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Reviewed, UniProtKB/Swiss-Prot P14263 (CP51_CANTR)

Last modified July 22, 2008. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Names and origin

Protein namesRecommended name:
    Cytochrome P450 51
    EC=1.14.13.70
Alternative name(s):
    CYPLI
    P450-LIA1
    Sterol 14-alpha demethylase
    Lanosterol 14-alpha demethylase
    P450-14DM
Gene names
Name: ERG11
Synonyms: CYP51
OrganismCandida tropicalis (Yeast)
Taxonomic identifier5482 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length528 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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.

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.

Subcellular location

MembranePotential. Membrane; Single-pass membrane protein.

Sequence similarities

Belongs to the cytochrome P450 family.

Ontologies

Keywords

   Biological processLipid synthesis
Steroid biosynthesis
Sterol biosynthesis
   Cellular componentMembrane
   LigandHeme
Iron
Metal-binding
NADP
   Molecular functionMonooxygenase
Oxidoreductase

Gene Ontology (GO)

   Molecular functionsterol 14-demethylase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 528528Cytochrome P450 51

Sites

Metal binding4701Iron (heme axial ligand)

Experimental info

Sequence conflict4481G → V in AAA34316. Ref.2
Sequence conflict5001V → G in AAA34316. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P14263-1 [UniParc].

Last modified November 1, 1990. Version 2.
Checksum: 83F8E3C1C1E826B9

FASTA52860,928
        10         20         30         40         50         60 
MAIVDTAIDG INYFLSLSLT QQITILVVFP FIYNIAWQLL YSLRKDRVPM VFYWIPWFGS 

        70         80         90        100        110        120 
AASYGMQPYE FFEKCRLKYG DVFSFMLLGK VMTVYLGPKG HEFIYNAKLS DVSAEEAYTH 

       130        140        150        160        170        180 
LTTPVFGKGV IYDCPNSRLM EQKKFAKFAL TTDSFKTYVP KIREEVLNYF VNDVSFKTKE 

       190        200        210        220        230        240 
RDHGVASVMK TQPEITIFTA SRCLFGDEMR KSFDRSFAQL YADLDKGFTP INFVFPNLPL 

       250        260        270        280        290        300 
PHYWRRDAAQ RKISAHYMKE IKRRRESGDI DPKRDLIDSL LVNSTYKDGV KMTDQEIANL 

       310        320        330        340        350        360 
LIGVLMGGQH TSASTSAWFL LHLAEQPQLQ DDLYEELTNL LKEKGGDLND LTYEDLQKLP 

       370        380        390        400        410        420 
LVNNTIKETL RMHMPLHSIF RKVMNPLRVP NTKYVIPKGH YVLVSAGYAH TSDRWFEHPE 

       430        440        450        460        470        480 
HFNPRRWESD DTKASAVSFN SEDTVDYGFG KISKGVSSPY LPFGGGRHRC IGEQFAYVQL 

       490        500        510        520 
GTILTTYIYN FKWRLNGDKV PDVDYQSMVT LPLEPAEIVW EKRDTCMV 

« Hide

References

[1]"Primary structure of the cytochrome P450 lanosterol 14 alpha-demethylase gene from Candida tropicalis."
Chen C., Kalb V.F., Turi T.G., Loper J.C.
DNA 7:617-626(1988) [PubMed: 3068024] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Isolation of the Candida tropicalis gene for P450 lanosterol demethylase and its expression in Saccharomyces cerevisiae."
Chen C., Turi T.G., Sanglard D., Loper J.C.
Biochem. Biophys. Res. Commun. 146:1311-1317(1987) [PubMed: 3304292] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 434-528.

Cross-references

Sequence databases

M23673 Genomic DNA. Translation: AAA53284.1.
M17595 Genomic DNA. Translation: AAA34316.1.
PIRA31854.

3D structure databases

ModBaseSearch...

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]
ProDomP14263.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

ProtoNetSearch...

Entry information

Entry nameCP51_CANTR
AccessionPrimary (citable) accession number: P14263
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 1, 1990
Last modified: July 22, 2008
This is version 55 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

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