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Carbonyl reductase [NADPH] 2 (EC 1.1.1.184) (Adipocyte protein P27) (AP27) (Lung carbonyl reductase) (LCR) (NADPH-dependent carbonyl reductase 2)

 CBR2_MOUSE              Reviewed;         244 AA.
P08074;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
28-FEB-2018, entry version 153.
RecName: Full=Carbonyl reductase [NADPH] 2;
EC=1.1.1.184;
AltName: Full=Adipocyte protein P27;
Short=AP27;
AltName: Full=Lung carbonyl reductase;
Short=LCR;
AltName: Full=NADPH-dependent carbonyl reductase 2;
Name=Cbr2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=CH3;
PubMed=2455724; DOI=10.1083/jcb.107.1.279;
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; DOI=10.1111/j.1432-1033.1995.tb20274.x;
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;
PubMed=15489334; DOI=10.1101/gr.2596504;
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.
PubMed=8040004; DOI=10.1007/BF00157764;
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.
PubMed=8999926; DOI=10.1074/jbc.272.4.2218;
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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND SER-176, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH NADPH.
PubMed=8805511; DOI=10.1016/S0969-2126(96)00007-X;
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).
-!- 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.
{ECO:0000269|PubMed:7705352}.
-!- CATALYTIC ACTIVITY: R-CHOH-R' + NADP(+) = R-CO-R' + NADPH.
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:8805511}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000269|PubMed:8040004}.
-!- 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. {ECO:0000305}.
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EMBL; D26123; BAA05120.1; -; mRNA.
EMBL; X07411; CAA30309.1; -; mRNA.
EMBL; BC010758; AAH10758.1; -; mRNA.
CCDS; CCDS25756.1; -.
PIR; S03382; A28053.
RefSeq; NP_031647.1; NM_007621.2.
UniGene; Mm.21454; -.
PDB; 1CYD; X-ray; 1.80 A; A/B/C/D=1-244.
PDBsum; 1CYD; -.
ProteinModelPortal; P08074; -.
SMR; P08074; -.
IntAct; P08074; 1.
MINT; P08074; -.
STRING; 10090.ENSMUSP00000026148; -.
iPTMnet; P08074; -.
PhosphoSitePlus; P08074; -.
PaxDb; P08074; -.
PeptideAtlas; P08074; -.
PRIDE; P08074; -.
Ensembl; ENSMUST00000026148; ENSMUSP00000026148; ENSMUSG00000025150.
GeneID; 12409; -.
KEGG; mmu:12409; -.
UCSC; uc007muj.2; mouse.
CTD; 12409; -.
MGI; MGI:107200; Cbr2.
eggNOG; KOG1207; Eukaryota.
eggNOG; ENOG410XQCY; LUCA.
GeneTree; ENSGT00910000144022; -.
HOVERGEN; HBG105069; -.
InParanoid; P08074; -.
KO; K00081; -.
OMA; SMKGAME; -.
OrthoDB; EOG091G0GV2; -.
PhylomeDB; P08074; -.
TreeFam; TF313841; -.
SABIO-RK; P08074; -.
EvolutionaryTrace; P08074; -.
PRO; PR:P08074; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000025150; -.
CleanEx; MM_CBR2; -.
ExpressionAtlas; P08074; baseline and differential.
Genevisible; P08074; MM.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0004090; F:carbonyl reductase (NADPH) activity; IDA:MGI.
GO; GO:0043621; F:protein self-association; IDA:MGI.
GO; GO:0006116; P:NADH oxidation; TAS:MGI.
GO; GO:0051262; P:protein tetramerization; IDA:MGI.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020904; Sc_DH/Rdtase_CS.
InterPro; IPR002347; SDR_fam.
PRINTS; PR00081; GDHRDH.
PRINTS; PR00080; SDRFAMILY.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00061; ADH_SHORT; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Mitochondrion; NAD; NADP; Oxidoreductase; Phosphoprotein;
Reference proteome.
CHAIN 1 244 Carbonyl reductase [NADPH] 2.
/FTId=PRO_0000054547.
NP_BIND 11 39 NADP. {ECO:0000269|PubMed:8805511}.
ACT_SITE 149 149 Proton acceptor.
BINDING 136 136 Substrate.
MOD_RES 42 42 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 176 176 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MUTAGEN 38 38 T->R: Converts the coenzyme specificity
from NADP to NAD.
{ECO:0000269|PubMed:8999926}.
STRAND 9 14 {ECO:0000244|PDB:1CYD}.
HELIX 18 29 {ECO:0000244|PDB:1CYD}.
STRAND 33 39 {ECO:0000244|PDB:1CYD}.
HELIX 41 50 {ECO:0000244|PDB:1CYD}.
STRAND 55 58 {ECO:0000244|PDB:1CYD}.
HELIX 64 71 {ECO:0000244|PDB:1CYD}.
STRAND 78 82 {ECO:0000244|PDB:1CYD}.
HELIX 92 94 {ECO:0000244|PDB:1CYD}.
HELIX 97 107 {ECO:0000244|PDB:1CYD}.
HELIX 109 125 {ECO:0000244|PDB:1CYD}.
STRAND 129 134 {ECO:0000244|PDB:1CYD}.
HELIX 137 139 {ECO:0000244|PDB:1CYD}.
HELIX 147 167 {ECO:0000244|PDB:1CYD}.
HELIX 168 170 {ECO:0000244|PDB:1CYD}.
STRAND 172 179 {ECO:0000244|PDB:1CYD}.
HELIX 185 190 {ECO:0000244|PDB:1CYD}.
HELIX 194 203 {ECO:0000244|PDB:1CYD}.
HELIX 212 223 {ECO:0000244|PDB:1CYD}.
HELIX 225 227 {ECO:0000244|PDB:1CYD}.
STRAND 232 238 {ECO:0000244|PDB:1CYD}.
HELIX 241 243 {ECO:0000244|PDB:1CYD}.
SEQUENCE 244 AA; 25958 MW; 4FA14C5722DD231E CRC64;
MKLNFSGLRA LVTGAGKGIG RDTVKALHAS GAKVVAVTRT NSDLVSLAKE CPGIEPVCVD
LGDWDATEKA LGGIGPVDLL VNNAALVIMQ PFLEVTKEAF DRSFSVNLRS VFQVSQMVAR
DMINRGVPGS IVNVSSMVAH VTFPNLITYS STKGAMTMLT KAMAMELGPH KIRVNSVNPT
VVLTDMGKKV SADPEFARKL KERHPLRKFA EVEDVVNSIL FLLSDRSAST SGGGILVDAG
YLAS


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