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RAT:ADH1
Contents
| Species (Taxon ID) | Rattus norvegicus (Rat). (10116) | |
| Gene Name(s) | Adh1 (synonyms: Adh-1) | |
| Protein Name(s) | Alcohol dehydrogenase 1
Alcohol dehydrogenase A subunit | |
| External Links | ||
| UniProt | P06757 | |
| EMBL | M29523 M29516 M29517 M29518 M29519 M29520 M29521 M29522 M15327 BC062403 | |
| PIR | A26468 | |
| RefSeq | NP_062159.3 | |
| UniGene | Rn.40222 | |
| ProteinModelPortal | P06757 | |
| SMR | P06757 | |
| MINT | MINT-4575526 | |
| STRING | 10116.ENSRNOP00000016346 | |
| ChEMBL | CHEMBL4862 | |
| PaxDb | P06757 | |
| PRIDE | P06757 | |
| GeneID | 24172 | |
| KEGG | rno:24172 | |
| CTD | 11522 | |
| RGD | 2044 | |
| eggNOG | COG1062 | |
| HOGENOM | HOG000294674 | |
| HOVERGEN | HBG000195 | |
| InParanoid | P06757 | |
| KO | K13951 | |
| PhylomeDB | P06757 | |
| SABIO-RK | P06757 | |
| NextBio | 602493 | |
| Proteomes | UP000002494 | |
| Genevestigator | P06757 | |
| GO | GO:0005829 GO:0004022 GO:0008144 GO:0035276 GO:0051287 GO:0004745 GO:0008270 GO:0046186 GO:0006069 GO:0031100 GO:0032570 | |
| Gene3D | 3.40.50.720 3.90.180.10 | |
| InterPro | IPR013149 IPR013154 IPR002085 IPR002328 IPR011032 IPR016040 | |
| PANTHER | PTHR11695 | |
| Pfam | PF08240 PF00107 | |
| SUPFAM | SSF50129 | |
| PROSITE | PS00059 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
|
enables |
GO:0051287 |
NAD binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0051287 |
NAD binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0046186 |
acetaldehyde biosynthetic process |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0035276 |
ethanol binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0035276 |
ethanol binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0032570 |
response to progesterone |
ECO:0000270 |
expression pattern evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0031100 |
animal organ regeneration |
ECO:0000270 |
expression pattern evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008144 |
drug binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
PubChem_Compound:7469 |
F |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0006069 |
ethanol oxidation |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006069 |
ethanol oxidation |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005829 |
cytosol |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004745 |
retinol dehydrogenase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004022 |
alcohol dehydrogenase (NAD) activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004022 |
alcohol dehydrogenase (NAD) activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0042573 |
retinoic acid metabolic process |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
MGI:MGI:87921 |
P |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0042572 |
retinol metabolic process |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
MGI:MGI:87921 |
P |
Seeded From UniProt |
complete | ||
|
enables |
GO:0008270 |
zinc ion binding |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG50010 |
F |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0006069 |
ethanol oxidation |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000191662 |
P |
Seeded From UniProt |
complete | ||
|
part_of |
GO:0005829 |
cytosol |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG50010 |
C |
Seeded From UniProt |
complete | ||
|
enables |
GO:0004745 |
retinol dehydrogenase activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
MGI:MGI:87926 |
F |
Seeded From UniProt |
complete | ||
|
enables |
GO:0004024 |
alcohol dehydrogenase activity, zinc-dependent |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG50010 |
F |
Seeded From UniProt |
complete | ||
|
enables |
GO:0008270 |
zinc ion binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004022 |
alcohol dehydrogenase (NAD) activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004022 |
alcohol dehydrogenase (NAD) activity |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005737 |
cytoplasm |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0046872 |
metal ion binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 1.2 1.3 Chen, L et al. (1992) Distribution of alcohol dehydrogenase and the low Km form of aldehyde dehydrogenase in isolated perivenous and periportal hepatocytes in rats. Alcohol. Clin. Exp. Res. 16 23-9 PubMed GONUTS page
- ↑ 2.0 2.1 2.2 2.3 2.4 Galli, A et al. (1999) High-level expression of rat class I alcohol dehydrogenase is sufficient for ethanol-induced fat accumulation in transduced HeLa cells. Hepatology 29 1164-70 PubMed GONUTS page
- ↑ Ohno, T et al. (2008) Evidence for the expression of alcohol dehydrogenase class I gene in rat uterus and its up-regulation by progesterone. Endocr. J. 55 83-90 PubMed GONUTS page
- ↑ López-Valencia, V et al. (2007) Involvement of alcohol and aldehyde dehydrogenase activities on hepatic retinoid metabolism and its possible participation in the progression of rat liver regeneration. Biochem. Pharmacol. 73 586-96 PubMed GONUTS page
- ↑ 5.0 5.1 Negoro, M & Wakabayashi, I (2005) Interactions of alcohol dehydrogenase to p-hydroxyacetophenone-sepharose and p-acetamidophenol-sepharose. Alcohol. Clin. Exp. Res. 29 304S-8S PubMed GONUTS page
- ↑ Julià, P et al. (1986) Ocular alcohol dehydrogenase in the rat: regional distribution and kinetics of the ADH-1 isoenzyme with retinol and retinal. Exp. Eye Res. 42 305-14 PubMed GONUTS page
- ↑ 7.0 7.1 7.2 7.3 7.4 7.5 7.6 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
- ↑ Galter, D et al. (2003) Distribution of class I, III and IV alcohol dehydrogenase mRNAs in the adult rat, mouse and human brain. Eur. J. Biochem. 270 1316-26 PubMed GONUTS page
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