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A0A485P362 · A0A485P362_LYNPA

Function

function

Sterol 14alpha-demethylase that plays a critical role in the cholesterol biosynthesis pathway, being cholesterol the major sterol component in mammalian membranes as well as a precursor for bile acid and steroid hormone synthesis. Cytochrome P450 monooxygenase that catalyzes the three-step oxidative removal of the 14alpha-methyl group (C-32) of sterols such as lanosterol (lanosta-8,24-dien-3beta-ol) and 24,25-dihydrolanosterol (DHL) in the form of formate, and converts the sterols to 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol and 4,4-dimethyl-8,14-cholestadien-3beta-ol, respectively, which are intermediates of cholesterol biosynthesis. Can also demethylate substrates not intrinsic to mammals, such as eburicol (24-methylene-24,25-dihydrolanosterol), but at a lower rate than DHL.

Catalytic activity

  • 24,25-dihydrolanosterol + 3 reduced [NADPH--hemoprotein reductase] + 3 O2 = 4,4-dimethyl-8,14-cholestadien-3beta-ol + formate + 3 oxidized [NADPH--hemoprotein reductase] + 4 H2O + 4 H+
    This reaction proceeds in the forward direction.
  • 24,25-dihydrolanosterol + reduced [NADPH--hemoprotein reductase] + O2 = 32-hydroxy-24,25-dihydrolanosterol + oxidized [NADPH--hemoprotein reductase] + H2O + H+
    This reaction proceeds in the forward direction.
  • 32-hydroxy-24,25-dihydrolanosterol + reduced [NADPH--hemoprotein reductase] + O2 = 32-oxo-24,25-dihydrolanosterol + oxidized [NADPH--hemoprotein reductase] + 2 H2O + H+
    This reaction proceeds in the forward direction.
  • 32-hydroxylanosterol + reduced [NADPH--hemoprotein reductase] + O2 = 32-oxolanosterol + oxidized [NADPH--hemoprotein reductase] + 2 H2O + H+
    This reaction proceeds in the forward direction.
  • 32-oxo-24,25-dihydrolanosterol + reduced [NADPH--hemoprotein reductase] + O2 = 4,4-dimethyl-8,14-cholestadien-3beta-ol + formate + oxidized [NADPH--hemoprotein reductase] + H2O + 2 H+
    This reaction proceeds in the forward direction.
  • 32-oxolanosterol + reduced [NADPH--hemoprotein reductase] + O2 = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + oxidized [NADPH--hemoprotein reductase] + H2O + 2 H+
    This reaction proceeds in the forward direction.
  • a 14alpha-formyl steroid + reduced [NADPH--hemoprotein reductase] + O2 = a Delta14 steroid + formate + oxidized [NADPH--hemoprotein reductase] + H2O + 2 H+
    This reaction proceeds in the forward direction.
  • a 14alpha-hydroxymethyl steroid + reduced [NADPH--hemoprotein reductase] + O2 = a 14alpha-formyl steroid + oxidized [NADPH--hemoprotein reductase] + 2 H2O + H+
    This reaction proceeds in the forward direction.
  • a 14alpha-methyl steroid + 3 reduced [NADPH--hemoprotein reductase] + 3 O2 = a Delta14 steroid + formate + 3 oxidized [NADPH--hemoprotein reductase] + 4 H2O + 4 H+
    This reaction proceeds in the forward direction.
    EC:1.14.14.154 (UniProtKB | ENZYME | Rhea)
  • a 14alpha-methyl steroid + reduced [NADPH--hemoprotein reductase] + O2 = a 14alpha-hydroxymethyl steroid + oxidized [NADPH--hemoprotein reductase] + H2O + H+
    This reaction proceeds in the forward direction.
  • lanosterol + 3 reduced [NADPH--hemoprotein reductase] + 3 O2 = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + 3 oxidized [NADPH--hemoprotein reductase] + 4 H2O + 4 H+
    This reaction proceeds in the forward direction.
    EC:1.14.14.154 (UniProtKB | ENZYME | Rhea)
  • lanosterol + reduced [NADPH--hemoprotein reductase] + O2 = 32-hydroxylanosterol + oxidized [NADPH--hemoprotein reductase] + H2O + H+
    This reaction proceeds in the forward direction.

Cofactor

heme (UniProtKB | Rhea| CHEBI:30413 )

Pathway

Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 1/6.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site449Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue

GO annotations

AspectTerm
Cellular Componentendoplasmic reticulum membrane
Molecular Functionheme binding
Molecular Functioniron ion binding
Molecular Functionmonooxygenase activity
Molecular Functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
Biological Processcholesterol metabolic process
Biological Processorganic hydroxy compound biosynthetic process
Biological Processsmall molecule biosynthetic process
Biological Processsteroid biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Lanosterol 14-alpha demethylase
  • EC number
  • Alternative names
    • CYPLI
    • Cytochrome P450 51A1
    • Cytochrome P450-14DM
    • Cytochrome P450LI

Gene names

    • ORF names
      LYPA_23C002699

Organism names

Accessions

  • Primary accession
    A0A485P362

Proteomes

Subcellular Location

Microsome membrane
; Single-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane25-44Helical

Keywords

Family & Domains

Sequence similarities

Belongs to the cytochrome P450 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    503
  • Mass (Da)
    56,828
  • Last updated
    2019-06-05 v1
  • MD5 Checksum
    8C92FDC4F6CC1674B90264DB68FE3AF9
MLLLGLLQAGGSVLGQAMERVTGGNLLSMLLIACAFTLGLVYLFRLAVGHLAPMPPGAKSPPYIFSPIPFLGHAIAFGKSPIEFLENAYEKYGPVFSFTMVGKTFTYLLGSDAAALLFNSKNEDLNAEDVYSRLTTPVFGKGVAYDVPNPVFLEQKKMLKSGLNIAHFRQHVSIIEKETKEYFQSWGESGEKNLFEALSELIILTASHCLHGKEIRSQLNEKVAQLYADLDGGFSHAAWLLPGWLPLPSFRRRDRAHREIKNIFYKAIQKRRQSEEKLDDILQTLLDSTYKDGRPLTDDEVAGMLIGLLLAGQHTSSTTSAWMGFFLARDKTLQEKCYLEQKTVCGEDLPPLTYDQLKDLNVLDRCIKETLRLRPPIMTMMRMAKTPQTVAGYTIPPGHQVCVSPTVNQRLKDSWVERLDFNPDRYLQDNPASGEKFAYVPFGAGRHRCIGENFAYVQIKTIWSTMLRLYEFDLIDGYFPTVNYTTMIHTPENPVIRYKRRSK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CAAGRJ010028562
EMBL· GenBank· DDBJ
VFV40160.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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