Q10231 (ERG7_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lanosterol synthase
EC=5.4.99.7

Alternative name(s):
2,3-epoxysqualene--lanosterol cyclase
Oxidosqualene--lanosterol cyclase
Short name=OSC

Gene names

Name:	erg7
ORF Names:	SPAC13G7.01c, SPAC4G9.21c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	721 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol nucleus.
Catalytic activity	(3S)-2,3-epoxy-2,3-dihydrosqualene = lanosterol.
Pathway	Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl diphosphate: step 3/3.
Sequence similarities	Belongs to the terpene cyclase/mutase family. Contains 4 PFTB repeats.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Steroid biosynthesis
Domain	Repeat
Molecular function	Isomerase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ergosterol biosynthetic process Inferred from sequence or structural similarity. Source: PomBase
Cellular_component	cytosol Inferred from direct assay PubMed 16823372. Source: PomBase endoplasmic reticulum Inferred from sequence or structural similarity. Source: PomBase
Molecular_function	lanosterol synthase activity Inferred from sequence or structural similarity. Source: PomBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 721	721	Lanosterol synthase		PRO_0000072656
Regions
	Repeat	121 – 162	42	PFTB 1
	Repeat	555 – 595	41	PFTB 2
	Repeat	604 – 645	42	PFTB 3
	Repeat	662 – 703	42	PFTB 4
Sites
	Active site	229	1	Proton acceptor By similarity
	Active site	451	1	Proton donor By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q10231 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 445B67F4BF7BFBA3	FASTA	721	82,819
	10 20 30 40 50 60 MEACRVRPEL SKTVEQIDKS LWRLNIDSAG GETWEYVTKE EAEKRPLTIA EKYFLGFDLD 70 80 90 100 110 120 LPKRPPAKTP LESAEYGYEF FRRLQLPDGH WASPYEGPMF LICGAVFAFY ISQTPFPKGW 130 140 150 160 170 180 APEIIQYLIN HTNDDGGWGI HTEGVSTVFG TSMNYVVLRI LGMDAGHPVA TRARNRLHEL 190 200 210 220 230 240 GGAIGCPHWG KFWLATLNCY DWDGVNPIPP ELWLLPDWIP FHPGKWWCHV RLVYLPMGYM 250 260 270 280 290 300 YGERLKCPKD SLIMQLRKEL YVENYDSINF ADHRNTISDV DLYFPHTQIL DRLNWILEKY 310 320 330 340 350 360 FTYLRPSWLK KLGTRRAYEL IKIEDQNTDY SCIGPVNAAM NTVCVYFHEG PSSKAFQKHI 370 380 390 400 410 420 QRLHDFMWVQ PEGMLMRGTN GLQVWETSFT LQALVESGLY EKEAFKPDIA KALEFLDRQQ 430 440 450 460 470 480 IRTQYEGSGY RYNSLGAWPF SNITQGYTVS DTTSEALRAV LLVQSLPDFE KLVDIPRLRL 490 500 510 520 530 540 SVDVILGMQN ENLGFASYEP ARTGEWMELL NPAEVFGNIM VEYSYPECTT SVILALRAFT 550 560 570 580 590 600 KYDPGYRRDE IENTIENALE YVVKMQRPDG SWYGSWAICF TYAAMFATGS LASAGRYYEN 610 620 630 640 650 660 CPVQKKACEF LLSKQRPDGG WSESYMACVT GVYTETESSL VTQTGWALDA LINAKYPDRK 670 680 690 700 710 720 PIEKGIKFLM ASQKSDGSWQ QKSMEGIFNK NVAIAYPNYK LYFSIYTLGK FAKQYGNYLT I

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of a Schizosaccharomyces pombe cDNA encoding lanosterol synthase and investigation of conserved tryptophan residues." Corey E.J., Matsuda S.P.T., Baker C.H., Ting A.Y., Cheng H. Biochem. Biophys. Res. Commun. 219:327-331(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U41368 mRNA. Translation: AAA92502.1. CU329670 Genomic DNA. Translation: CAA93571.1.
PIR	JC4643.
RefSeq	NP_593702.2. NM_001019134.2.
3D structure databases
ProteinModelPortal	Q10231.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPAC13G7.01c-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC13G7.01c.1; SPAC13G7.01c.1:pep; SPAC13G7.01c.
GeneID	2542882.
KEGG	spo:SPAC13G7.01c.
Organism-specific databases
PomBase	SPAC13G7.01c.
Phylogenomic databases
eggNOG	COG1657.
HOGENOM	HOG000234317.
KO	K01852.
OMA	SWLLHVV.
OrthoDB	EOG4STWCS.
Enzyme and pathway databases
UniPathway	UPA00767; UER00753.
Family and domain databases
InterPro	IPR001330. Prenyltrans. IPR018333. Squalene_cyclase. IPR002365. Terpene_synthase_CS. IPR008930. Terpenoid_cyclase/PrenylTrfase. [Graphical view]
Pfam	PF00432. Prenyltrans. 3 hits. [Graphical view]
SUPFAM	SSF48239. Terp_cyc_toroid. 2 hits.
TIGRFAMs	TIGR01787. squalene_cyclas. 1 hit.
PROSITE	PS01074. TERPENE_SYNTHASES. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20803922.

Entry information

Entry name

ERG7_SCHPO

Accession

Primary (citable) accession number: Q10231

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program