P15122
Gene name |
AKR1B1 |
Protein name |
Aldo-keto reductase family 1 member B1 |
Names |
Aldehyde reductase, Aldose reductase, AR |
Species |
Oryctolagus cuniculus (Rabbit) |
KEGG Pathway |
ocu:100009122 |
EC number |
1.1.1.300: With NAD(+) or NADP(+) as acceptor |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for P15122
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P15122-F1 | Predicted | AlphaFoldDB |
No variants for P15122
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P15122 | |||||
No associated diseases with P15122
4 regional properties for P15122
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Aldo/keto reductase, conserved site | 39 - 56 | IPR018170-1 |
| conserved_site | Aldo/keto reductase, conserved site | 145 - 162 | IPR018170-2 |
| conserved_site | Aldo/keto reductase, conserved site | 261 - 276 | IPR018170-3 |
| domain | NADP-dependent oxidoreductase domain | 16 - 289 | IPR023210 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.1.1.300 | With NAD(+) or NADP(+) as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| alditol:NADP+ 1-oxidoreductase activity | Catalysis of the reaction: an alditol + NADP+ = an aldose + NADPH + H+. |
| allyl-alcohol dehydrogenase activity | Catalysis of the reaction: allyl alcohol + NADP(+) = acrolein + H(+) + NADPH. |
| glycerol dehydrogenase [NADP+] activity | Catalysis of the reaction: glycerol + NADP+ = D-glyceraldehyde + NADPH. |
| NADP-retinol dehydrogenase activity | Catalysis of the reaction: all-trans-retinol + NADP+ = all-trans-retinal + NADPH + H+. |
| prostaglandin H2 endoperoxidase reductase activity | Catalysis of the reaction: prostaglandin H2 + NADPH + H+ -> prostaglandin F2alpha + NADP+. This reaction is the reduction of prostaglandin H2 ((5Z,13E)-(15S)-9alpha,11alpha-Epidioxy-15-hydroxyprosta-5,13-dienoate) to prostaglandin F2alpha ((5Z,13E)-(15S)-9alpha,11alpha,15-Trihydroxyprosta-5,13-dienoate). |
| retinal dehydrogenase activity | Catalysis of the reaction: retinal + NAD+ + H2O = retinoate + NADH. Acts on both 11-trans and 13-cis forms of retinal. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| retinoid metabolic process | The chemical reactions and pathways involving retinoids, any member of a class of isoprenoids that contain or are derived from four prenyl groups linked head-to-tail. Retinoids include retinol and retinal and structurally similar natural derivatives or synthetic compounds, but need not have vitamin A activity. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MATHLVLYNG | AKMPILGLGT | WKSPPGQVTE | AVKTAIDLGY | RHIDCAHVYQ | NENEVGVALQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EKLKEQVVKR | EELFIVSKLW | CTSHDKSLVK | GACQKTLNDL | KLDYLDLYLI | HWPTGFKHGS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EYFPLDAAGN | VIPSDTDFLD | TWEAMEGLVD | EGLVKSIGVS | NFNHLQIERI | LNKPGLKYKP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AVNQIECHPY | LTQEKLIQYC | HSKGIVVTAY | SPLGSPDRPW | AKPEDPSLLE | DPRIKAIADK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| HKKTTAQVLI | RFPMQRNLVV | IPKSVTPARI | AENFQVFDFE | LSSEDMTTLL | SYNRNWRVCA |
| 310 | |||||
| LVSCASHKDY | PFHAEF |