Reviewed, UniProtKB/Swiss-Prot O46420 (CP51A_PIG)

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
    P450LI
    Sterol 14-alpha demethylase
    P450-14DM
      Short name=P45014DM

Gene names

Name:	CYP51A1
Synonyms:	CYP51

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	503 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Catalyzes C14-demethylation of lanosterol; it transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol By similarity.
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.

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
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 Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 503	503	Lanosterol 14-alpha demethylase		PRO_0000051999
Regions
	Transmembrane	24 – 44	21	Potential
Sites
	Metal binding	449	1	Iron (heme axial ligand) By similarity

Sequences

	Sequence		Length	Mass (Da)
	O46420-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 0302949CE461AFD6	FASTA	503	56,867
	10 20 30 40 50 60 MVLLGLLQAG GSVLGQAMEQ VTGVNLLSSL LLACAFTLIL VYLFRQAIGH LAPLPAGAKS 70 80 90 100 110 120 PPYIFSPIPF LGHAIAFGKS PIEFLENAYE KYGPVFSFTM VGKTFTYLLG SDAAALLFNS 130 140 150 160 170 180 KNEDLNAEDV YSRLTTPVFG KGVAYDVPNP VFLEQKKMLK SGLNIAHFRQ HVSIIEKETK 190 200 210 220 230 240 EYFQSWGESG ERNLFEALSE LIILTASHCL HGKEIRSQLN EKVAQLYADL DGGFSHAAWL 250 260 270 280 290 300 LPGWLPLPSF RRRDRAHREI KNIFYKAIQK RRQSEEKIDD ILQTLLDSTY KDGRPLTDDE 310 320 330 340 350 360 VAGMLIGLLL AGQHTSSTTS AWMGFFLARD KTLQEKCYLE QKTVCGEDLP PLTYDQLKDL 370 380 390 400 410 420 NLLDRCIKET LRLRPPIMTM MRMAKTPQTV AGYTIPPGHQ VCVSPTVNQR LKDSWVERLD 430 440 450 460 470 480 FNPDRYLQDN PASGEKFAYV PFGAGRHRCI GENFAYVQIK TIWSTMLRLY EFDLIDGYFP 490 500 TVNYTTMIHT PENPVIRYKR RSK

References

[1]	"Cloning of a pig lanosterol 14-demethylase cDNA." Kojima M., Morozumi T., Hamasima N., Okamoto T. Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Structure of the pig sterol 14 alpha-demethylase (CYP51) gene and its expression in the testis and other tissues." Kojima M., Morozumi T., Onishi A., Mitsuhashi T. J. Biochem. 127:805-811(2000) [PubMed: 10788789] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB009988 mRNA. Translation: BAA24134.1. AB042982 Genomic DNA. Translation: BAA96092.1.
PIR	JC7243.
RefSeq	NP_999597.1.
UniGene	Ssc.5712
3D structure databases
HSSP	HSSP built from PDB template 1E9X based on UniProtKB P77901.
ModBase	Search...
Genome annotation databases
GeneID	403334.
KEGG	ssc:403334.
Phylogenomic databases
HOVERGEN	O46420.
Enzyme and pathway databases
BRENDA	1.14.13.70. 249.
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...

Entry information

Entry name

CP51A_PIG

Accession

Primary (citable) accession number: O46420

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	June 1, 1998
Last modified:	June 16, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)