O43488 · ARK72_HUMAN
- ProteinAflatoxin B1 aldehyde reductase member 2
- GeneAKR7A2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids359 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate. May have an important role in producing the neuromodulator gamma-hydroxybutyrate (GHB). Has broad substrate specificity. Has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). Can reduce 1,2-naphthoquinone and 9,10-phenanthrenequinone (in vitro). Can reduce the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. May be involved in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen.
Catalytic activity
- 4-hydroxybutanoate + NADP+ = H+ + NADPH + succinate semialdehyde
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
20 μM | succinic semialdehyde | |||||
17 μM | 2-carboxybenzaldehyde | |||||
8 μM | 9,10-phenanthrenequinone | |||||
102 μM | 1,2-naphthoquinone |
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 72 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 77 | Proton donor | ||||
Sequence: Y | ||||||
Site | 105 | Lowers pKa of active site Tyr | ||||
Sequence: K | ||||||
Binding site | 141 | substrate | ||||
Sequence: H | ||||||
Binding site | 171-172 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SN | ||||||
Binding site | 197 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 226-236 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: NPLAGGLLTGK | ||||||
Binding site | 250 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 260 | substrate | ||||
Sequence: Y | ||||||
Binding site | 263 | substrate | ||||
Sequence: R | ||||||
Binding site | 318-326 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SSLEQLEQN | ||||||
Binding site | 359 | substrate | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | extracellular exosome | |
Cellular Component | Golgi apparatus | |
Cellular Component | mitochondrion | |
Molecular Function | aldo-keto reductase (NADPH) activity | |
Molecular Function | aldose reductase (NADPH) activity | |
Molecular Function | electron transfer activity | |
Molecular Function | phenanthrene-9,10-epoxide hydrolase activity | |
Biological Process | carbohydrate metabolic process | |
Biological Process | cellular aldehyde metabolic process | |
Biological Process | daunorubicin metabolic process | |
Biological Process | doxorubicin metabolic process | |
Biological Process | lipid metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAflatoxin B1 aldehyde reductase member 2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO43488
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_048209 | 135 | in dbSNP:rs6670759 | |||
Sequence: V → M | ||||||
Natural variant | VAR_017413 | 142 | in dbSNP:rs1043657 | |||
Sequence: A → T | ||||||
Natural variant | VAR_017414 | 157 | in dbSNP:rs859208 | |||
Sequence: Q → H | ||||||
Natural variant | VAR_060222 | 180 | in dbSNP:rs859210 | |||
Sequence: E → K | ||||||
Natural variant | VAR_048210 | 198 | in dbSNP:rs2231200 | |||
Sequence: G → S | ||||||
Natural variant | VAR_017415 | 214 | in dbSNP:rs2235794 | |||
Sequence: C → Y | ||||||
Natural variant | VAR_048211 | 255 | in dbSNP:rs2231203 | |||
Sequence: S → N |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 498 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Transit peptide | 1-38 | UniProt | Mitochondrion | ||||
Sequence: MLSAASRVVSRAAVHCALRSPPPEARALAMSRPPPPRV | |||||||
Chain | PRO_0000070375 | 39-359 | UniProt | Aflatoxin B1 aldehyde reductase member 2 | |||
Sequence: ASVLGTMEMGRRMDAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLGLGGGDCRVKIATKANPWDGKSLKPDSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKSNGWILPTVYQGMYNATTRQVETELFPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKDGKQPVGRFFGNSWAETYRNRFWKEHHFEAIALVEKALQAAYGASAPSVTSAALRWMYHHSQLQGAHGDAVILGMSSLEQLEQNLAATEEGPLEPAVVDAFNQAWHLVAHECPNYFR | |||||||
Modified residue | 40 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 121 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 128 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 236 | UniProt | N6-succinyllysine | ||||
Sequence: K | |||||||
Modified residue | 255 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 255 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Tissue specificity
Detected in brain, liver, small intestine and testis, and at lower levels in heart, prostate, skeletal muscle and spleen. Detected in kidney proximal and distal tubules, endothelial cells lining the Bowman's capsules and some cysts. Detected at low levels in lung and pancreas (at protein level). Widely expressed.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homodimer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O43488 | AKR7A3 O95154 | 8 | EBI-748855, EBI-748869 | |
BINARY | O43488 | APBB2 Q92870-2 | 3 | EBI-748855, EBI-21535880 | |
BINARY | O43488 | ATXN3 P54252 | 3 | EBI-748855, EBI-946046 | |
BINARY | O43488 | CYGB Q8WWM9 | 3 | EBI-748855, EBI-6309037 | |
BINARY | O43488 | ZBTB1 Q9Y2K1 | 4 | EBI-748855, EBI-2682961 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length359
- Mass (Da)39,589
- Last updated2003-11-14 v3
- Checksum2C9775FE4B977D2A
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL035413 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC004111 EMBL· GenBank· DDBJ | AAH04111.3 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC007352 EMBL· GenBank· DDBJ | AAH07352.2 EMBL· GenBank· DDBJ | mRNA | ||
BC010852 EMBL· GenBank· DDBJ | AAH10852.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC011586 EMBL· GenBank· DDBJ | AAH11586.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC012171 EMBL· GenBank· DDBJ | AAH12171.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC013996 EMBL· GenBank· DDBJ | AAH13996.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AF026947 EMBL· GenBank· DDBJ | AAC52104.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
Y16675 EMBL· GenBank· DDBJ | CAA76347.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BT007347 EMBL· GenBank· DDBJ | AAP36011.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BK000395 EMBL· GenBank· DDBJ | DAA00088.1 EMBL· GenBank· DDBJ | mRNA |