Skip Header

Contribute Send feedback
Read comments (?) or add your own

P84466 (ERG7_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length732 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Enzyme regulation

Inhibited by the benzophenone containing OSC inhibitor Ro48-8071 and to a lesser extent by other benzophene containing inhibitors. Ref.2

Pathway

Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl diphosphate: step 3/3. Ref.2

Subunit structure

Monomer By similarity.

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein By similarity.

Tissue specificity

Detected in the liver (at protein level). Ref.2

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the terpene cyclase/mutase family. UniProtKB P48449

Contains 5 PFTB repeats.

Biophysicochemical properties

Kinetic parameters:

KM=11 µM for (3S)-2,3-oxidosqualine Ref.2

pH dependence:

Optimum pH is 7.4. Active from pH 5.0 to 10.0. Ref.2

Temperature dependence:

Optimum temperature is 37 degrees Celsius. Active from 25 to 50 degrees Celsius. Ref.2

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionlanosterol synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 732731Lanosterol synthase
PRO_0000072658

Regions

Repeat124 – 16542PFTB 1
Repeat483 – 52846PFTB 2
Repeat560 – 60041PFTB 3
Repeat612 – 66352PFTB 4
Repeat670 – 71243PFTB 5

Sites

Active site2321Proton acceptor By similarity
Active site4551Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
P84466 [UniParc].

Last modified June 27, 2006. Version 2.
Checksum: B06289C2FE03B4B2

FASTA73283,184
        10         20         30         40         50         60 
MTEGTCLRRR GGPYKTEPAT DLSRWRLSNQ VGRQTWTYSQ EEDPVREQSG LEAHLLGLDT 

        70         80         90        100        110        120 
KSFFKDLPKA HTACRGALNG VTFYAALQTE DGHWAGDYGG PLFLLPGLLI TCHVANIPLP 

       130        140        150        160        170        180 
AGYREEIIRY LRSVQLPDGG WGLHIEDKST VFGTALNYVS LRILGVGPDD PDLVRARNLL 

       190        200        210        220        230        240 
HKKGGAVFIP SWGKFWLAVL NVYSWEGLNT LFPEMWLFPD WMPAHPSTIW CHCRQVYLPM 

       250        260        270        280        290        300 
AYCYSTRLSA EEGPLVQSLR QELYLEDYSC IDWAAHRNSV APDDLYTPHS WLLHVVYAIL 

       310        320        330        340        350        360 
NLYERHHSTS LRQWATQKLY EHIAADDRFT KCISIGPISK TINMLVRWHV DGPASAVFQE 

       370        380        390        400        410        420 
HVSRIPDYLW LGLDGMKMQG TNGSQIWDTA FAIQALLEAR AQHRPEFWSC LRKAHEYLRI 

       430        440        450        460        470        480 
SQVPDNFPDY QKYYRHMSKG GFSFSTLDCG WIVADCTAEA LKSILLLQEK CPFVSNHVPR 

       490        500        510        520        530        540 
ERLFDTVAVL LSLRNPDGGF ATYETKRGGH LLELLNPSEV FGDIMIDYTY VECTSAVMQA 

       550        560        570        580        590        600 
LKTFHKQFPD HRAGEIRETL EQGLQFCRQK QRPDGSWEGS WGVCFTYGAW FGLEAFACMG 

       610        620        630        640        650        660 
HTYHNGVACA EISRACDFLL SRQMADGGWG EDFESCKQRR YVQSAQSQIH NTCWALMGLM 

       670        680        690        700        710        720 
AVRHPDVAAL ERGVSYLLEK QLPNGDWPQE NISGVFNKSC AISYTSYRNV FPIWTLGRFS 

       730 
RLHPDPALAG HP

« Hide

References

[1]"Molecular cloning and active-site mapping of oxidosqualene-lanosterol cyclase from bovine liver."
Chang C.-H., Huang C.-Y., Ko C.-Y., Wu T.-K.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Purification, tandem mass characterization, and inhibition studies of oxidosqualene-lanosterol cyclase enzyme from bovine liver."
Wu T.-K., Huang C.-Y., Ko C.-Y., Chang C.-H., Chen Y.-J., Liao H.-K.
Arch. Biochem. Biophys. 421:42-53(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 163-174; 247-258 AND 493-506, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, TISSUE SPECIFICITY.
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		DQ372933 mRNA. Translation: ABD24094.1.
IPIIPI00688804.
RefSeqNP_001040029.1. NM_001046564.1.
UniGeneBt.46034.

3D structure databases

ProteinModelPortalP84466.
SMRP84466. Positions 6-732.
ModBaseSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000025201.

Proteomic databases

PRIDEP84466.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID615906.
KEGGbta:615906.

Organism-specific databases

CTD4047.

Phylogenomic databases

eggNOGCOG1657.
HOGENOMHOG000234317.
HOVERGENHBG005604.
InParanoidP84466.
KOK01852.
OrthoDBEOG4SQWW4.

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. 1 hit.
[Graphical view]
SUPFAMSSF48239. Terp_cyc_toroid. 2 hits.
TIGRFAMsTIGR01787. squalene_cyclas. 1 hit.
PROSITEPS01074. TERPENE_SYNTHASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20899856.

Entry information

Entry nameERG7_BOVIN
AccessionPrimary (citable) accession number: P84466
Secondary accession number(s): Q2EMV7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: June 27, 2006
Last modified: April 3, 2013
This is version 53 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents