Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot Q09736 (CP51_SCHPO)

Last modified July 22, 2008. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Cytochrome P450 51
    EC=1.14.13.70
Alternative name(s):
    CYPLI
    P450-LIA1
    Sterol 14-alpha demethylase erg11
    Lanosterol 14-alpha demethylase erg11
    P450-14DM
Gene names
Name: erg11
Synonyms: cyp51
ORF Names: SPAC13A11.02c
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Hide | Top

Protein attributes

Sequence length495 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

Catalyzes C14-demethylation of lanosterol which is critical for ergosterol biosynthesis. It transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol By similarity.

Catalytic activity

Obtusifoliol + 3 O(2) + 3 NADPH = 4-alpha-methyl-5-alpha-ergosta-8,14,24(28)-trien-3-beta-ol + formate + 3 NADP(+) + 4 H(2)O.

Cofactor

Heme group By similarity.

Pathway

Steroid metabolism; zymosterol biosynthesis; zymosterol from lanosterol: step 1/6.

Subunit structure

Interacts with dap1.

Subcellular location

Endoplasmic reticulum. Membrane; Multi-pass membrane proteinPotential.

Induction

Up-regulated by sre1 in response to absence of oxygen.

Sequence similarities

Belongs to the cytochrome P450 family.

Hide | Top

Ontologies

Keywords

   Biological processLipid synthesis
Steroid biosynthesis
Sterol biosynthesis
Stress response
   Cellular componentEndoplasmic reticulum
Membrane
   DomainSignal
Transmembrane
   LigandHeme
Iron
Metal-binding
NADP
   Molecular functionMonooxygenase
Oxidoreductase
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processergosterol biosynthetic process

Inferred from expression pattern. Source: GeneDB_SPombe

   Cellular componentendoplasmic reticulum Ref.3

Inferred from direct assay. Source: GeneDB_SPombe

   Molecular functionprotein binding Ref.4

Inferred from physical interaction. Source: GeneDB_SPombe

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Signal peptide1 – 1515 Potential
Chain16 – 495480Cytochrome P450 51

Regions

Transmembrane35 – 5521 Potential
Transmembrane283 – 30321 Potential

Sites

Metal binding4421Iron (heme axial ligand) By similarity

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q09736-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 193333395F6C8B31

FASTA49556,331
        10         20         30         40         50         60 
MAFSLVSILL SIALAWYVGY IINQLTSRNS KRPPIVFHWI PFVGSAVAYG MDPYVFFREC 

        70         80         90        100        110        120 
RAKYGDVFTF VCMGRKMTAF LGVQGNDFLF NGKLADLNAE EAYSHLTTPV FGKDVVYDIP 

       130        140        150        160        170        180 
NHVFMEHKKF IKSGLGFSQF RSYVPLILNE MDAFLSTSPD FGPGKEGVAD LLKTMPVMTI 

       190        200        210        220        230        240 
YTASRTLQGA EVRKGFDAGF ADLYHDLDQG FSPVNFVFPW LPLPRNRRRD RAHKIMQKTY 

       250        260        270        280        290        300 
LKIIKDRRSS TENPGTDMIW TLMSCKYRDG RPLKEHEIAG MMIALLMAGQ HTSAATIVWV 

       310        320        330        340        350        360 
LALLGSKPEI IEMLWEEQKR VVGENLELKF DQYKDMPLLN YVIQETLRLH PPIHSHMRKV 

       370        380        390        400        410        420 
KRDLPVPGSK IVIPANNYLL AAPGLTATEE EYFTHATDFD PKRWNDRVNE DENAEQIDYG 

       430        440        450        460        470        480 
YGLVTKGAAS PYLPFGAGRH RCIGEQFAYM HLSTIISKFV HDYTWTLIGK VPNVDYSSMV 

       490 
ALPLGPVKIA WKRRN

« Hide

Hide | Top

References

« Hide 'large scale' references
[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 38366 / 972.
[2]"Sterol regulatory element binding protein is a principal regulator of anaerobic gene expression in fission yeast."
Todd B.L., Stewart E.V., Burg J.S., Hughes A.L., Espenshade P.J.
Mol. Cell. Biol. 26:2817-2831(2006) [PubMed: 16537923] [Abstract]
Cited for: INDUCTION.
[3]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[4]"Dap1/PGRMC1 binds and regulates cytochrome P450 enzymes."
Hughes A.L., Powell D.W., Bard M., Eckstein J., Barbuch R., Link A.J., Espenshade P.J.
Cell Metab. 5:143-149(2007) [PubMed: 17276356] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH DAP1.

Hide | Top

Cross-references

Sequence databases

CU329670 Genomic DNA. Translation: CAA90803.1.
PIRT37609.
RefSeqNP_592990.1.

3D structure databases

HSSPHSSP built from PDB template 1E9X based on UniProtKB P77901.
ModBaseSearch...

Genome annotation databases

GeneID2542599.
KEGGspo:SPAC13A11.02c.
NMPDRfig|4896.1.peg.2960.

Organism-specific databases

GeneDB_SpombeSPAC13A11.02c.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-000714-MON.

Gene expression databases

ArrayExpressQ09736.

Family and domain databases

InterProIPR001128. Cyt_P450.
IPR002403. Cyt_P450_E_grp-IV.
[Graphical view]
Gene3DG3DSA:1.10.630.10. Cyt_P450. 1 hit.
PANTHERPTHR19383. Cyt_P450. 1 hit.
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00465. EP450IV.
PR00385. P450.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProDomQ09736.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

ProtoNetSearch...

Hide | Top

Entry information

Entry nameCP51_SCHPO
AccessionPrimary (citable) accession number: Q09736
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 22, 2008
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Hide | Top

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents