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Q10231 (ERG7_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length721 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 721721Lanosterol synthase
PRO_0000072656

Regions

Repeat121 – 16242PFTB 1
Repeat555 – 59541PFTB 2
Repeat604 – 64542PFTB 3
Repeat662 – 70342PFTB 4

Sites

Active site2291Proton acceptor By similarity
Active site4511Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q10231 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 445B67F4BF7BFBA3

FASTA72182,819
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U41368 mRNA. Translation: AAA92502.1.
CU329670 Genomic DNA. Translation: CAA93571.1.
PIRJC4643.
RefSeqNP_593702.2. NM_001019134.2.

3D structure databases

ProteinModelPortalQ10231.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4697960.
STRING4896.SPAC13G7.01c-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC13G7.01c.1; SPAC13G7.01c.1:pep; SPAC13G7.01c.
GeneID2542882.
KEGGspo:SPAC13G7.01c.

Organism-specific databases

PomBaseSPAC13G7.01c.

Phylogenomic databases

eggNOGCOG1657.
HOGENOMHOG000234317.
KOK01852.
OMAENINFAS.
OrthoDBEOG70610B.

Enzyme and pathway databases

UniPathwayUPA00767; UER00753.

Family and domain databases

InterProIPR001330. Prenyltrans.
IPR018333. Squalene_cyclase.
IPR002365. Terpene_synthase_CS.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PfamPF00432. Prenyltrans. 3 hits.
[Graphical view]
SUPFAMSSF48239. SSF48239. 2 hits.
TIGRFAMsTIGR01787. squalene_cyclas. 1 hit.
PROSITEPS01074. TERPENE_SYNTHASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20803922.
PROQ10231.

Entry information

Entry nameERG7_SCHPO
AccessionPrimary (citable) accession number: Q10231
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 19, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways