P08074 (CBR2_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 110.
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] 2 EC=1.1.1.184 Alternative name(s): Adipocyte protein P27 Short name=AP27 Lung carbonyl reductase Short name=LCR NADPH-dependent carbonyl reductase 2 | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus |
Protein attributes
| Sequence length | 244 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | May function in the pulmonary metabolism of endogenous carbonyl compounds, such as aliphatic aldehydes and ketones derived from lipid peroxidation, 3-ketosteroids and fatty aldehydes, as well as in xenobiotic metabolism. Ref.2 |
| Catalytic activity | R-CHOH-R' + NADP+ = R-CO-R' + NADPH. |
| Subunit structure | Homotetramer. |
| Subcellular location | |
| Tissue specificity | Lung (ciliated cells, non-ciliated bronchiolar cells and type-II alveolar pneumocytes). Low expression in adipose tissue > testis = heart > kidney = spleen > brain = liver. |
| Induction | By glucocorticoids. Activated by fatty acids. |
| Miscellaneous | Uses both NADP and NAD as substrates. Has a strong preference for NADP. |
| Sequence similarities | Belongs to the short-chain dehydrogenases/reductases (SDR) family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Ligand | NAD NADP |
| Molecular function | Oxidoreductase |
| Technical term | 3D-structure Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological process | NADH oxidation Traceable author statement Ref.6. Source: MGI protein tetramerizationInferred from direct assay Ref.2. Source: MGI |
| Cellular component | mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | carbonyl reductase (NADPH) activity Inferred from direct assay Ref.2. Source: MGI nucleotide bindingInferred from electronic annotation. Source: InterPro protein self-associationInferred from direct assay Ref.2. Source: MGI |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 244 | 244 | Carbonyl reductase [NADPH] 2 | PRO_0000054547 | ||||||||||||||||||||||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Nucleotide binding | 11 – 39 | 29 | NADP | |||||||||||||||||||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Active site | 149 | 1 | Proton acceptor | |||||||||||||||||||||||||||||||||||||||||||||||
| Binding site | 136 | 1 | Substrate | |||||||||||||||||||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 38 | 1 | T → R: Converts the coenzyme specificity from NADP to NAD. Ref.5 | |||||||||||||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 9 – 14 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 18 – 29 | 12 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 33 – 39 | 7 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 41 – 50 | 10 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 55 – 58 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 64 – 71 | 8 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 78 – 82 | 5 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 92 – 94 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 97 – 107 | 11 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 109 – 125 | 17 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 129 – 134 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 137 – 139 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 147 – 167 | 21 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 168 – 170 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 172 – 179 | 8 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 185 – 190 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 194 – 203 | 10 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 212 – 223 | 12 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 225 – 227 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 232 – 238 | 7 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 241 – 243 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "A growth factor-repressible gene associated with protein kinase C-mediated inhibition of adipocyte differentiation." Navre M., Ringold G.M. J. Cell Biol. 107:279-286(1988) [PubMed: 2455724] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: CH3. |
| [2] | "Cloning, expression and tissue distribution of mouse tetrameric carbonyl reductase. Identity with an adipocyte 27-kDa protein." Nakanishi M., Deyashiki Y., Ohshima K., Hara A. Eur. J. Biochem. 228:381-387(1995) [PubMed: 7705352] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION. |
| [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]. Strain: FVB/N. Tissue: Colon. |
| [4] | "Ultrastructural localization of carbonyl reductase in mouse lung." Matsuura K., Bunai Y., Ohya I., Hara A., Nakanishi M., Sawada H. Histochem. J. 26:311-316(1994) [PubMed: 8040004] [Abstract] Cited for: SUBCELLULAR LOCATION. |
| [5] | "Switch of coenzyme specificity of mouse lung carbonyl reductase by substitution of threonine 38 with aspartic acid." Nakanishi M., Matsuura K., Kaibe H., Tanaka N., Nonaka T., Mitsui Y., Hara A. J. Biol. Chem. 272:2218-2222(1997) [PubMed: 8999926] [Abstract] Cited for: MUTAGENESIS OF THR-38, COENZYME SPECIFICITY. |
| [6] | "Crystal structure of the ternary complex of mouse lung carbonyl reductase at 1.8-A resolution: the structural origin of coenzyme specificity in the short-chain dehydrogenase/reductase family." Tanaka N., Nonaka T., Nakanishi M., Deyashiki Y., Hara A., Mitsui Y. Structure 4:33-45(1996) [PubMed: 8805511] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH NADPH. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | D26123 mRNA. Translation: BAA05120.1. X07411 mRNA. Translation: CAA30309.1. BC010758 mRNA. Translation: AAH10758.1. | ||||||||||||
| IPI | IPI00128642. | ||||||||||||
| PIR | A28053. S03382. | ||||||||||||
| RefSeq | NP_031647.1. NM_007621.2. | ||||||||||||
| UniGene | Mm.21454. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P08074. | ||||||||||||
| SMR | P08074. Positions 3-244. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| STRING | P08074. | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | P08074. | ||||||||||||
Proteomic databases | |||||||||||||
| PRIDE | P08074. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENSMUST00000026148; ENSMUSP00000026148; ENSMUSG00000025150. | ||||||||||||
| GeneID | 12409. | ||||||||||||
| KEGG | mmu:12409. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 12409. | ||||||||||||
| MGI | MGI:107200. Cbr2. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | roNOG13281. | ||||||||||||
| HOGENOM | HBG750976. | ||||||||||||
| HOVERGEN | HBG105069. | ||||||||||||
| InParanoid | P08074. | ||||||||||||
| OMA | RSVFQVS. | ||||||||||||
| OrthoDB | EOG4PK28V. | ||||||||||||
| PhylomeDB | P08074. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | P08074. | ||||||||||||
| Bgee | P08074. | ||||||||||||
| CleanEx | MM_CBR2. | ||||||||||||
| Genevestigator | P08074. | ||||||||||||
| GermOnline | ENSMUSG00000025150. Mus musculus. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. IPR020904. Sc_DH/Rdtase_CS. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. | ||||||||||||
| KO | K00081. | ||||||||||||
| 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 | 281190. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | CBR2_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P08074 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with