Q63042 · ALR_RAT
- ProteinFAD-linked sulfhydryl oxidase ALR
- GeneGfer
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids198 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
FAD-dependent sulfhydryl oxidase that regenerates the redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with GFER/ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re-oxidized by donating electrons to cytochrome c or molecular oxygen. May have a function in liver regeneration and spermatogenesis.
Catalytic activity
- O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR'
Cofactor
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 92-100 | FAD (UniProtKB | ChEBI) | ||||
Sequence: REELGRNTW | ||||||
Binding site | 104 | FAD (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 133 | FAD (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 164-176 | FAD (UniProtKB | ChEBI) | ||||
Sequence: CRLHNEVNRKLGK | ||||||
Binding site | 187-188 | FAD (UniProtKB | ChEBI) | ||||
Sequence: RW |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | extracellular space | |
Cellular Component | mitochondrial intermembrane space | |
Cellular Component | mitochondrion | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | flavin-dependent sulfhydryl oxidase activity | |
Molecular Function | growth factor activity | |
Molecular Function | protein-disulfide reductase activity | |
Biological Process | cellular response to actinomycin D | |
Biological Process | cellular response to lipopolysaccharide | |
Biological Process | cellular response to toxic substance | |
Biological Process | cellular response to tumor necrosis factor | |
Biological Process | liver development | |
Biological Process | liver regeneration | |
Biological Process | negative regulation of apoptotic process | |
Biological Process | negative regulation of natural killer cell mediated cytotoxicity | |
Biological Process | positive regulation of DNA biosynthetic process | |
Biological Process | response to lipopolysaccharide |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFAD-linked sulfhydryl oxidase ALR
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ63042
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000208550 | 1-198 | FAD-linked sulfhydryl oxidase ALR | |||
Sequence: MAAPSEPAGFPRGSRFSFLPGGAHSEMTDDLVTDARGRGARHRKDNAPAAAPAPKGLEHGKRPCRACVDFKSWMRTQQKRDIKFREDCPQDREELGRNTWAFLHTLAAYYPDMPTPEQQQDMAQFIHIFSKFYPCEECAEDIRKRIDRSQPDTSTRVSFSQWLCRLHNEVNRKLGKPDFDCSRVDERWRDGWKDGSCD | ||||||
Disulfide bond | 88 | Interchain (with C-197) | ||||
Sequence: C | ||||||
Disulfide bond | 135↔138 | Redox-active | ||||
Sequence: CEEC | ||||||
Disulfide bond | 164↔181 | |||||
Sequence: CRLHNEVNRKLGKPDFDC | ||||||
Disulfide bond | 197 | Interchain (with C-88) | ||||
Sequence: C |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-59 | Disordered | ||||
Sequence: MAAPSEPAGFPRGSRFSFLPGGAHSEMTDDLVTDARGRGARHRKDNAPAAAPAPKGLEH | ||||||
Compositional bias | 29-45 | Basic and acidic residues | ||||
Sequence: DDLVTDARGRGARHRKD | ||||||
Domain | 88-188 | ERV/ALR sulfhydryl oxidase | ||||
Sequence: CPQDREELGRNTWAFLHTLAAYYPDMPTPEQQQDMAQFIHIFSKFYPCEECAEDIRKRIDRSQPDTSTRVSFSQWLCRLHNEVNRKLGKPDFDCSRVDERW |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length198
- Mass (Da)22,837
- Last updated2008-12-16 v2
- Checksum46AD9BEC2EF0C393
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 29-45 | Basic and acidic residues | ||||
Sequence: DDLVTDARGRGARHRKD |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D30735 EMBL· GenBank· DDBJ | BAA06399.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AF197192 EMBL· GenBank· DDBJ | AAF12808.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation |