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Reviewed, UniProtKB/Swiss-Prot P08074 (CBR2_MOUSE)

Last modified June 16, 2009. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

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Names and origin

Protein namesRecommended name:
    Carbonyl reductase [NADPH] 2
    EC=1.1.1.184
Alternative name(s):
    NADPH-dependent carbonyl reductase 2
    Lung carbonyl reductase
      Short name=LCR
    Adipocyte protein P27
      Short name=AP27
Gene names
Name: Cbr2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length244 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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

Mitochondrion matrix. Ref.4

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.

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Ontologies

Keywords
   Cellular componentMitochondrion
   LigandNAD
NADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processNADH oxidation Ref.6

Traceable author statement. Source: MGI

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

protein tetramerization Ref.2

Inferred from direct assay. Source: MGI

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncarbonyl reductase (NADPH) activity Ref.2 Ref.6

Inferred from direct assay. Source: MGI

protein self-association Ref.2

Inferred from direct assay. Source: MGI

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 244244Carbonyl reductase [NADPH] 2
PRO_0000054547

Regions

Nucleotide binding11 – 3929NADP

Sites

Active site1491Proton acceptor
Binding site1361Substrate

Experimental info

Mutagenesis381T → R: Converts the coenzyme specificity from NADP to NAD. Ref.5

Secondary structure

1 .......................................... 244
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P08074-1 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 4FA14C5722DD231E

FASTA24425,958
        10         20         30         40         50         60 
MKLNFSGLRA LVTGAGKGIG RDTVKALHAS GAKVVAVTRT NSDLVSLAKE CPGIEPVCVD 

        70         80         90        100        110        120 
LGDWDATEKA LGGIGPVDLL VNNAALVIMQ PFLEVTKEAF DRSFSVNLRS VFQVSQMVAR 

       130        140        150        160        170        180 
DMINRGVPGS IVNVSSMVAH VTFPNLITYS STKGAMTMLT KAMAMELGPH KIRVNSVNPT 

       190        200        210        220        230        240 
VVLTDMGKKV SADPEFARKL KERHPLRKFA EVEDVVNSIL FLLSDRSAST SGGGILVDAG 


YLAS

« Hide

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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.

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Cross-references

Sequence databases

D26123 mRNA. Translation: BAA05120.1.
X07411 mRNA. Translation: CAA30309.1.
BC010758 mRNA. Translation: AAH10758.1.
IPIIPI00128642.
PIRA28053. S03382.
RefSeqNP_031647.1.
UniGeneMm.21454

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1CYDX-ray1.80A/B/C/D1-244[»]
ModBaseSearch...

Proteomic databases

PRIDEP08074.

Genome annotation databases

EnsemblENSMUSG00000025150. Mus musculus. [Contig view]
GeneID12409.
KEGGmmu:12409.

Organism-specific databases

MGIMGI:107200. Cbr2.

Phylogenomic databases

HOGENOMP08074.
HOVERGENP08074.
OMAP08074. KGAMTML.

Enzyme and pathway databases

BRENDA1.1.1.184. 244.

Gene expression databases

ArrayExpressP08074.
BgeeP08074.
CleanExMM_CBR2.
GermOnlineENSMUSG00000025150. Mus musculus.

Family and domain databases

InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR19410. ADH_short_C2. 1 hit.
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio281190.
SOURCESearch...

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Entry information

Entry nameCBR2_MOUSE
AccessionPrimary (citable) accession number: P08074
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: June 16, 2009
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents