Reviewed,
UniProtKB/Swiss-Prot P15122 (ALDR_RABIT)
Last modified
June 16, 2009.
Version 64.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Aldose reductase Short name=AR EC=1.1.1.21 Alternative name(s): Aldehyde reductase | ||
| Gene names |
| ||
| Organism | Oryctolagus cuniculus (Rabbit) | ||
| Taxonomic identifier | 9986 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus |
Protein attributes
| Sequence length | 316 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. |
| Catalytic activity | Alditol + NAD(P)+ = aldose + NAD(P)H. |
| Subunit structure | Monomer. |
| Subcellular location | |
| Sequence similarities | Belongs to the aldo/keto reductase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | NADP |
| Molecular function | Oxidoreductase |
| PTM | Acetylation Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | aldehyde reductase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 316 | 315 | Aldose reductase | PRO_0000124626 | |||||
Regions | |||||||||
| Nucleotide binding | 10 – 19 | 10 | NADP Potential | ||||||
| Nucleotide binding | 211 – 273 | 63 | NADP By similarity | ||||||
Sites | |||||||||
| Active site | 49 | 1 | Proton donor By similarity | ||||||
| Binding site | 111 | 1 | Substrate By similarity | ||||||
| Site | 78 | 1 | Lowers pKa of active site Tyr By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylalanine By similarity | ||||||
| Modified residue | 23 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 40 | 1 | Phosphotyrosine By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Cloning, genomic organization, and osmotic response of the aldose reductase gene." Ferraris J.D., Williams C.K., Martin B.M., Burg M.B., Garcia-Perez A. Proc. Natl. Acad. Sci. U.S.A. 91:10742-10746(1994) [PubMed: 7938022] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Tissue: Spleen. |
| [2] | "Molecular cloning of cDNA coding for kidney aldose reductase. Regulation of specific mRNA accumulation by NaCl-mediated osmotic stress." Garcia-Perez A., Martin B., Murphy H.R., Uchida S., Murer H., Cowley B.D. Jr., Handler J.S., Burg M.B. J. Biol. Chem. 264:16815-16821(1989) [PubMed: 2506183] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 15-316. Tissue: Kidney. |
Cross-references
Sequence databases | |
|---|---|
U13694 U13693 Genomic DNA. Translation: AAB60687.1. M32818 mRNA. Translation: AAA31160.1. U12316 mRNA. Translation: AAA50833.1. J05048 mRNA. Translation: AAA31157.1. | |
| PIR | A34406. |
| RefSeq | NP_001075756.1. |
| UniGene | Ocu.1743 |
3D structure databases | |
| HSSP | HSSP built from PDB template 2ACQ based on UniProtKB P15121. |
| SMR | P15122. Positions 1-316. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 100009122. |
Phylogenomic databases | |
| HOVERGEN | P15122. |
Enzyme and pathway databases | |
| BRENDA | 1.1.1.21. 255. |
Family and domain databases | |
| InterPro | IPR001395. Aldo/ket_red. IPR018170. Aldo/ket_reductase_CS. [Graphical view] |
| Gene3D | G3DSA:3.20.20.100. Aldo/ket_red. 1 hit. |
| PANTHER | PTHR11732. Aldo/ket_red. 1 hit. |
| Pfam | PF00248. Aldo_ket_red. 1 hit. [Graphical view] |
| ProDom | PD000288. Aldo/ket_red. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| PROSITE | PS00798. ALDOKETO_REDUCTASE_1. 1 hit. PS00062. ALDOKETO_REDUCTASE_2. 1 hit. PS00063. ALDOKETO_REDUCTASE_3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ALDR_RABIT | ||||||||
| Accession | Primary (citable) accession number: P15122 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


