Reviewed,
UniProtKB/Swiss-Prot P06757 (ADH1_RAT)
Last modified
June 16, 2009.
Version 85.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Alcohol dehydrogenase 1 EC=1.1.1.1 Alternative name(s): Alcohol dehydrogenase A subunit | ||||
| Gene names |
| ||||
| Organism | Rattus norvegicus (Rat) | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 376 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | An alcohol + NAD+ = an aldehyde or ketone + NADH. |
| Cofactor | Binds 2 zinc ions per subunit. |
| Subunit structure | Dimer of identical or non-identical chains of three types (A, B, C), which are coded by 3 separate genes at different loci. |
| Subcellular location | |
| Sequence similarities | Belongs to the zinc-containing alcohol dehydrogenase family. Class-I subfamily. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Metal-binding NAD Zinc |
| Molecular function | Oxidoreductase |
| PTM | Acetylation |
| Gene Ontology (GO) | |
| Biological process | acetaldehyde biosynthetic process Inferred from direct assay. Source: RGD ethanol oxidationInferred from direct assay. Source: RGD oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytosol Inferred from direct assay. Source: RGD soluble fractionInferred from direct assay. Source: RGD |
| Molecular function | NAD or NADH binding Inferred from direct assay. Source: RGD alcohol dehydrogenase activityInferred from direct assay. Source: RGD drug bindingInferred from physical interaction. Source: RGD ethanol bindingInferred from direct assay. Source: RGD zinc ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed | ||||||
| Chain | 2 – 376 | 375 | Alcohol dehydrogenase 1 | PRO_0000160669 | |||||
Regions | |||||||||
| Nucleotide binding | 201 – 206 | 6 | NAD By similarity | ||||||
| Nucleotide binding | 294 – 296 | 3 | NAD By similarity | ||||||
Sites | |||||||||
| Metal binding | 47 | 1 | Zinc 1; catalytic | ||||||
| Metal binding | 68 | 1 | Zinc 1; catalytic | ||||||
| Metal binding | 98 | 1 | Zinc 2 | ||||||
| Metal binding | 101 | 1 | Zinc 2 | ||||||
| Metal binding | 104 | 1 | Zinc 2 | ||||||
| Metal binding | 112 | 1 | Zinc 2 | ||||||
| Metal binding | 176 | 1 | Zinc 1; catalytic | ||||||
| Binding site | 225 | 1 | NAD By similarity | ||||||
| Binding site | 230 | 1 | NAD By similarity | ||||||
| Binding site | 371 | 1 | NAD By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylserine Ref.4 | ||||||
Experimental info | |||||||||
| Sequence conflict | 143 | 1 | I → L in AAA40681. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Complete amino acid sequence of rat liver alcohol dehydrogenase deduced from the cDNA sequence." Crabb D.W., Edenberg H.J. Gene 48:287-291(1986) [PubMed: 2881847] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver. |
| [2] | "Structure and expression of the rat class I alcohol dehydrogenase gene." Crabb D.W., Stein P.M., Dipple K.M., Hittle J.B., Sidhu R., Qulali M., Zhang K., Edenberg H.J. Genomics 5:906-914(1989) [PubMed: 2591969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. |
| [3] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Prostate. |
| [4] | "Structural studies of alcohol dehydrogenase from rat liver." Joernvall H., Markovic O. Eur. J. Biochem. 29:167-174(1972) [PubMed: 4673366] [Abstract] Cited for: ACETYLATION AT SER-2. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
M29523 M29522 Genomic DNA. Translation: AAA85462.1. M15327 mRNA. Translation: AAA40681.1. BC062403 mRNA. Translation: AAH62403.1. | |
| IPI | IPI00331983. |
| PIR | A26468. |
| RefSeq | NP_062159.3. |
| UniGene | Rn.40222 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1HT0 based on UniProtKB P00326. |
| SMR | P06757. Positions 2-376. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P06757. |
Genome annotation databases | |
| Ensembl | ENSRNOG00000012464. Rattus norvegicus. [Contig view] |
| GeneID | 24172. |
| KEGG | rno:24172. |
Organism-specific databases | |
| RGD | 2044. Adh1. |
Phylogenomic databases | |
| HOVERGEN | P06757. |
Enzyme and pathway databases | |
| BRENDA | 1.1.1.1. 248. |
Gene expression databases | |
| ArrayExpress | P06757. |
| GermOnline | ENSRNOG00000012464. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR013154. ADH_GroES-like. IPR002085. ADH_SF_Zn. IPR013149. ADH_Zn-bd. IPR002328. ADH_Zn_CS. [Graphical view] |
| PANTHER | PTHR11695. ADH_Sf_Zn. 1 hit. |
| Pfam | PF08240. ADH_N. 1 hit. PF00107. ADH_zinc_N. 1 hit. [Graphical view] |
| PROSITE | PS00059. ADH_ZINC. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 602493. |
Entry information
| Entry name | ADH1_RAT | ||||||||
| Accession | Primary (citable) accession number: P06757 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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