[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; DOI=10.1006/bbrc.1994.1848; PubMed=8024575 [NCBI, ExPASy, EBI, Israel, Japan] Aoyama Y., Funae Y., Noshiro M., Horiuchi T., Yoshida Y.; "Occurrence of a P450 showing high homology to yeast lanosterol 14-demethylase (P450(14DM)) in the rat liver."; Biochem. Biophys. Res. Commun. 201:1320-1326(1994).
[2]	NUCLEOTIDE SEQUENCE. STRAIN=Wistar; PubMed=9498553 [NCBI, ExPASy, EBI, Israel, Japan] Noshiro M., Aoyama Y., Kawamoto T., Gotoh O., Horiuchi T., Yoshida Y.; "Structural and evolutionary studies on sterol 14-demethylase P450 (CYP51), the most conserved P450 monooxygenase: I. Structural analyses of the gene and multiple sizes of mRNA."; J. Biochem. 122:1114-1121(1997).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Kidney; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	NUCLEOTIDE SEQUENCE [MRNA] OF 18-503. TISSUE=Liver; DOI=10.1016/0378-1119(95)00211-N; PubMed=7665087 [NCBI, ExPASy, EBI, Israel, Japan] Sloane D.L., So O.Y., Leung R., Scarafia L.E., Saldou N., Jarnagin K., Swinney D.C.; "Cloning and functional expression of the cDNA encoding rat lanosterol 14-alpha demethylase."; Gene 161:243-248(1995).

Comments

FUNCTION: Catalyzes C14-demethylation of lanosterol; 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: Endoplasmic reticulum membrane (Potential). Microsome membrane (Potential).
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

D55681; BAA09529.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB004096; BAA20354.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC087033; AAH87033.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U17697; AAA87074.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JC4240; JC4240.
JC4758; JC4758.

RefSeq

NP_037073.1; -.

UniGene

Rn.107152

3D structure databases

HSSP

P77901; 1E9X. [HSSP ENTRY / PDB]

ModBase

Q64654.

Organism-specific databases

RGD

2481; Cyp51.

Gene expression databases

ArrayExpress

Q64654; -.

GermOnline

ENSRNOG00000007234; Rattus norvegicus.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005792;	Cellular component: microsome (inferred from electronic annotation from UniProtKB-KW).
GO:0008398;	Molecular function: sterol 14-demethylase activity (inferred from electronic annotation from EC).
GO:0006695;	Biological process: cholesterol biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (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.

Genome annotation databases

Ensembl

ENSRNOG00000007234; Rattus norvegicus. [Contig view]

GeneID

25427; -.

KEGG

rno:25427; -.

Phylogenomic databases

HOVERGEN

Q64654; -.

Other

NextBio

606607; -.

UniRef

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

Keywords

Cholesterol biosynthesis; Endoplasmic reticulum; Heme; Iron; Lipid synthesis; Membrane; Metal-binding; Microsome; Monooxygenase; NADP; Oxidoreductase; Steroid biosynthesis; Sterol biosynthesis; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 503`	`503`	`Cytochrome P450 51A1.`	`PRO_0000052001`
`TRANSMEM`	`24 44`	`21`	`Potential.`
`METAL`	`449 449`		`Iron (heme axial ligand) (By similarity).`
`CONFLICT`	`181 181`		`E -> K (in Ref. 4; AAA87074).`

Sequence information

Length: 503 AA [This is the length of the unprocessed precursor]

Molecular weight: 56707 Da [This is the MW of the unprocessed precursor]

CRC64: 33D8F345FFE9CF21 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVLLGLLQSG GSVLGQAMEQ VTGGNLLSTL LIACAFTLSL VYLFRLAVGH MVQLPAGAKS 

        70         80         90        100        110        120 
PPYIYSPIPF LGHAIAFGKS PIEFLENAYE KYGPVFSFTM VGKTFTYLLG SDAAALLFNS 

       130        140        150        160        170        180 
KNEDLNAEEV YGRLTTPVFG KGVAYDVPNA VFLEQKKILK SGLNIAHFKQ YVSIIEKEAK 

       190        200        210        220        230        240 
EYFKSWGESG ERNVFEALSE LIILTASHCL HGKEIRSQLN EKVAQLYADL DGGFSHAAWL 

       250        260        270        280        290        300 
LPGWLPLPSF RRRDRAHREI KNIFYKAIQK RRLSKEPAED ILQTLLDSTY KDGRPLTDDE 

       310        320        330        340        350        360 
IAGMLIGLLL AGQHTSSTTS AWMGFFLARD KPLQDKCYLE QKTVCGEDLP PLTYEQLKDL 

       370        380        390        400        410        420 
NLLDRCIKET LRLRPPIMTM MRMAKTPQTV AGYTIPPGHQ VCVSPTVNQR LKDSWVERLD 

       430        440        450        460        470        480 
FNPDRYLQDN PASGEKFAYV PFGAGRHRCI GENFAYVQIK TIWSTMLRLY EFDLINGYFP 

       490        500 
SVNYTTMIHT PENPVIRYKR RSK

Q64654 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