Overview
| Uniprot ID | P50578 |
|---|
| Protein Name | Aldo-keto reductase family 1 member A1 |
|---|
| Gene Name | AKR1A1 |
|---|
| Organism | Sus scrofa |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 257 |
LRWQVQRKVICIPKS |
| 263 |
RKVICIPKSVTPSRI |
| 30 |
KSEPGQVKAAIKYAL |
| 85 |
TSKLWNTKHHPEDVE |
Function
Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosaccharides and bile acids, with a preference for negatively charged substrates, such as glucuronate and succinic semialdehyde (By similarity). Plays an important role in ascorbic acid biosynthesis by catalyzing the reduction of D-glucuronic acid and D-glucurono-gamma-lactone (By similarity). Functions as a detoxifiying enzyme by reducing a range of toxic aldehydes. Reduces methylglyoxal and 3-deoxyglucosone, which are present at elevated levels under hyperglycemic conditions and are cytotoxic. Involved also in the detoxification of lipid-derived aldehydes like acrolein (By similarity). Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs (By similarity). Also acts as an inhibitor of protein S-nitrosylation by mediating degradation of S-nitroso-coenzyme A (S-nitroso-CoA), a cofactor required to S-nitrosylate proteins (By similarity). S-nitroso-CoA reductase activity is involved in reprogramming intermediary metabolism in renal proximal tubules, notably by inhibiting protein S-nitrosylation of isoform 2 of PKM (PKM2) (By similarity). Also acts as a S-nitroso-glutathione reductase by catalyzing the NADPH-dependent reduction of S-nitrosoglutathione (By similarity). Displays no reductase activity towards retinoids (PubMed:12732097)
Protein Sequence
10
MAASCVLLHT
20
GQKMPLIGLG
30
TWKSEPGQVK
40
AAIKYALTVG
50
YRHIDCAAIY
60
GNELEIGEAL
70
QETVGPGKAV
80
PREELFVTSK
90
LWNTKHHPED
100
VEPALRKTLA
110
DLQLEYLDLY
120
LMHWPYAFER
130
GDNPFPKNAD
140
GTIRYDATHY
150
KDTWKALEAL
160
VAKGLVRALG
170
LSNFSSRQID
180
DVLSVASVRP
190
AVLQVECHPY
200
LAQNELIAHC
210
QARGLEVTAY
220
SPLGSSDRAW
230
RDPNEPVLLE
240
EPVVQALAEK
250
YNRSPAQILL
260
RWQVQRKVIC
270
IPKSVTPSRI
280
LQNIQVFDFT
290
FSPEEMKQLD
300
ALNKNLRFIV
310
PMLTVDGKRV
320
PRDAGHPLYP
FNDPY
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0016324 |
apical plasma membrane |
| Biological Process |
GO:0006629 |
lipid metabolic process |
| Cellular Component |
GO:0005829 |
cytosol |
| Molecular Function |
GO:0004032 |
aldose reductase (NADPH) activity |
| Molecular Function |
GO:0047655 |
allyl-alcohol dehydrogenase activity |
| Molecular Function |
GO:0047941 |
glucuronolactone reductase activity |
| Molecular Function |
GO:0047956 |
glycerol dehydrogenase (NADP+) activity |
| Molecular Function |
GO:0047939 |
L-glucuronate reductase activity |
| Molecular Function |
GO:1990002 |
methylglyoxal reductase (NADPH) (acetol producing) activity |
| Molecular Function |
GO:0160163 |
S-nitrosoglutathione reductase (NADPH) activity |
| Biological Process |
GO:0046185 |
aldehyde catabolic process |
| Biological Process |
GO:0110095 |
cellular detoxification of aldehyde |
| Biological Process |
GO:0042840 |
D-glucuronate catabolic process |
| Biological Process |
GO:0019853 |
L-ascorbic acid biosynthetic process |
Reference
[1] Fan S, Zhou R, Wen H, Ye H, Ma S et al.. Global profiling of protein lactylome in porcine granulosa cells.. J Ovarian Res 18(1):177. 2025 Aug 8. PMID: 40781717.