[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=CH3; DOI=10.1083/jcb.107.1.279; PubMed=2455724 [NCBI, ExPASy, EBI, Israel, Japan] Navre M., Ringold G.M.; "A growth factor-repressible gene associated with protein kinase C-mediated inhibition of adipocyte differentiation."; J. Cell Biol. 107:279-286(1988).
[2]	NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND FUNCTION. PubMed=7705352 [NCBI, ExPASy, EBI, Israel, Japan] Nakanishi M., Deyashiki Y., Ohshima K., Hara A.; "Cloning, expression and tissue distribution of mouse tetrameric carbonyl reductase. Identity with an adipocyte 27-kDa protein."; Eur. J. Biochem. 228:381-387(1995).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=FVB/N; TISSUE=Colon; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	SUBCELLULAR LOCATION. DOI=10.1007/BF00157764; PubMed=8040004 [NCBI, ExPASy, EBI, Israel, Japan] Matsuura K., Bunai Y., Ohya I., Hara A., Nakanishi M., Sawada H.; "Ultrastructural localization of carbonyl reductase in mouse lung."; Histochem. J. 26:311-316(1994).
[5]	MUTAGENESIS OF THR-38, AND COENZYME SPECIFICITY. DOI=10.1074/jbc.272.4.2218; PubMed=8999926 [NCBI, ExPASy, EBI, Israel, Japan] Nakanishi M., Matsuura K., Kaibe H., Tanaka N., Nonaka T., Mitsui Y., Hara A.; "Switch of coenzyme specificity of mouse lung carbonyl reductase by substitution of threonine 38 with aspartic acid."; J. Biol. Chem. 272:2218-2222(1997).
[6]	X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH NADPH. DOI=10.1016/S0969-2126(96)00007-X; PubMed=8805511 [NCBI, ExPASy, EBI, Israel, Japan] Tanaka N., Nonaka T., Nakanishi M., Deyashiki Y., Hara A., Mitsui Y.; "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."; Structure 4:33-45(1996).

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.
CATALYTIC ACTIVITY: R-CHOH-R' + NADP⁺ = R-CO-R' + NADPH.
SUBUNIT: Homotetramer.
SUBCELLULAR LOCATION: Mitochondrion matrix.
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.
SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D26123; BAA05120.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X07411; CAA30309.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC010758; AAH10758.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S03382; A28053.

NP_031647.1; -.

3D structure databases

PDB

1CYD; X-ray; 1.80 A; A/B/C/D=1-244.

[ExPASy / RCSB / EBI]

PDBsum

1CYD; -.

ModBase

P08074.

Organism-specific databases

MGI

MGI:107200; Cbr2.

Gene expression databases

ArrayExpress

P08074; -.

CleanEx

MM_CBR2; -.

GermOnline

ENSMUSG00000025150; Mus musculus.

Ontologies

GO:0005739;	Cellular component: mitochondrion (inferred from direct assay from MGI).
GO:0004090;	Molecular function: carbonyl reductase (NADPH) activity (traceable author statement from MGI).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from MGI).
GO:0006116;	Biological process: NADH oxidation (traceable author statement from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR002198; DHase_sc/Rdtase_SDR.
IPR002347; Glc/ribitol_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

PANTHER

PTHR19410; ADH_short_C2; 1.

Pfam

PF00106; adh_short; 1.
Pfam graphical view of domain structure.

PRINTS

PR00081; GDHRDH.
PR00080; SDRFAMILY.

PROSITE

PS00061; ADH_SHORT; 1.

Genome annotation databases

Ensembl

ENSMUSG00000025150; Mus musculus. [Contig view]

GeneID

12409; -.

KEGG

mmu:12409; -.

Phylogenomic databases

HOGENOM

P08074; -.

HOVERGEN

P08074; -.

Other

P08074; -.

281190; -.

Cbr2; Mus musculus.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Direct protein sequencing; Mitochondrion; NAD; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 244`	`244`	`Carbonyl reductase [NADPH] 2.`	`PRO_0000054547`
`NP_BIND`	`11 39`	`29`	`NADP.`
`ACT_SITE`	`149 149`		`Proton acceptor.`
`BINDING`	`136 136`		`Substrate.`
`MUTAGEN`	`38 38`		`T->R: Converts the coenzyme specificity from NADP to NAD.`
`STRAND`	`9 14`	`6`
`HELIX`	`18 29`	`12`
`STRAND`	`33 39`	`7`
`HELIX`	`41 50`	`10`
`STRAND`	`55 58`	`4`
`HELIX`	`64 71`	`8`
`STRAND`	`78 82`	`5`
`HELIX`	`92 94`	`3`
`HELIX`	`97 107`	`11`
`HELIX`	`109 125`	`17`
`STRAND`	`129 134`	`6`
`HELIX`	`137 139`	`3`
`HELIX`	`147 167`	`21`
`HELIX`	`168 170`	`3`
`STRAND`	`172 179`	`8`
`HELIX`	`185 190`	`6`
`HELIX`	`194 203`	`10`
`HELIX`	`212 223`	`12`
`HELIX`	`225 227`	`3`
`STRAND`	`232 238`	`7`
`HELIX`	`241 243`	`3`

Sequence information

Length: 244 AA [This is the length of the unprocessed precursor]

Molecular weight: 25958 Da [This is the MW of the unprocessed precursor]

CRC64: 4FA14C5722DD231E [This is a checksum on the sequence]

        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

P08074 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools