Lanosterol 14-alpha demethylase - Rattus norvegicus (Rat)

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Reviewed, UniProtKB/Swiss-Prot Q64654 (CP51A_RAT)

Last modified January 19, 2010. Version 85. History...

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

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Names and origin

Protein names

Recommended name:
    Lanosterol 14-alpha demethylase
      Short name=LDM
    EC=1.14.13.70
Alternative name(s):
    Cytochrome P450 51A1
    CYPLI
    Cytochrome P450LI
    Sterol 14-alpha demethylase
    Cytochrome P450-14DM
      Short name=Cytochrome P45014DM

Gene names

Name:	Cyp51a1
Synonyms:	Cyp51

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length	503 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

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General annotation (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-8,14,24(28)-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.
Sequence similarities	Belongs to the cytochrome P450 family.

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Ontologies

Keywords
Biological process	Cholesterol biosynthesis Lipid synthesis Steroid biosynthesis Sterol biosynthesis
Cellular component	Endoplasmic reticulum Membrane Microsome
Domain	Transmembrane
Ligand	Heme Iron Metal-binding NADP
Molecular function	Monooxygenase Oxidoreductase
Gene Ontology (GO)
Biological process	cholesterol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW regulation of cholesterol biosynthetic process Ref.4 Traceable author statement. Source: RGD
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW microsome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro sterol 14-demethylase activity Ref.4 Inferred from direct assay. Source: RGD
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 503

503

Lanosterol 14-alpha demethylase

PRO_0000052001

Regions

Transmembrane

24 – 44

Potential

Sites

Metal binding

449

Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict

181

E → K in AAA87074. Ref.4

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Sequences

Sequence

Length

Mass (Da)

Tools

Q64654-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 33D8F345FFE9CF21
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FASTA

503

56,707

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Occurrence of a P450 showing high homology to yeast lanosterol 14-demethylase (P450(14DM)) in the rat liver." Aoyama Y., Funae Y., Noshiro M., Horiuchi T., Yoshida Y. Biochem. Biophys. Res. Commun. 201:1320-1326(1994) [PubMed: 8024575] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"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." Noshiro M., Aoyama Y., Kawamoto T., Gotoh O., Horiuchi T., Yoshida Y. J. Biochem. 122:1114-1121(1997) [PubMed: 9498553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: Wistar.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.
[4]	"Cloning and functional expression of the cDNA encoding rat lanosterol 14-alpha demethylase." Sloane D.L., So O.Y., Leung R., Scarafia L.E., Saldou N., Jarnagin K., Swinney D.C. Gene 161:243-248(1995) [PubMed: 7665087] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 18-503. Tissue: Liver.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	D55681 mRNA. Translation: BAA09529.1. AB004096 Genomic DNA. Translation: BAA20354.1. BC087033 mRNA. Translation: AAH87033.1. U17697 mRNA. Translation: AAA87074.1.
IPI	IPI00214482.
PIR	JC4240. JC4758.
RefSeq	NP_037073.1.
UniGene	Rn.107152
3D structure databases
SMR	Q64654. Positions 66-502.
ModBase	Search...
Protein-protein interaction databases
STRING	Q64654.
Proteomic databases
PRIDE	Q64654.
Genome annotation databases
Ensembl	ENSRNOT00000009985; ENSRNOP00000009985; ENSRNOG00000007234; Rattus norvegicus. [Genome view]
GeneID	25427.
KEGG	rno:25427.
UCSC	NM_012941. rat.
Organism-specific databases
CTD	25427.
RGD	2481. Cyp51.
Phylogenomic databases
eggNOG	roNOG14720.
HOVERGEN	Q64654.
InParanoid	Q64654.
OMA	CAFTLSL.
OrthoDB	EOG9GTP0F.
PhylomeDB	Q64654.
Enzyme and pathway databases
BRENDA	1.14.13.70. 248.
Gene expression databases
ArrayExpress	Q64654.
Genevestigator	Q64654.
GermOnline	ENSRNOG00000007234. Rattus norvegicus.
Family and domain databases
InterPro	IPR001128. Cyt_P450. IPR017973. Cyt_P450_C. IPR017972. Cyt_P450_CS. IPR002403. Cyt_P450_E_grp-IV. [Graphical view]
Gene3D	G3DSA:1.10.630.10. Cyt_P450. 1 hit.
PANTHER	PTHR19383. Cyt_P450. 1 hit.
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00465. EP450IV. PR00385. P450.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	606607.

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Entry information

Entry name

CP51A_RAT

Accession

Primary (citable) accession number: Q64654
Secondary accession number(s): Q64549

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	January 19, 2010
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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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)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents