewart E.V., Burg J.S., Hughes A.L., Espenshade P.J.;
RT   "Sterol regulatory element binding protein is a principal regulator of
RT   anaerobic gene expression in fission yeast.";
RL   Mol. Cell. Biol. 26:2817-2831(2006).
RN   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the
RT   fission yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH DAP1.
RX   PubMed=17276356; DOI=10.1016/j.cmet.2006.12.009;
RA   Hughes A.L., Powell D.W., Bard M., Eckstein J., Barbuch R., Link A.J.,
RA   Espenshade P.J.;
RT   "Dap1/PGRMC1 binds and regulates cytochrome P450 enzymes.";
RL   Cell Metab. 5:143-149(2007).
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 (By
CC       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   -!- SUBUNIT: Interacts with dap1.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum. Membrane; Multi-pass
CC       membrane protein (Potential).
CC   -!- INDUCTION: Up-regulated by sre1 in response to absence of oxygen.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR   EMBL; CU329670; CAA90803.1; -; Genomic_DNA.
DR   PIR; T37609; T37609.
DR   RefSeq; NP_592990.1; -.
DR   HSSP; P77901; 1E9X.
DR   GeneID; 2542599; -.
DR   KEGG; spo:SPAC13A11.02c; -.
DR   NMPDR; fig|4896.1.peg.2960; -.
DR   GeneDB_Spombe; SPAC13A11.02c; -.
DR   OMA; Q09736; MEQVTGG.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-000714-MON; -.
DR   BRENDA; 1.14.13.70; 653.
DR   ArrayExpress; Q09736; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:GeneDB_SPombe.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:GeneDB_SPombe.
DR   GO; GO:0008398; F:sterol 14-demethylase activity; IEA:EC.
DR   GO; GO:0006696; P:ergosterol biosynthetic process; IEP:GeneDB_SPombe.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006950; P:response to stress; 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   1: Evidence at protein level;
KW   Complete proteome; Endoplasmic reticulum; Heme; Iron; Lipid synthesis;
KW   Membrane; Metal-binding; Monooxygenase; NADP; Oxidoreductase; Signal;
KW   Steroid biosynthesis; Sterol biosynthesis; Stress response;
KW   Transmembrane.
FT   SIGNAL        1     15       Potential.
FT   CHAIN        16    495       Lanosterol 14-alpha demethylase erg11.
FT                                /FTId=PRO_0000052009.
FT   TRANSMEM     35     55       Potential.
FT   TRANSMEM    283    303       Potential.
FT   METAL       442    442       Iron (heme axial ligand) (By similarity).
SQ   SEQUENCE   495 AA;  56331 MW;  193333395F6C8B31 CRC64;
     MAFSLVSILL SIALAWYVGY IINQLTSRNS KRPPIVFHWI PFVGSAVAYG MDPYVFFREC
     RAKYGDVFTF VCMGRKMTAF LGVQGNDFLF NGKLADLNAE EAYSHLTTPV FGKDVVYDIP
     NHVFMEHKKF IKSGLGFSQF RSYVPLILNE MDAFLSTSPD FGPGKEGVAD LLKTMPVMTI
     YTASRTLQGA EVRKGFDAGF ADLYHDLDQG FSPVNFVFPW LPLPRNRRRD RAHKIMQKTY
     LKIIKDRRSS TENPGTDMIW TLMSCKYRDG RPLKEHEIAG MMIALLMAGQ HTSAATIVWV
     LALLGSKPEI IEMLWEEQKR VVGENLELKF DQYKDMPLLN YVIQETLRLH PPIHSHMRKV
     KRDLPVPGSK IVIPANNYLL AAPGLTATEE EYFTHATDFD PKRWNDRVNE DENAEQIDYG
     YGLVTKGAAS PYLPFGAGRH RCIGEQFAYM HLSTIISKFV HDYTWTLIGK VPNVDYSSMV
     ALPLGPVKIA WKRRN
//