P47199 · QOR_MOUSE
- ProteinQuinone oxidoreductase
- GeneCryz
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids331 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Does not have alcohol dehydrogenase activity. Binds NADP and acts through a one-electron transfer process. Orthoquinones, such as 1,2-naphthoquinone or 9,10-phenanthrenequinone, are the best substrates (in vitro). May act in the detoxification of xenobiotics. Interacts with (AU)-rich elements (ARE) in the 3'-UTR of target mRNA species and enhances their stability. NADPH binding interferes with mRNA binding (By similarity).
Catalytic activity
- 2 a quinone + H+ + NADPH = 2 a 1,4-benzosemiquinone + NADP+
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 53 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 158-161 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SGGV | ||||||
Binding site | 181 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 200 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 231 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 248-251 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: VGCR | ||||||
Binding site | 271-273 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: VSL |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | identical protein binding | |
Molecular Function | mRNA 3'-UTR binding | |
Molecular Function | NADP binding | |
Molecular Function | NADPH binding | |
Molecular Function | NADPH:quinone reductase activity | |
Molecular Function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor | |
Molecular Function | zinc ion binding | |
Biological Process | protein homotetramerization | |
Biological Process | xenobiotic catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameQuinone oxidoreductase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP47199
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 25 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000160908 | 2-331 | Quinone oxidoreductase | |||
Sequence: ATGQKLMRAIRVFEFGGPEVLKLQSDVVVPVPQSHQVLIKVHACGVNPVETYIRSGAYSRKPALPYTPGSDVAGIIESVGDKVSAFKKGDRVFCYSTVSGGYAEFALAADDTIYPLPETLNFRQGAALGIPYFTACRALFHSARARAGESVLVHGASGGVGLATCQIARAHGLKVLGTAGSEEGKKLVLQNGAHEVFNHKEANYIDKIKMSVGDKDKGVDVIIEMLANENLSNDLKLLSHGGRVVVVGCRGPIEINPRDTMAKETSIIGVSLSSSTKEEFQQFAGLLQAGIEKGWVKPVIGSEYPLEKAAQAHEDIIHGSGKTGKMILLL | ||||||
Modified residue | 23 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 35 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 186 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 298 | N6-succinyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Length331
- Mass (Da)35,269
- Last updated1995-11-01 v1
- Checksum35816C043EFE16A2
Computationally mapped potential isoform sequences
There are 8 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
V9GXY8 | V9GXY8_MOUSE | Cryz | 223 | ||
A0A0A6YVS7 | A0A0A6YVS7_MOUSE | Cryz | 171 | ||
A0A0A6YXR4 | A0A0A6YXR4_MOUSE | Cryz | 301 | ||
D3YUG9 | D3YUG9_MOUSE | Cryz | 173 | ||
D3YWU6 | D3YWU6_MOUSE | Cryz | 97 | ||
D3Z4Q4 | D3Z4Q4_MOUSE | Cryz | 137 | ||
D3Z2X0 | D3Z2X0_MOUSE | Cryz | 152 | ||
A0A0G2JFU5 | A0A0G2JFU5_MOUSE | Cryz | 56 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 58 | in Ref. 2; AAH03800 | ||||
Sequence: A → T | ||||||
Sequence conflict | 131-133 | in Ref. 3; BAA11463 | ||||
Sequence: IPY → TMD |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
S70056 EMBL· GenBank· DDBJ | AAB30620.2 EMBL· GenBank· DDBJ | mRNA | ||
BC003800 EMBL· GenBank· DDBJ | AAH03800.1 EMBL· GenBank· DDBJ | mRNA | ||
D78646 EMBL· GenBank· DDBJ | BAA11463.1 EMBL· GenBank· DDBJ | mRNA |