ID   CBR2_PIG                Reviewed;         244 AA.
AC   Q29529;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Carbonyl reductase [NADPH] 2;
DE            EC=1.1.1.184;
DE   AltName: Full=Lung carbonyl reductase;
DE            Short=LCR;
DE   AltName: Full=NADPH-dependent carbonyl reductase 2;
GN   Name=CBR2;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Lung;
RX   PubMed=8352790; DOI=10.1006/bbrc.1993.1967;
RA   Nakanishi M., Deyashiki Y., Nakayama T., Sato T., Hara A.;
RT   "Cloning and sequence analysis of a cDNA encoding tetrameric carbonyl
RT   reductase of pig lung.";
RL   Biochem. Biophys. Res. Commun. 194:1311-1316(1993).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=1731616; DOI=10.1016/0003-9861(92)90028-u;
RA   Oritani H., Deyashiki Y., Nakayama T., Hara A., Sawada H., Matsuura K.,
RA   Bunai Y., Ohya I.;
RT   "Purification and characterization of pig lung carbonyl reductase.";
RL   Arch. Biochem. Biophys. 292:539-547(1992).
CC   -!- FUNCTION: May function in the pulmonary metabolism of endogenous
CC       carbonyl compounds, such as aliphatic aldehydes and ketones derived
CC       from lipid peroxidation, 3-ketosteroids and fatty aldehydes, as well as
CC       in xenobiotic metabolism. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a secondary alcohol + NADP(+) = a ketone + H(+) + NADPH;
CC         Xref=Rhea:RHEA:19257, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC         ChEBI:CHEBI:35681, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.184;
CC   -!- ACTIVITY REGULATION: Allosteric enzyme exhibiting negative
CC       cooperativity. Activated 2-5 fold by fatty acids.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Lung (ciliated cells, non-ciliated bronchiolar
CC       cells and type-II alveolar pneumocytes). Low expression in all
CC       extrapulmonary tissues, including adipose tissue.
CC   -!- INDUCTION: By glucocorticoids.
CC   -!- MISCELLANEOUS: Uses both NADP and NAD as substrates. Has a strong
CC       preference for NADP.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; D16511; BAA03963.1; -; mRNA.
DR   PIR; JN0703; JN0703.
DR   RefSeq; NP_998992.1; NM_213827.1.
DR   AlphaFoldDB; Q29529; -.
DR   SMR; Q29529; -.
DR   PeptideAtlas; Q29529; -.
DR   PRIDE; Q29529; -.
DR   GeneID; 396780; -.
DR   KEGG; ssc:396780; -.
DR   CTD; 12409; -.
DR   InParanoid; Q29529; -.
DR   OrthoDB; 1051625at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004090; F:carbonyl reductase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   Allosteric enzyme; Direct protein sequencing; Mitochondrion; NAD; NADP;
KW   Oxidoreductase; Phosphoprotein; Reference proteome.
FT   CHAIN           1..244
FT                   /note="Carbonyl reductase [NADPH] 2"
FT                   /id="PRO_0000054548"
FT   ACT_SITE        149
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         11..39
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         176
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08074"
SQ   SEQUENCE   244 AA;  25986 MW;  7F4AE194B3DB7674 CRC64;
     MQMNFSGLRA LVTGAGKGIG RDTVKALHVS GARVVAVTRT NGDLVSLSQE CPGIEPVCVD
     LGDWEATERA LGGVGPVDLL VNNAAVALMQ PFLDTTKEVF DRSFNVNLRS VFQVSQIVAR
     SMIERGVPGS IVNVSSMVSH VTYPGLAAYS STKGAMTMLT KSMAMELGPH KIRVNSVNPT
     VVLTAMGRSV TSDPELARKL KERHPMRKFA EVEDVVNSIL FLLSDRSAST SGSSIFVDAG
     YLAS