QSOX1
Function
Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide (PubMed:17331072, PubMed:18393449, PubMed:23704371, PubMed:23867277, PubMed:30367560). Plays a role in disulfide bond formation in a variety of extracellular proteins (PubMed:17331072, PubMed:22801504, PubMed:23867277, PubMed:30367560). In fibroblasts, required for normal incorporation of laminin into the extracellular matrix, and thereby for normal cell-cell adhesion and cell migration (PubMed:23704371, PubMed:23867277, PubMed:30367560).
Post-translational modifications
N-glycosylated (PubMed:17331072, PubMed:29757379). O-glycosylated on Thr and Ser residues (PubMed:29757379).
Sequence Similarities
Belongs to the quiescin-sulfhydryl oxidase (QSOX) family.
Tissue Specificity
Expressed in heart, placenta, lung, liver, skeletal muscle, pancreas and very weakly in brain and kidney.
Cellular localization
- Isoform 1
- Golgi apparatus membrane
- Single-pass membrane protein
- Secreted
- A small proportion is secreted, probably via a proteolytic cleavage that removes the membrane anchor.
- Isoform 2
- Secreted
- Found in the extracellular medium of quiescent cells but is not found in proliferating cells.
Alternative names
QSCN6, UNQ2520/PRO6013, QSOX1, Sulfhydryl oxidase 1, hQSOX, Quiescin Q6