[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=3068024 [NCBI, ExPASy, EBI, Israel, Japan] Chen C., Kalb V.F., Turi T.G., Loper J.C.; "Primary structure of the cytochrome P450 lanosterol 14 alpha-demethylase gene from Candida tropicalis."; DNA 7:617-626(1988).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 434-528. DOI=10.1016/0006-291X(87)90792-3; PubMed=3304292 [NCBI, ExPASy, EBI, Israel, Japan] Chen C., Turi T.G., Sanglard D., Loper J.C.; "Isolation of the Candida tropicalis gene for P450 lanosterol demethylase and its expression in Saccharomyces cerevisiae."; Biochem. Biophys. Res. Commun. 146:1311-1317(1987).

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 metabolism; 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

M23673; AAA53284.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M17595; AAA34316.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A31854; A31854.

3D structure databases

ModBase

P14263.

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

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_0000052005`
`METAL`	`470 470`		`Iron (heme axial ligand).`
`CONFLICT`	`448 448`		`G -> V (in Ref. 2; AAA34316).`
`CONFLICT`	`500 500`		`V -> G (in Ref. 2; AAA34316).`

Sequence information

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

Molecular weight: 60928 Da [This is the MW of the unprocessed precursor]

CRC64: 83F8E3C1C1E826B9 [This is a checksum on the sequence]

        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

P14263 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