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Protein

Carbonyl reductase [NADPH] 2

Gene

Cbr2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

R-CHOH-R' + NADP+ = R-CO-R' + NADPH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei136 – 1361Substrate
Active sitei149 – 1491Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 3929NADP1 PublicationAdd
BLAST

GO - Molecular functioni

  • carbonyl reductase (NADPH) activity Source: MGI
  • protein self-association Source: MGI

GO - Biological processi

  • NADH oxidation Source: MGI
  • protein tetramerization Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

SABIO-RKP08074.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Cbr2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:107200. Cbr2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi38 – 381T → R: Converts the coenzyme specificity from NADP to NAD. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 244244Carbonyl reductase [NADPH] 2PRO_0000054547Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421PhosphoserineCombined sources
Modified residuei176 – 1761PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP08074.
PaxDbiP08074.
PeptideAtlasiP08074.
PRIDEiP08074.

PTM databases

iPTMnetiP08074.
PhosphoSiteiP08074.

Expressioni

Tissue specificityi

Lung (ciliated cells, non-ciliated bronchiolar cells and type-II alveolar pneumocytes). Low expression in adipose tissue > testis = heart > kidney = spleen > brain = liver.

Inductioni

By glucocorticoids. Activated by fatty acids.

Gene expression databases

BgeeiP08074.
CleanExiMM_CBR2.
ExpressionAtlasiP08074. baseline and differential.
GenevisibleiP08074. MM.

Interactioni

Subunit structurei

Homotetramer.1 Publication

GO - Molecular functioni

  • protein self-association Source: MGI

Protein-protein interaction databases

IntActiP08074. 1 interaction.
MINTiMINT-4090057.
STRINGi10090.ENSMUSP00000026148.

Structurei

Secondary structure

1
244
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 146Combined sources
Helixi18 – 2912Combined sources
Beta strandi33 – 397Combined sources
Helixi41 – 5010Combined sources
Beta strandi55 – 584Combined sources
Helixi64 – 718Combined sources
Beta strandi78 – 825Combined sources
Helixi92 – 943Combined sources
Helixi97 – 10711Combined sources
Helixi109 – 12517Combined sources
Beta strandi129 – 1346Combined sources
Helixi137 – 1393Combined sources
Helixi147 – 16721Combined sources
Helixi168 – 1703Combined sources
Beta strandi172 – 1798Combined sources
Helixi185 – 1906Combined sources
Helixi194 – 20310Combined sources
Helixi212 – 22312Combined sources
Helixi225 – 2273Combined sources
Beta strandi232 – 2387Combined sources
Helixi241 – 2433Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CYDX-ray1.80A/B/C/D1-244[»]
ProteinModelPortaliP08074.
SMRiP08074. Positions 3-244.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08074.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1207. Eukaryota.
ENOG410XQCY. LUCA.
HOVERGENiHBG105069.
InParanoidiP08074.
KOiK00081.
OMAiKGAMTML.
OrthoDBiEOG74TX0K.
PhylomeDBiP08074.
TreeFamiTF313841.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P08074-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLNFSGLRA LVTGAGKGIG RDTVKALHAS GAKVVAVTRT NSDLVSLAKE
60 70 80 90 100
CPGIEPVCVD LGDWDATEKA LGGIGPVDLL VNNAALVIMQ PFLEVTKEAF
110 120 130 140 150
DRSFSVNLRS VFQVSQMVAR DMINRGVPGS IVNVSSMVAH VTFPNLITYS
160 170 180 190 200
STKGAMTMLT KAMAMELGPH KIRVNSVNPT VVLTDMGKKV SADPEFARKL
210 220 230 240
KERHPLRKFA EVEDVVNSIL FLLSDRSAST SGGGILVDAG YLAS
Length:244
Mass (Da):25,958
Last modified:August 1, 1988 - v1
Checksum:i4FA14C5722DD231E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26123 mRNA. Translation: BAA05120.1.
X07411 mRNA. Translation: CAA30309.1.
BC010758 mRNA. Translation: AAH10758.1.
CCDSiCCDS25756.1.
PIRiS03382. A28053.
RefSeqiNP_031647.1. NM_007621.2.
UniGeneiMm.21454.

Genome annotation databases

EnsembliENSMUST00000026148; ENSMUSP00000026148; ENSMUSG00000025150.
GeneIDi12409.
KEGGimmu:12409.
UCSCiuc007muj.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26123 mRNA. Translation: BAA05120.1.
X07411 mRNA. Translation: CAA30309.1.
BC010758 mRNA. Translation: AAH10758.1.
CCDSiCCDS25756.1.
PIRiS03382. A28053.
RefSeqiNP_031647.1. NM_007621.2.
UniGeneiMm.21454.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CYDX-ray1.80A/B/C/D1-244[»]
ProteinModelPortaliP08074.
SMRiP08074. Positions 3-244.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP08074. 1 interaction.
MINTiMINT-4090057.
STRINGi10090.ENSMUSP00000026148.

PTM databases

iPTMnetiP08074.
PhosphoSiteiP08074.

Proteomic databases

EPDiP08074.
PaxDbiP08074.
PeptideAtlasiP08074.
PRIDEiP08074.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026148; ENSMUSP00000026148; ENSMUSG00000025150.
GeneIDi12409.
KEGGimmu:12409.
UCSCiuc007muj.2. mouse.

Organism-specific databases

CTDi12409.
MGIiMGI:107200. Cbr2.

Phylogenomic databases

eggNOGiKOG1207. Eukaryota.
ENOG410XQCY. LUCA.
HOVERGENiHBG105069.
InParanoidiP08074.
KOiK00081.
OMAiKGAMTML.
OrthoDBiEOG74TX0K.
PhylomeDBiP08074.
TreeFamiTF313841.

Enzyme and pathway databases

SABIO-RKP08074.

Miscellaneous databases

EvolutionaryTraceiP08074.
PROiP08074.
SOURCEiSearch...

Gene expression databases

BgeeiP08074.
CleanExiMM_CBR2.
ExpressionAtlasiP08074. baseline and differential.
GenevisibleiP08074. MM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF THR-38, COENZYME SPECIFICITY.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND SER-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas and Testis.
  7. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH NADPH.

Entry informationi

Entry nameiCBR2_MOUSE
AccessioniPrimary (citable) accession number: P08074
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: July 6, 2016
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Uses both NADP and NAD as substrates. Has a strong preference for NADP.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.