Q09736 (CP51_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lanosterol 14-alpha demethylase erg11
EC=1.14.13.70

Alternative name(s):
CYPLI
Cytochrome P450 51
Cytochrome P450-14DM
Cytochrome P450-LIA1
Sterol 14-alpha demethylase erg11

Gene names

Name:	erg11
Synonyms:	cyp51
ORF Names:	SPAC13A11.02c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	495 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (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 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.
Subunit structure	Interacts with dap1. Ref.4
Subcellular location	Endoplasmic reticulum. Membrane; Single-pass membrane protein Potential Ref.3.
Induction	Up-regulated by sre1 in response to absence of oxygen. Ref.2
Sequence similarities	Belongs to the cytochrome P450 family.

Ontologies

Keywords
Biological process	Lipid synthesis Steroid biosynthesis Sterol biosynthesis Stress response
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Heme Iron Metal-binding NADP
Molecular function	Monooxygenase Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ergosterol biosynthetic process Inferred from expression pattern. Source: GeneDB_Spombe response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Inferred from sequence or structural similarity. Source: GeneDB_Spombe integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: GeneDB_Spombe sterol 14-demethylase activity Inferred from sequence or structural similarity. Source: GeneDB_Spombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 495	495	Lanosterol 14-alpha demethylase erg11		PRO_0000052009
Regions
	Transmembrane	2 – 22	21	Helical; Potential
Sites
	Metal binding	442	1	Iron (heme axial ligand) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q09736 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 193333395F6C8B31	FASTA	495	56,331
	10 20 30 40 50 60 MAFSLVSILL SIALAWYVGY IINQLTSRNS KRPPIVFHWI PFVGSAVAYG MDPYVFFREC 70 80 90 100 110 120 RAKYGDVFTF VCMGRKMTAF LGVQGNDFLF NGKLADLNAE EAYSHLTTPV FGKDVVYDIP 130 140 150 160 170 180 NHVFMEHKKF IKSGLGFSQF RSYVPLILNE MDAFLSTSPD FGPGKEGVAD LLKTMPVMTI 190 200 210 220 230 240 YTASRTLQGA EVRKGFDAGF ADLYHDLDQG FSPVNFVFPW LPLPRNRRRD RAHKIMQKTY 250 260 270 280 290 300 LKIIKDRRSS TENPGTDMIW TLMSCKYRDG RPLKEHEIAG MMIALLMAGQ HTSAATIVWV 310 320 330 340 350 360 LALLGSKPEI IEMLWEEQKR VVGENLELKF DQYKDMPLLN YVIQETLRLH PPIHSHMRKV 370 380 390 400 410 420 KRDLPVPGSK IVIPANNYLL AAPGLTATEE EYFTHATDFD PKRWNDRVNE DENAEQIDYG 430 440 450 460 470 480 YGLVTKGAAS PYLPFGAGRH RCIGEQFAYM HLSTIISKFV HDYTWTLIGK VPNVDYSSMV 490 ALPLGPVKIA WKRRN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
[2]	"Sterol regulatory element binding protein is a principal regulator of anaerobic gene expression in fission yeast." Todd B.L., Stewart E.V., Burg J.S., Hughes A.L., Espenshade P.J. Mol. Cell. Biol. 26:2817-2831(2006) [PubMed: 16537923] [Abstract] Cited for: INDUCTION.
[3]	"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[4]	"Dap1/PGRMC1 binds and regulates cytochrome P450 enzymes." Hughes A.L., Powell D.W., Bard M., Eckstein J., Barbuch R., Link A.J., Espenshade P.J. Cell Metab. 5:143-149(2007) [PubMed: 17276356] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH DAP1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAA90803.1.
PIR	T37609.
RefSeq	NP_592990.1. NM_001018389.1.
3D structure databases
ProteinModelPortal	Q09736.
ModBase	Search...
Protein-protein interaction databases
STRING	Q09736.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC13A11.02c.1; SPAC13A11.02c.1:pep; SPAC13A11.02c.
GeneID	2542599.
GenomeReviews	Gene locus erg11 in contig CU329670_GR.
KEGG	spo:SPAC13A11.02c.
NMPDR	fig|4896.1.peg.2960.
Organism-specific databases
GeneDB_Spombe	SPAC13A11.02c.
Phylogenomic databases
eggNOG	fuNOG06039.
GeneTree	EFGT00050000000280.
HOGENOM	HBG566517.
OMA	DYATRHE.
OrthoDB	EOG4QJVWH.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-000714-MONOMER.
Gene expression databases
ArrayExpress	Q09736.
Family and domain databases
InterPro	IPR001128. Cyt_P450. IPR017972. Cyt_P450_CS. IPR002403. Cyt_P450_E_grp-IV. [Graphical view]
Gene3D	G3DSA:1.10.630.10. Cyt_P450. 1 hit.
KO	K05917.
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00465. EP450IV. PR00385. P450.
SUPFAM	SSF48264. Cytochrome_P450. 1 hit.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CP51_SCHPO

Accession

Primary (citable) accession number: Q09736

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	December 14, 2011
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program