P84466 · LSS_BOVIN

  • Protein
    Lanosterol synthase
  • Gene
    LSS
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Key enzyme in the cholesterol biosynthesis pathway. Catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol nucleus (PubMed:14678783).
Through the production of lanosterol may regulate lens protein aggregation and increase transparency (By similarity).

Catalytic activity

Activity regulation

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

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
11 μM(3S)-2,3-oxidosqualine

pH Dependence

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

Temperature Dependence

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

Pathway

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

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site455Proton donor

GO annotations

AspectTerm
Cellular Componentendoplasmic reticulum membrane
Cellular Componentlipid droplet
Molecular Functionlanosterol synthase activity
Biological Processcholesterol biosynthetic process
Biological Processsteroid biosynthetic process
Biological Processtriterpenoid biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Lanosterol synthase
  • EC number
  • Alternative names
    • 2,3-epoxysqualene--lanosterol cyclase
    • Oxidosqualene--lanosterol cyclase (OSC)

Gene names

    • Name
      LSS

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos

Accessions

  • Primary accession
    P84466
  • Secondary accessions
    • Q2EMV7

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylthreonine
ChainPRO_00000726582-732Lanosterol synthase

Post-translational modification

The N-terminus is blocked.

Keywords

Proteomic databases

Expression

Tissue specificity

Detected in the liver (at protein level).

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for repeat.

TypeIDPosition(s)Description
Repeat124-165PFTB 1
Repeat483-528PFTB 2
Repeat560-600PFTB 3
Repeat612-663PFTB 4
Repeat670-712PFTB 5

Sequence similarities

Belongs to the terpene cyclase/mutase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    732
  • Mass (Da)
    83,184
  • Last updated
    2006-06-27 v2
  • Checksum
    B06289C2FE03B4B2
MTEGTCLRRRGGPYKTEPATDLSRWRLSNQVGRQTWTYSQEEDPVREQSGLEAHLLGLDTKSFFKDLPKAHTACRGALNGVTFYAALQTEDGHWAGDYGGPLFLLPGLLITCHVANIPLPAGYREEIIRYLRSVQLPDGGWGLHIEDKSTVFGTALNYVSLRILGVGPDDPDLVRARNLLHKKGGAVFIPSWGKFWLAVLNVYSWEGLNTLFPEMWLFPDWMPAHPSTIWCHCRQVYLPMAYCYSTRLSAEEGPLVQSLRQELYLEDYSCIDWAAHRNSVAPDDLYTPHSWLLHVVYAILNLYERHHSTSLRQWATQKLYEHIAADDRFTKCISIGPISKTINMLVRWHVDGPASAVFQEHVSRIPDYLWLGLDGMKMQGTNGSQIWDTAFAIQALLEARAQHRPEFWSCLRKAHEYLRISQVPDNFPDYQKYYRHMSKGGFSFSTLDCGWIVADCTAEALKSILLLQEKCPFVSNHVPRERLFDTVAVLLSLRNPDGGFATYETKRGGHLLELLNPSEVFGDIMIDYTYVECTSAVMQALKTFHKQFPDHRAGEIRETLEQGLQFCRQKQRPDGSWEGSWGVCFTYGAWFGLEAFACMGHTYHNGVACAEISRACDFLLSRQMADGGWGEDFESCKQRRYVQSAQSQIHNTCWALMGLMAVRHPDVAALERGVSYLLEKQLPNGDWPQENISGVFNKSCAISYTSYRNVFPIWTLGRFSRLHPDPALAGHP

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DQ372933
EMBL· GenBank· DDBJ
ABD24094.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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