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Q8BLN5 (ERG7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. 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:Lss
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length733 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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 By similarity. UniProtKB P48450

Catalytic activity

(3S)-2,3-epoxy-2,3-dihydrosqualene = lanosterol.

Pathway

Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl diphosphate: step 3/3.

Subunit structure

Monomer By similarity.

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein By similarity.

Sequence similarities

Belongs to the terpene cyclase/mutase family. UniProtKB P48450

Contains 4 PFTB repeats.

Ontologies

Keywords
   Biological processLipid biosynthesis
Lipid metabolism
Steroid biosynthesis
   Cellular componentEndoplasmic reticulum
Membrane
   DomainRepeat
   Molecular functionIsomerase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcholesterol biosynthetic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

lipid particle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionlanosterol synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 733732Lanosterol synthase
PRO_0000072660

Regions

Repeat125 – 16642PFTB 1
Repeat484 – 52946PFTB 2
Repeat561 – 60141PFTB 3
Repeat613 – 65442PFTB 4

Sites

Active site2331Proton acceptor By similarity
Active site4561Proton donor By similarity

Amino acid modifications

Modified residue21N-acetylthreonine By similarity

Experimental info

Sequence conflict2971V → A in BAC37102. Ref.1
Sequence conflict3471V → A in BAC31739. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8BLN5 [UniParc].

Last modified March 29, 2005. Version 2.
Checksum: 17C3ED638C0D66B0

FASTA73383,141
        10         20         30         40         50         60 
MTEGTCLRRR GGPYKTEPAT DLTRWRLQNE LGRQRWTYYQ AEDDPGREQT GLEAHSLGLD 

        70         80         90        100        110        120 
TRSYFTDLPK AQTAHEGALN GVTFYAKLQA EDGHWAGDYG GPLFLLPGLL ITCHISHISL 

       130        140        150        160        170        180 
PAGYREEMVR YLRSVQLPDG GWGLHIEDKS TVFGTALNYV ALRILGIGPD DPDLVRARNV 

       190        200        210        220        230        240 
LHKKGGAVAI PSWGKFWLAV LNVYSWEGLN TLFPEMWLFP EWVPAHPSTL WCHCRQVYLP 

       250        260        270        280        290        300 
MSYCYATRLS ASEDPLVQSL RQELYVQDYA SIDWPAQRNN VSPDEMYTPH SWLLHVVYGL 

       310        320        330        340        350        360 
LNLYERFHST SLRKWAVQML YEHIAADDCF TKCISIGPIS KTINMLVRWS VDGPSSPAFQ 

       370        380        390        400        410        420 
EHVSRIKDYL WLGLDGMKMQ GTNGSQIWDT SFAIQALLEA GAHHRPEFLP CLQKAHEFLR 

       430        440        450        460        470        480 
LSQVPENCPD YQKYYRHMRK GGFSFSTLDC GWIVADCTAE GLKAVLLLQN QCPSITEHIP 

       490        500        510        520        530        540 
RERLCDAVDV LLSLRNADGG FATYEKKRGG YLLELLNPSE VFGDIMIDYT YVECTSAVMQ 

       550        560        570        580        590        600 
ALKHFHEHFP DYRAAEVRET LNQGLDFCRR KQRADGSWEG SWGVCFTYGT WFGLEAFACM 

       610        620        630        640        650        660 
GHTYQDGAAC AEVAQACNFL LSQQMADGGW GEDFESCEQR RYVQSARSQV HSTCWALMGL 

       670        680        690        700        710        720 
MAVRHPDITA QERGIRCLLG KQLPNGDWPQ ENISGVFNKS CAISYTSYRN IFPIWALGRF 

       730 
SNLYPDNTLA GHI 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Brain cortex and Head.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK044016 mRNA. Translation: BAC31739.1.
AK078023 mRNA. Translation: BAC37102.1.
BC029082 mRNA. Translation: AAH29082.1.
CCDSCCDS23948.1.
RefSeqNP_666118.1. NM_146006.1.
UniGeneMm.55075.

3D structure databases

ProteinModelPortalQ8BLN5.
SMRQ8BLN5. Positions 6-732.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ8BLN5.

Proteomic databases

MaxQBQ8BLN5.
PaxDbQ8BLN5.
PRIDEQ8BLN5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000048678; ENSMUSP00000046856; ENSMUSG00000033105.
GeneID16987.
KEGGmmu:16987.
UCSCuc007fuq.1. mouse.

Organism-specific databases

CTD4047.
MGIMGI:1336155. Lss.

Phylogenomic databases

eggNOGCOG1657.
GeneTreeENSGT00390000011570.
HOGENOMHOG000234317.
HOVERGENHBG005604.
InParanoidQ8BLN5.
KOK01852.
OMAGLNYIYG.
OrthoDBEOG70W3CN.
PhylomeDBQ8BLN5.
TreeFamTF300406.

Enzyme and pathway databases

UniPathwayUPA00767; UER00753.

Gene expression databases

ArrayExpressQ8BLN5.
BgeeQ8BLN5.
CleanExMM_LSS.
GenevestigatorQ8BLN5.

Family and domain databases

Gene3D1.50.10.20. 2 hits.
InterProIPR001330. Prenyltrans.
IPR018333. Squalene_cyclase.
IPR002365. Terpene_synthase_CS.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PfamPF00432. Prenyltrans. 1 hit.
[Graphical view]
SUPFAMSSF48239. SSF48239. 2 hits.
TIGRFAMsTIGR01787. squalene_cyclas. 1 hit.
PROSITEPS01074. TERPENE_SYNTHASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio291072.
PROQ8BLN5.
SOURCESearch...

Entry information

Entry nameERG7_MOUSE
AccessionPrimary (citable) accession number: Q8BLN5
Secondary accession number(s): Q8BVJ4, Q8K307
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: July 9, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot