Reviewed, UniProtKB/Swiss-Prot Q09736 (CP51_SCHPO)

Names and origin

Protein names

Recommended name:
    Cytochrome P450 51
    EC=1.14.13.70
Alternative name(s):
    CYPLI
    P450-LIA1
    Sterol 14-alpha demethylase erg11
    Lanosterol 14-alpha demethylase erg11
    P450-14DM

Gene names

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

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	495 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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 O(2) + 3 NADPH = 4-alpha-methyl-5-alpha-ergosta-8,14,24(28)-trien-3-beta-ol + formate + 3 NADP(+) + 4 H(2)O.
Cofactor	Heme group By similarity.
Pathway	Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 1/6.
Subunit structure	Interacts with dap1.
Subcellular location	Endoplasmic reticulum. Membrane; Multi-pass membrane proteinPotential.
Induction	Up-regulated by sre1 in response to absence of oxygen.
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	Signal Transmembrane
Ligand	Heme Iron Metal-binding NADP
Molecular function	Monooxygenase Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ergosterol biosynthetic process Inferred from expression pattern. Source: GeneDB_SPombe oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Ref.3 Inferred from electronic annotation. Source: UniProtKB-KW 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 iron ion binding Inferred from electronic annotation. Source: InterPro protein binding Ref.4 Inferred from physical interaction. Source: GeneDB_SPombe 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
	Signal peptide	1 – 15	15	Potential
	Chain	16 – 495	480	Cytochrome P450 51		PRO_0000052009
Regions
	Transmembrane	35 – 55	21	Potential
	Transmembrane	283 – 303	21	Potential
Sites
	Metal binding	442	1	Iron (heme axial ligand) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q09736-1 [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: ATCC 38366 / 972.
[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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329670 Genomic DNA. Translation: CAA90803.1.
PIR	T37609.
RefSeq	NP_592990.1.
3D structure databases
HSSP	HSSP built from PDB template 1E9X based on UniProtKB P77901.
ModBase	Search...
Genome annotation databases
GeneID	2542599.
KEGG	spo:SPAC13A11.02c.
NMPDR	fig|4896.1.peg.2960.
Organism-specific databases
GeneDB_Spombe	SPAC13A11.02c.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-000714-MON.
Gene expression databases
ArrayExpress	Q09736.
Family and domain databases
InterPro	IPR001128. Cyt_P450. 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

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:	November 25, 2008
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)