[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=SC5314; DOI=10.1093/nar/17.2.804; PubMed=2644625 [NCBI, ExPASy, EBI, Israel, Japan] Lai M.H., Kirsch D.R.; "Nucleotide sequence of cytochrome P450 L1A1 (lanosterol 14 alpha-demethylase) from Candida albicans."; Nucleic Acids Res. 17:804-804(1989).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-48 AND 467-528, AND VARIANT LYS-467. STRAIN=SS; PubMed=9210671 [NCBI, ExPASy, EBI, Israel, Japan] White T.C.; "The presence of an R467K amino acid substitution and loss of allelic variation correlate with an azole-resistant lanosterol 14-alpha demethylase in Candida albicans."; Antimicrob. Agents Chemother. 41:1488-1494(1997).
[3]	3D-STRUCTURE MODELING. DOI=10.1016/0263-7855(94)80086-3; PubMed=7819160 [NCBI, ExPASy, EBI, Israel, Japan] Boscott P.E., Grant G.H.; "Modeling cytochrome P450 14-alpha demethylase (Candida albicans) from P450cam."; J. Mol. Graph. 12:185-192(1994).
[4]	VARIANTS FLUCONAZOLE-RESISTANT. DOI=10.1016/S0378-1097(97)00172-9; PubMed=9228762 [NCBI, ExPASy, EBI, Israel, Japan] Loffler J., Kelly S.L., Hebart H., Schumacher U., Lass-Florl C., Einsele H.; "Molecular analysis of cyp51 from fluconazole-resistant Candida albicans strains."; FEMS Microbiol. Lett. 151:263-268(1997).

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 O₂ + 3 NADPH = 4-alpha-methyl-5-alpha-ergosta-8,14,24²⁸-trien-3-beta-ol + formate + 3 NADP⁺ + 4 H₂O.
COFACTOR: Heme group (By similarity).
PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 1/6 .
SUBCELLULAR LOCATION: Membrane (Potential). Membrane; Single-pass membrane protein.
SIMILARITY: Belongs to the cytochrome P450 family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X13296; CAA31658.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U67192; AAB08099.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U67193; AAB08100.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S02713; O4CK51.

3D structure databases

ModBase

P10613.

Organism-specific databases

CGD

CAL0003627; ERG11.

Ontologies

GO:0016020;	Cellular component: membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0008398;	Molecular function: sterol 14-demethylase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0016126;	Biological process: sterol biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001128; Cyt_P450.
IPR002403; Cyt_P450_E_grp-IV.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.630.10; Cyt_P450; 1.

PANTHER

PTHR19383; Cyt_P450; 1.

Pfam

PF00067; p450; 1.
Pfam graphical view of domain structure.

PRINTS

PR00465; EP450IV.
PR00385; P450.

PROSITE

PS00086; CYTOCHROME_P450; 1.

Other

DB00646; Nystatin.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Heme; Iron; Lipid synthesis; Membrane; Metal-binding; Monooxygenase; NADP; Oxidoreductase; Steroid biosynthesis; Sterol biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 528`	`528`	`Cytochrome P450 51.`	`PRO_0000052003`
`METAL`	`470 470`		`Iron (heme axial ligand) (By similarity).`
`VARIANT`	`105 105`	`1`	`F -> L (in fluconazole-resistant isolates).`
`VARIANT`	`266 266`	`1`	`E -> D (in strain: fluconazole-resistant isolates).`
`VARIANT`	`287 287`	`1`	`K -> R (in strain: fluconazole-resistant isolates).`
`VARIANT`	`450 450`	`1`	`G -> E (in strain: fluconazole-resistant isolates).`
`VARIANT`	`464 464`	`1`	`G -> S (in strain: fluconazole-resistant isolates).`
`VARIANT`	`467 467`	`1`	`R -> K (in strain: Isolate 13; azole-resistant).`
`VARIANT`	`488 488`	`1`	`V -> I (in strain: fluconazole-resistant isolates).`
`CONFLICT`	`19 19`		`V -> D (in Ref. 2; AAB08099).`

Sequence information

Length: 528 AA [This is the length of the unprocessed precursor]

Molecular weight: 60675 Da [This is the MW of the unprocessed precursor]

CRC64: 026948CEE4AF1B88 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAIVETVIDG INYFLSLSVT QQISILLGVP FVYNLVWQYL YSLRKDRAPL VFYWIPWFGS 

        70         80         90        100        110        120 
AASYGQQPYE FFESCRQKYG DVFSFMLLGK IMTVYLGPKG HEFVFNAKLS DVSAEDAYKH 

       130        140        150        160        170        180 
LTTPVFGKGV IYDCPNSRLM EQKKFAKFAL TTDSFKRYVP KIREEILNYF VTDESFKLKE 

       190        200        210        220        230        240 
KTHGVANVMK TQPEITIFTA SRSLFGDEMR RIFDRSFAQL YSDLDKGFTP INFVFPNLPL 

       250        260        270        280        290        300 
PHYWRRDAAQ KKISATYMKE IKSRRERGDI DPNRDLIDSL LIHSTYKDGV KMTDQEIANL 

       310        320        330        340        350        360 
LIGILMGGQH TSASTSAWFL LHLGEKPHLQ DVIYQEVVEL LKEKGGDLND LTYEDLQKLP 

       370        380        390        400        410        420 
SVNNTIKETL RMHMPLHSIF RKVTNPLRIP ETNYIVPKGH YVLVSPGYAH TSERYFDNPE 

       430        440        450        460        470        480 
DFDPTRWDTA AAKANSVSFN SSDEVDYGFG KVSKGVSSPY LPFGGGRHRC IGEQFAYVQL 

       490        500        510        520 
GTILTTFVYN LRWTIDGYKV PDPDYSSMVV LPTEPAEIIW EKRETCMF

P10613 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools