O08841 · QSOX1_CAVPO

Function

function

Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. Plays a role in disulfide bond formation in a variety of extracellular proteins. In fibroblasts, required for normal incorporation of laminin into the extracellular matrix, and thereby for normal cell-cell adhesion and cell migration.

Catalytic activity

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

Note: Binds 1 FAD per subunit.

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site71Nucleophile
Active site74Nucleophile
Binding site402FAD (UniProtKB | ChEBI)
Binding site409FAD (UniProtKB | ChEBI)
Binding site413FAD (UniProtKB | ChEBI)
Binding site452FAD (UniProtKB | ChEBI)
Binding site456FAD (UniProtKB | ChEBI)
Binding site479-486FAD (UniProtKB | ChEBI)
Binding site501FAD (UniProtKB | ChEBI)
Binding site504FAD (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular exosome
Cellular Componentextracellular space
Cellular ComponentGolgi membrane
Cellular Componentintercellular bridge
Molecular FunctionFAD binding
Molecular Functionflavin-dependent sulfhydryl oxidase activity
Molecular Functionprotein disulfide isomerase activity
Biological Processextracellular matrix assembly
Biological Processnegative regulation of macroautophagy
Biological Processprotein folding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Sulfhydryl oxidase 1
  • EC number
  • Alternative names
    • FAD-dependent sulfhydryl oxidase-3
      (SOx-3
      )
    • Glandular epithelial cells protein 3
    • Quiescin Q6

Gene names

    • Name
      QSOX1
    • Synonyms
      GEC3, QSCN6, SOX3

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Hystricomorpha > Caviidae > Cavia

Accessions

  • Primary accession
    O08841

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation, modified residue.

TypeIDPosition(s)Description
Signal1-30
ChainPRO_000024953631-613Sulfhydryl oxidase 1
Disulfide bond71↔74Redox-active
Disulfide bond102↔111
Glycosylation131N-linked (GlcNAc...) asparagine
Glycosylation244N-linked (GlcNAc...) asparagine
Disulfide bond394↔406
Modified residue427Phosphoserine
Disulfide bond450↔453
Disulfide bond510↔513

Post-translational modification

N-glycosylated. O-glycosylated on Thr and Ser residues.

Keywords

PTM databases

Expression

Tissue specificity

Detected in endometrium and in uterus glandular epithelial cells (at protein level). Expressed in testis, placenta, pancreas, lung, ovary, endometrium, but not in brain, liver and kidney tissues. Higher expression in epithelial cells.

Gene expression databases

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain37-157Thioredoxin
Domain397-504ERV/ALR sulfhydryl oxidase

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    613
  • Mass (Da)
    68,595
  • Last updated
    2001-03-01 v2
  • Checksum
    34105EF608CA7B55
MTGCGRRSGWLPPLRLLLLPLLLGGPGVGAAQLAALYSASDPLTLLQADTVRSTVLNSPSAWAVEFFASWCGHCIAFAPTWKALAKDIKDWRPALNLAALNCADETNNAVCRDFNIAGFPSVRFFKAFSKNSTGTTLPVAGANVQMLRERLIDALESHHDTWPSACPPLEPVKPKEIDTFFARNNQEYLVLIFEQENSYLGREVTLDLSQHHDLVVRRVLSTEANVVRKFGVADFPSCYLLFRNGSVSRVPVLVESRRFYTAYLQRLSEVTREGTPTPAVPTISDQIAPTVWKFADRSKIYMADLESALHYILRVEVGRFSVLEGQRLMALKKFVTVLTKYFPGQPLVRNFLQSTNEWLKRQHKKKMPYSFFKTAMDSRNEEAVITKEVNWVGCQGSESHFRGFPCSLWILFHFLTVQASQKNAESSQKPANGQEVLQAIRNYVRFFFGCRDCANHFEQMAAGSMHRVKSPNDAVLWLWTSHNRVNARLAGAPSEDPQFPKVQWPPPELCSACHNELSGEPVWDVDATLRFLKTHFSPSNIVLNFPPAEPASRSSVHSWGATPHLELDALGLVTRNSALALERAEISESPGSNAMPNIPAERPELFEALSHSR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U82982
EMBL· GenBank· DDBJ
AAB58401.2
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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