O08841 · QSOX1_CAVPO
- ProteinSulfhydryl oxidase 1
- GeneQSOX1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids613 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
- O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR'
Cofactor
Note: Binds 1 FAD per subunit.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 71 | Nucleophile | ||||
Sequence: C | ||||||
Active site | 74 | Nucleophile | ||||
Sequence: C | ||||||
Binding site | 402 | FAD (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 409 | FAD (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 413 | FAD (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 452 | FAD (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 456 | FAD (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 479-486 | FAD (UniProtKB | ChEBI) | ||||
Sequence: WTSHNRVN | ||||||
Binding site | 501 | FAD (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 504 | FAD (UniProtKB | ChEBI) | ||||
Sequence: W |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular exosome | |
Cellular Component | extracellular space | |
Cellular Component | Golgi membrane | |
Cellular Component | intercellular bridge | |
Molecular Function | FAD binding | |
Molecular Function | flavin-dependent sulfhydryl oxidase activity | |
Molecular Function | protein disulfide isomerase activity | |
Biological Process | extracellular matrix assembly | |
Biological Process | negative regulation of macroautophagy | |
Biological Process | protein folding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSulfhydryl oxidase 1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Hystricomorpha > Caviidae > Cavia
Accessions
- Primary accessionO08841
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-30 | |||||
Sequence: MTGCGRRSGWLPPLRLLLLPLLLGGPGVGA | ||||||
Chain | PRO_0000249536 | 31-613 | Sulfhydryl oxidase 1 | |||
Sequence: AQLAALYSASDPLTLLQADTVRSTVLNSPSAWAVEFFASWCGHCIAFAPTWKALAKDIKDWRPALNLAALNCADETNNAVCRDFNIAGFPSVRFFKAFSKNSTGTTLPVAGANVQMLRERLIDALESHHDTWPSACPPLEPVKPKEIDTFFARNNQEYLVLIFEQENSYLGREVTLDLSQHHDLVVRRVLSTEANVVRKFGVADFPSCYLLFRNGSVSRVPVLVESRRFYTAYLQRLSEVTREGTPTPAVPTISDQIAPTVWKFADRSKIYMADLESALHYILRVEVGRFSVLEGQRLMALKKFVTVLTKYFPGQPLVRNFLQSTNEWLKRQHKKKMPYSFFKTAMDSRNEEAVITKEVNWVGCQGSESHFRGFPCSLWILFHFLTVQASQKNAESSQKPANGQEVLQAIRNYVRFFFGCRDCANHFEQMAAGSMHRVKSPNDAVLWLWTSHNRVNARLAGAPSEDPQFPKVQWPPPELCSACHNELSGEPVWDVDATLRFLKTHFSPSNIVLNFPPAEPASRSSVHSWGATPHLELDALGLVTRNSALALERAEISESPGSNAMPNIPAERPELFEALSHSR | ||||||
Disulfide bond | 71↔74 | Redox-active | ||||
Sequence: CGHC | ||||||
Disulfide bond | 102↔111 | |||||
Sequence: CADETNNAVC | ||||||
Glycosylation | 131 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 244 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 394↔406 | |||||
Sequence: CQGSESHFRGFPC | ||||||
Modified residue | 427 | Phosphoserine | ||||
Sequence: S | ||||||
Disulfide bond | 450↔453 | |||||
Sequence: CRDC | ||||||
Disulfide bond | 510↔513 | |||||
Sequence: CSAC |
Post-translational modification
N-glycosylated. O-glycosylated on Thr and Ser residues.
Keywords
- PTM
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
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 37-157 | Thioredoxin | ||||
Sequence: YSASDPLTLLQADTVRSTVLNSPSAWAVEFFASWCGHCIAFAPTWKALAKDIKDWRPALNLAALNCADETNNAVCRDFNIAGFPSVRFFKAFSKNSTGTTLPVAGANVQMLRERLIDALES | ||||||
Domain | 397-504 | ERV/ALR sulfhydryl oxidase | ||||
Sequence: SESHFRGFPCSLWILFHFLTVQASQKNAESSQKPANGQEVLQAIRNYVRFFFGCRDCANHFEQMAAGSMHRVKSPNDAVLWLWTSHNRVNARLAGAPSEDPQFPKVQW |
Sequence similarities
Belongs to the quiescin-sulfhydryl oxidase (QSOX) family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length613
- Mass (Da)68,595
- Last updated2001-03-01 v2
- Checksum34105EF608CA7B55
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U82982 EMBL· GenBank· DDBJ | AAB58401.2 EMBL· GenBank· DDBJ | mRNA |