Q3SZD7 (CBR1_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 55.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Carbonyl reductase [NADPH] 1 EC=1.1.1.184 | ||
| Gene names |
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| Organism | Bos taurus (Bovine) [Reference proteome] | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos![]() |
Protein attributes
| Sequence length | 277 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 | NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol. Can convert prostaglandin E2 to prostaglandin F2-alpha. Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione By similarity. |
| Catalytic activity | R-CHOH-R' + NADP+ = R-CO-R' + NADPH. (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. (13E)-(15S)-11-alpha,15-dihydroxy-9-oxoprost-13-enoate + NADP+ = (13E)-11-alpha-hydroxy-9,15-dioxoprost-13-enoate + NADPH. |
| Subunit structure | Monomer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the short-chain dehydrogenases/reductases (SDR) family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | NADP |
| Molecular function | Oxidoreductase |
| PTM | Acetylation |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | drug metabolic process Inferred from sequence or structural similarity. Source: UniProtKB vitamin K metabolic processInferred from sequence or structural similarity. Source: UniProtKB |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | 15-hydroxyprostaglandin dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: EC carbonyl reductase (NADPH) activityInferred from sequence or structural similarity. Source: UniProtKB nucleotide bindingInferred from electronic annotation. Source: InterPro prostaglandin-E2 9-reductase activityInferred 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 – 277 | 276 | Carbonyl reductase [NADPH] 1 | PRO_0000284143 | |||||
Regions | |||||||||
| Nucleotide binding | 10 – 34 | 25 | NADP By similarity | ||||||
| Nucleotide binding | 63 – 64 | 2 | NADP By similarity | ||||||
| Nucleotide binding | 194 – 198 | 5 | NADP By similarity | ||||||
| Nucleotide binding | 231 – 233 | 3 | NADP By similarity | ||||||
| Region | 95 – 97 | 3 | Glutathione binding By similarity | ||||||
| Region | 193 – 194 | 2 | Glutathione binding By similarity | ||||||
Sites | |||||||||
| Active site | 194 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 90 | 1 | NADP; via carbonyl oxygen By similarity | ||||||
| Binding site | 106 | 1 | Glutathione By similarity | ||||||
| Binding site | 140 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylserine By similarity | ||||||
| Modified residue | 239 | 1 | N6-1-carboxyethyl lysine By similarity | ||||||
Sequences
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References
| [1] | NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus. Tissue: Ileum. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BC102943 mRNA. Translation: AAI02944.1. |
| IPI | IPI00708761. |
| RefSeq | NP_001029685.1. NM_001034513.1. |
| UniGene | Bt.7872. |
3D structure databases | |
| ProteinModelPortal | Q3SZD7. |
| SMR | Q3SZD7. Positions 7-277. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 9913.ENSBTAP00000019311. |
Proteomic databases | |
| PaxDb | Q3SZD7. |
| PRIDE | Q3SZD7. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 515946. |
| KEGG | bta:515946. |
Organism-specific databases | |
| CTD | 873. |
Phylogenomic databases | |
| eggNOG | COG1028. |
| HOVERGEN | HBG001909. |
| KO | K00079. |
| OrthoDB | EOG4BP1CB. |
Family and domain databases | |
| Gene3D | 3.40.50.720. 1 hit. |
| InterPro | IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. IPR020904. Sc_DH/Rdtase_CS. [Graphical view] |
| Pfam | PF00106. adh_short. 1 hit. [Graphical view] |
| PRINTS | PR00081. GDHRDH. PR00080. SDRFAMILY. |
| PROSITE | PS00061. ADH_SHORT. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 20872066. |
Entry information
| Entry name | CBR1_BOVIN | ||||||||
| Accession | Primary (citable) accession number: Q3SZD7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
