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Protein

Carbonyl reductase [NADPH] 2

Gene

Cbr2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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

Miscellaneous

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

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei136Substrate1
Active sitei149Proton acceptor1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi11 – 39NADP1 PublicationAdd BLAST29

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

Keywordsi

Molecular functionOxidoreductase
LigandNAD, NADP

Enzyme and pathway databases

SABIO-RKiP08074

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:107200 Cbr2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi38T → R: Converts the coenzyme specificity from NADP to NAD. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000545471 – 244Carbonyl reductase [NADPH] 2Add BLAST244

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei42PhosphoserineCombined sources1
Modified residuei176PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP08074
PeptideAtlasiP08074
PRIDEiP08074

PTM databases

iPTMnetiP08074
PhosphoSitePlusiP08074

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

BgeeiENSMUSG00000025150
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 interactor
MINTiP08074
STRINGi10090.ENSMUSP00000026148

Structurei

Secondary structure

1244
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 14Combined sources6
Helixi18 – 29Combined sources12
Beta strandi33 – 39Combined sources7
Helixi41 – 50Combined sources10
Beta strandi55 – 58Combined sources4
Helixi64 – 71Combined sources8
Beta strandi78 – 82Combined sources5
Helixi92 – 94Combined sources3
Helixi97 – 107Combined sources11
Helixi109 – 125Combined sources17
Beta strandi129 – 134Combined sources6
Helixi137 – 139Combined sources3
Helixi147 – 167Combined sources21
Helixi168 – 170Combined sources3
Beta strandi172 – 179Combined sources8
Helixi185 – 190Combined sources6
Helixi194 – 203Combined sources10
Helixi212 – 223Combined sources12
Helixi225 – 227Combined sources3
Beta strandi232 – 238Combined sources7
Helixi241 – 243Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP08074

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1207 Eukaryota
ENOG410XQCY LUCA
GeneTreeiENSGT00910000144022
HOVERGENiHBG105069
InParanoidiP08074
KOiK00081
OMAiSMKGAME
OrthoDBiEOG091G0GV2
PhylomeDBiP08074
TreeFamiTF313841

Family and domain databases

InterProiView protein in InterPro
IPR036291 NAD(P)-bd_dom_sf
IPR020904 Sc_DH/Rdtase_CS
IPR002347 SDR_fam
PRINTSiPR00081 GDHRDH
PR00080 SDRFAMILY
SUPFAMiSSF51735 SSF51735, 1 hit
PROSITEiView protein in PROSITE
PS00061 ADH_SHORT, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiCBR2_MOUSE
AccessioniPrimary (citable) accession number: P08074
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: May 23, 2018
This is version 154 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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

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