Q28960
Gene name |
CBR1 |
Protein name |
Carbonyl reductase [NADPH] 1 |
Names |
15-hydroxyprostaglandin dehydrogenase [NADP(+)], 20-beta-hydroxysteroid dehydrogenase, Alcohol dehydrogenase [NAD(P)+] CBR1, NADPH-dependent carbonyl reductase 1, Prostaglandin 9-ketoreductase, PG-9-KR, Prostaglandin-E(2) 9-reductase |
Species |
Sus scrofa (Pig) |
KEGG Pathway |
ssc:397143 |
EC number |
1.1.1.71: 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
2 structures for Q28960
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1N5D | X-ray | 230 A | A | 2-289 | PDB |
| AF-Q28960-F1 | Predicted | AlphaFoldDB |
14 variants for Q28960
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3473621978 | 23 | R>W | No | EVA | |
| rs3472676782 | 71 | R>H | No | EVA | |
| rs789516822 | 98 | D>E | No | EVA | |
| rs1112960120 | 99 | N>D | No | EVA | |
| rs790472373 | 102 | P>L | No | EVA | |
| rs789242412 | 116 | M>L | No | EVA | |
| rs790054285 | 120 | N>D | No | EVA | |
| rs788102132 | 125 | L>F | No | EVA | |
| rs3475192036 | 199 | I>N | No | EVA | |
| rs3471022500 | 213 | R>S | No | EVA | |
| rs1109160061 | 246 | V>E | No | EVA | |
| rs1112430940 | 270 | T>S | No | EVA | |
| rs1113829832 | 274 | V>F | No | EVA | |
| rs3475529615 | 287 | V>A | No | EVA |
No associated diseases with Q28960
1 regional properties for Q28960
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Short-chain dehydrogenase/reductase, conserved site | 181 - 209 | IPR020904 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.1.1.71 | 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 |
|---|---|
| 15-hydroxyprostaglandin dehydrogenase (NADP+) activity | Catalysis of the reaction: NADP(+) + prostaglandin E(1) = 15-dehydro-prostaglandin E1 + H(+) + NADPH. |
| 15-hydroxyprostaglandin-D dehydrogenase (NADP+) activity | Catalysis of the reaction: NADP+ + (5Z,13E)-(15S)-9-alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate = NADPH + H+ + (5Z,13E)-9-alpha-hydroxy-11,15-dioxoprosta-5,13-dienoate. |
| alcohol dehydrogenase (NADP+) activity | Catalysis of the reaction: an alcohol + NADP+ = an aldehyde + NADPH + H+. |
| carbonyl reductase (NADPH) activity | Catalysis of the reaction: R-CHOH-R' + NADP+ = R-CO-R' + NADPH + H+. |
| oxidoreductase activity | Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. |
| prostaglandin-E2 9-reductase activity | Catalysis of the reaction: (5Z,13E)-(15S)-9-alpha,11-alpha,15-trihydroxyprosta-5,13-dienoate + NADP+ = (5Z,13E)-(15S)-11-alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate + NADPH. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| lipid metabolic process | The chemical reactions and pathways involving lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. Includes fatty acids; neutral fats, other fatty-acid esters, and soaps; long-chain (fatty) alcohols and waxes; sphingoids and other long-chain bases; glycolipids, phospholipids and sphingolipids; and carotenes, polyprenols, sterols, terpenes and other isoprenoids. |
| vitamin K metabolic process | The chemical reactions and pathways involving any of the forms of vitamin K, quinone-derived vitamins which are involved in the synthesis of blood-clotting factors in mammals. Vitamin K substances share a methylated naphthoquinone ring structure and vary in the aliphatic side chains attached to the molecule. |
| xenobiotic metabolic process | The chemical reactions and pathways involving a xenobiotic compound, a compound foreign to the organim exposed to it. It may be synthesized by another organism (like ampicilin) or it can be a synthetic chemical. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P16152 | CBR1 | Carbonyl reductase [NADPH] 1 | Homo sapiens (Human) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSSNTRVALV | TGANKGIGFA | IVRDLCRQFA | GDVVLTARDV | ARGQAAVKQL | QAEGLSPRFH |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QLDIIDLQSI | RALCDFLRKE | YGGLDVLVNN | AAIAFQLDNP | TPFHIQAELT | MKTNFMGTRN |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VCTELLPLIK | PQGRVVNVSS | TEGVRALNEC | SPELQQKFKS | ETITEEELVG | LMNKFVEDTK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| NGVHRKEGWS | DSTYGVTKIG | VSVLSRIYAR | KLREQRAGDK | ILLNACCPGW | VRTDMGGPKA |
| 250 | 260 | 270 | 280 | ||
| PKSPEVGAET | PVYLALLPSD | AEGPHGQFVT | DKKVVEWGVP | PESYPWVNA |