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Protein

Lanosterol synthase

Gene

Lss

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol nucleus.By similarity

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei233 – 2331Proton acceptorBy similarity
Active sitei456 – 4561Proton donorBy similarity

GO - Molecular functioni

  1. lanosterol synthase activity Source: UniProtKB-EC

GO - Biological processi

  1. cholesterol biosynthetic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis

Enzyme and pathway databases

ReactomeiREACT_198969. Activation of gene expression by SREBF (SREBP).
REACT_208531. Cholesterol biosynthesis.
UniPathwayiUPA00767; UER00753.

Names & Taxonomyi

Protein namesi
Recommended name:
Lanosterol synthase (EC:5.4.99.7)
Alternative name(s):
2,3-epoxysqualene--lanosterol cyclase
Oxidosqualene--lanosterol cyclase
Short name:
OSC
Gene namesi
Name:LssImported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:1336155. Lss.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. lipid particle Source: MGI
  3. membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 733732Lanosterol synthasePRO_0000072660Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8BLN5.
PaxDbiQ8BLN5.
PRIDEiQ8BLN5.

PTM databases

PhosphoSiteiQ8BLN5.

Expressioni

Gene expression databases

BgeeiQ8BLN5.
CleanExiMM_LSS.
ExpressionAtlasiQ8BLN5. baseline and differential.
GenevestigatoriQ8BLN5.

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ8BLN5.
SMRiQ8BLN5. Positions 6-732.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati125 – 16642PFTB 1Sequence AnalysisAdd
BLAST
Repeati484 – 52946PFTB 2Sequence AnalysisAdd
BLAST
Repeati561 – 60141PFTB 3Sequence AnalysisAdd
BLAST
Repeati613 – 65442PFTB 4Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the terpene cyclase/mutase family.By similarity
Contains 4 PFTB repeats.Sequence Analysis

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1657.
GeneTreeiENSGT00390000011570.
HOGENOMiHOG000234317.
HOVERGENiHBG005604.
InParanoidiQ8BLN5.
KOiK01852.
OMAiTARCVSM.
OrthoDBiEOG70W3CN.
PhylomeDBiQ8BLN5.
TreeFamiTF300406.

Family and domain databases

Gene3Di1.50.10.20. 2 hits.
InterProiIPR001330. Prenyltrans.
IPR018333. Squalene_cyclase.
IPR002365. Terpene_synthase_CS.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PfamiPF00432. Prenyltrans. 1 hit.
[Graphical view]
SUPFAMiSSF48239. SSF48239. 2 hits.
TIGRFAMsiTIGR01787. squalene_cyclas. 1 hit.
PROSITEiPS01074. TERPENE_SYNTHASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8BLN5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEGTCLRRR GGPYKTEPAT DLTRWRLQNE LGRQRWTYYQ AEDDPGREQT
60 70 80 90 100
GLEAHSLGLD TRSYFTDLPK AQTAHEGALN GVTFYAKLQA EDGHWAGDYG
110 120 130 140 150
GPLFLLPGLL ITCHISHISL PAGYREEMVR YLRSVQLPDG GWGLHIEDKS
160 170 180 190 200
TVFGTALNYV ALRILGIGPD DPDLVRARNV LHKKGGAVAI PSWGKFWLAV
210 220 230 240 250
LNVYSWEGLN TLFPEMWLFP EWVPAHPSTL WCHCRQVYLP MSYCYATRLS
260 270 280 290 300
ASEDPLVQSL RQELYVQDYA SIDWPAQRNN VSPDEMYTPH SWLLHVVYGL
310 320 330 340 350
LNLYERFHST SLRKWAVQML YEHIAADDCF TKCISIGPIS KTINMLVRWS
360 370 380 390 400
VDGPSSPAFQ EHVSRIKDYL WLGLDGMKMQ GTNGSQIWDT SFAIQALLEA
410 420 430 440 450
GAHHRPEFLP CLQKAHEFLR LSQVPENCPD YQKYYRHMRK GGFSFSTLDC
460 470 480 490 500
GWIVADCTAE GLKAVLLLQN QCPSITEHIP RERLCDAVDV LLSLRNADGG
510 520 530 540 550
FATYEKKRGG YLLELLNPSE VFGDIMIDYT YVECTSAVMQ ALKHFHEHFP
560 570 580 590 600
DYRAAEVRET LNQGLDFCRR KQRADGSWEG SWGVCFTYGT WFGLEAFACM
610 620 630 640 650
GHTYQDGAAC AEVAQACNFL LSQQMADGGW GEDFESCEQR RYVQSARSQV
660 670 680 690 700
HSTCWALMGL MAVRHPDITA QERGIRCLLG KQLPNGDWPQ ENISGVFNKS
710 720 730
CAISYTSYRN IFPIWALGRF SNLYPDNTLA GHI
Length:733
Mass (Da):83,141
Last modified:March 29, 2005 - v2
Checksum:i17C3ED638C0D66B0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti297 – 2971V → A in BAC37102 (PubMed:16141072).Curated
Sequence conflicti347 – 3471V → A in BAC31739 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK044016 mRNA. Translation: BAC31739.1.
AK078023 mRNA. Translation: BAC37102.1.
BC029082 mRNA. Translation: AAH29082.1.
CCDSiCCDS23948.1.
RefSeqiNP_666118.1. NM_146006.1.
UniGeneiMm.55075.

Genome annotation databases

EnsembliENSMUST00000048678; ENSMUSP00000046856; ENSMUSG00000033105.
GeneIDi16987.
KEGGimmu:16987.
UCSCiuc007fuq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK044016 mRNA. Translation: BAC31739.1.
AK078023 mRNA. Translation: BAC37102.1.
BC029082 mRNA. Translation: AAH29082.1.
CCDSiCCDS23948.1.
RefSeqiNP_666118.1. NM_146006.1.
UniGeneiMm.55075.

3D structure databases

ProteinModelPortaliQ8BLN5.
SMRiQ8BLN5. Positions 6-732.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ8BLN5.

Proteomic databases

MaxQBiQ8BLN5.
PaxDbiQ8BLN5.
PRIDEiQ8BLN5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000048678; ENSMUSP00000046856; ENSMUSG00000033105.
GeneIDi16987.
KEGGimmu:16987.
UCSCiuc007fuq.1. mouse.

Organism-specific databases

CTDi4047.
MGIiMGI:1336155. Lss.

Phylogenomic databases

eggNOGiCOG1657.
GeneTreeiENSGT00390000011570.
HOGENOMiHOG000234317.
HOVERGENiHBG005604.
InParanoidiQ8BLN5.
KOiK01852.
OMAiTARCVSM.
OrthoDBiEOG70W3CN.
PhylomeDBiQ8BLN5.
TreeFamiTF300406.

Enzyme and pathway databases

UniPathwayiUPA00767; UER00753.
ReactomeiREACT_198969. Activation of gene expression by SREBF (SREBP).
REACT_208531. Cholesterol biosynthesis.

Miscellaneous databases

NextBioi291072.
PROiQ8BLN5.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BLN5.
CleanExiMM_LSS.
ExpressionAtlasiQ8BLN5. baseline and differential.
GenevestigatoriQ8BLN5.

Family and domain databases

Gene3Di1.50.10.20. 2 hits.
InterProiIPR001330. Prenyltrans.
IPR018333. Squalene_cyclase.
IPR002365. Terpene_synthase_CS.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PfamiPF00432. Prenyltrans. 1 hit.
[Graphical view]
SUPFAMiSSF48239. SSF48239. 2 hits.
TIGRFAMsiTIGR01787. squalene_cyclas. 1 hit.
PROSITEiPS01074. TERPENE_SYNTHASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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 tumorImported.

Entry informationi

Entry nameiERG7_MOUSE
AccessioniPrimary (citable) accession number: Q8BLN5
Secondary accession number(s): Q8BVJ4, Q8K307
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: March 4, 2015
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.