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Carbonyl reductase [NADPH] 1 (EC 1.1.1.184) (15-hydroxyprostaglandin dehydrogenase [NADP( )]) (EC 1.1.1.197) (NADPH-dependent carbonyl reductase 1) (Prostaglandin 9-ketoreductase) (Prostaglandin-E(2) 9-reductase) (EC 1.1.1.189) (Short chain dehydrogenase/reductase family 21C member 1)

 CBR1_HUMAN              Reviewed;         277 AA.
P16152; B2RBZ7; B4DFK7; Q3LHW8;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 193.
RecName: Full=Carbonyl reductase [NADPH] 1;
EC=1.1.1.184;
AltName: Full=15-hydroxyprostaglandin dehydrogenase [NADP(+)];
EC=1.1.1.197;
AltName: Full=NADPH-dependent carbonyl reductase 1;
AltName: Full=Prostaglandin 9-ketoreductase;
AltName: Full=Prostaglandin-E(2) 9-reductase;
EC=1.1.1.189;
AltName: Full=Short chain dehydrogenase/reductase family 21C member 1;
Name=CBR1; Synonyms=CBR, CRN, SDR21C1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Placenta;
PubMed=3141401;
Wermuth B., Bohren K.M., Heinemann G., von Wartburg J.-P.,
Gabbay K.H.;
"Human carbonyl reductase. Nucleotide sequence analysis of a cDNA and
amino acid sequence of the encoded protein.";
J. Biol. Chem. 263:16185-16188(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Mammary gland;
PubMed=2182121; DOI=10.1016/0167-4781(90)90050-C;
Forrest G.L., Akman S., Krutzik S., Paxton R.J., Sparkes R.S.,
Doroshow J., Felsted R.L., Mohandas T., Bachur N.R.;
"Induction of a human carbonyl reductase gene located on chromosome
21.";
Biochim. Biophys. Acta 1048:149-155(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=1921984;
Forrest G.L., Akman S., Doroshow J., Rivera H., Kaplan W.D.;
"Genomic sequence and expression of a cloned human carbonyl reductase
gene with daunorubicin reductase activity.";
Mol. Pharmacol. 40:502-507(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=9740676; DOI=10.1006/geno.1998.5380;
Watanabe K., Sugawara C., Ono A., Fukuzumi Y., Itakura S.,
Yamazaki M., Tashiro H., Osoegawa K., Soeda E., Nomura T.;
"Mapping of a novel human carbonyl reductase, CBR3, and ribosomal
pseudogenes to human chromosome 21q22.2.";
Genomics 52:95-100(1998).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fetal brain;
Terada T., Mizobuchi H.;
"Human fetal brain carbonyl reductases.";
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Hippocampus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANT SER-131.
SeattleSNPs variation discovery resource;
Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10830953; DOI=10.1038/35012518;
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
Lehrach H., Reinhardt R., Yaspo M.-L.;
"The DNA sequence of human chromosome 21.";
Nature 405:311-319(2000).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
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).
[13]
PARTIAL PROTEIN SEQUENCE, AND N6-1-CARBOXYETHYLATION AT LYS-239.
PubMed=8421682; DOI=10.1073/pnas.90.2.502;
Krook M., Ghosh D., Stroemberg R., Carlquist M., Joernvall H.;
"Carboxyethyllysine in a protein: native carbonyl reductase/NADP(+)-
dependent prostaglandin dehydrogenase.";
Proc. Natl. Acad. Sci. U.S.A. 90:502-506(1993).
[14]
ENZYME REGULATION, AND FUNCTION.
PubMed=18449627; DOI=10.1007/s11095-008-9592-5;
Gonzalez-Covarrubias V., Kalabus J.L., Blanco J.G.;
"Inhibition of polymorphic human carbonyl reductase 1 (CBR1) by the
cardioprotectant flavonoid 7-monohydroxyethyl rutoside (monoHER).";
Pharm. Res. 25:1730-1734(2008).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
X-RAY CRYSTALLOGRAPHY (1.24 ANGSTROMS) OF 2-276 IN COMPLEX WITH THE
SYNTHETIC INHIBITOR HYDROXY-PP AND NADP, IDENTIFICATION BY MASS
SPECTROMETRY, PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
PubMed=15799708; DOI=10.1371/journal.pbio.0030128;
Tanaka M., Bateman R., Rauh D., Vaisberg E., Ramachandani S.,
Zhang C., Hansen K.C., Burlingame A.L., Trautman J.K., Shokat K.M.,
Adams C.L.;
"An unbiased cell morphology-based screen for new, biologically active
small molecules.";
PLoS Biol. 3:E128-E128(2005).
[18]
X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 2-277 IN COMPLEX WITH NADP
AND FORMALDEHYDE-GLUTATHIONE ADDUCT, AND FUNCTION.
PubMed=17912391; DOI=10.1039/b707602a;
Bateman R., Rauh D., Shokat K.M.;
"Glutathione traps formaldehyde by formation of a
bicyclo[4.4.1]undecane adduct.";
Org. Biomol. Chem. 5:3363-3367(2007).
[19]
X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 2-277 IN COMPLEX WITH NADP,
SUBSTRATE ANALOGS, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=18826943; DOI=10.1074/jbc.M807125200;
Bateman R.L., Rauh D., Tavshanjian B., Shokat K.M.;
"Human carbonyl reductase 1 is an S-nitrosoglutathione reductase.";
J. Biol. Chem. 283:35756-35762(2008).
[20]
VARIANT ILE-88, CHARACTERIZATION OF VARIANT ILE-88, BIOPHYSICOCHEMICAL
PROPERTIES, AND ENZYME REGULATION.
PubMed=17344335; DOI=10.1124/dmd.107.014779;
Gonzalez-Covarrubias V., Ghosh D., Lakhman S.S., Pendyala L.,
Blanco J.G.;
"A functional genetic polymorphism on human carbonyl reductase 1 (CBR1
V88I) impacts on catalytic activity and NADPH binding affinity.";
Drug Metab. Dispos. 35:973-980(2007).
-!- FUNCTION: NADPH-dependent reductase with broad substrate
specificity. Catalyzes the reduction of a wide variety of carbonyl
compounds including quinones, prostaglandins, menadione, plus
various xenobiotics. Catalyzes the reduction of the antitumor
anthracyclines doxorubicin and daunorubicin to the cardiotoxic
compounds doxorubicinol and daunorubicinol. Can convert
prostaglandin E2 to prostaglandin F2-alpha. Can bind glutathione,
which explains its higher affinity for glutathione-conjugated
substrates. Catalyzes the reduction of S-nitrosoglutathione.
{ECO:0000269|PubMed:15799708, ECO:0000269|PubMed:17912391,
ECO:0000269|PubMed:18449627, ECO:0000269|PubMed:18826943}.
-!- CATALYTIC ACTIVITY: R-CHOH-R' + NADP(+) = R-CO-R' + NADPH.
-!- CATALYTIC ACTIVITY: (5Z,13E)-(15S)-9-alpha,11-alpha,15-
trihydroxyprosta-5,13-dienoate + NADP(+) = (5Z,13E)-(15S)-11-
alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate + NADPH.
-!- CATALYTIC ACTIVITY: (13E)-(15S)-11-alpha,15-dihydroxy-9-oxoprost-
13-enoate + NADP(+) = (13E)-11-alpha-hydroxy-9,15-dioxoprost-13-
enoate + NADPH.
-!- ENZYME REGULATION: Inhibited by quercetin, rutenin and its
derivatives. {ECO:0000269|PubMed:17344335,
ECO:0000269|PubMed:18449627}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=30 uM for S-nitrosoglutathione {ECO:0000269|PubMed:17344335,
ECO:0000269|PubMed:18826943};
KM=22 uM for menadione {ECO:0000269|PubMed:17344335,
ECO:0000269|PubMed:18826943};
KM=309 uM for prostaglandin E2 {ECO:0000269|PubMed:17344335,
ECO:0000269|PubMed:18826943};
KM=173 uM for daunorubicin {ECO:0000269|PubMed:17344335,
ECO:0000269|PubMed:18826943};
KM=247 uM for NADPH {ECO:0000269|PubMed:17344335,
ECO:0000269|PubMed:18826943};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15799708,
ECO:0000269|PubMed:17912391, ECO:0000269|PubMed:18826943}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P16152-1; Sequence=Displayed;
Name=2;
IsoId=P16152-2; Sequence=VSP_054796, VSP_054797;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
(SDR) family. {ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/cbr1/";
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EMBL; J04056; AAA52070.1; -; mRNA.
EMBL; M62420; AAA17881.1; -; Genomic_DNA.
EMBL; AB003151; BAA33498.1; -; Genomic_DNA.
EMBL; AP000688; BAA89424.1; -; Genomic_DNA.
EMBL; AB124848; BAE45940.1; -; mRNA.
EMBL; BT019843; AAV38646.1; -; mRNA.
EMBL; CR541708; CAG46509.1; -; mRNA.
EMBL; AK294142; BAG57468.1; -; mRNA.
EMBL; AK314879; BAG37394.1; -; mRNA.
EMBL; EF141836; ABK97430.1; -; Genomic_DNA.
EMBL; AP001724; BAA95508.1; -; Genomic_DNA.
EMBL; CH471079; EAX09754.1; -; Genomic_DNA.
EMBL; CH471079; EAX09755.1; -; Genomic_DNA.
EMBL; BC002511; AAH02511.1; -; mRNA.
EMBL; BC015640; AAH15640.1; -; mRNA.
CCDS; CCDS13641.1; -. [P16152-1]
CCDS; CCDS68202.1; -. [P16152-2]
PIR; A61271; RDHUCB.
RefSeq; NP_001273718.1; NM_001286789.1. [P16152-2]
RefSeq; NP_001748.1; NM_001757.3. [P16152-1]
UniGene; Hs.88778; -.
PDB; 1WMA; X-ray; 1.24 A; A=2-277.
PDB; 2PFG; X-ray; 1.54 A; A=2-277.
PDB; 3BHI; X-ray; 2.27 A; A=2-277.
PDB; 3BHJ; X-ray; 1.77 A; A=2-277.
PDB; 3BHM; X-ray; 1.80 A; A=2-277.
PDB; 4Z3D; X-ray; 1.80 A; A/B/C/D=2-277.
PDBsum; 1WMA; -.
PDBsum; 2PFG; -.
PDBsum; 3BHI; -.
PDBsum; 3BHJ; -.
PDBsum; 3BHM; -.
PDBsum; 4Z3D; -.
ProteinModelPortal; P16152; -.
SMR; P16152; -.
BioGrid; 107319; 38.
DIP; DIP-33136N; -.
IntAct; P16152; 27.
MINT; MINT-1418935; -.
STRING; 9606.ENSP00000290349; -.
BindingDB; P16152; -.
ChEMBL; CHEMBL5586; -.
DrugBank; DB00414; Acetohexamide.
DrugBank; DB00997; Doxorubicin.
DrugBank; DB00502; Haloperidol.
DrugBank; DB01046; Lubiprostone.
DrugBank; DB05197; Sofalcone.
DrugBank; DB04844; Tetrabenazine.
GuidetoPHARMACOLOGY; 1383; -.
iPTMnet; P16152; -.
PhosphoSitePlus; P16152; -.
SwissPalm; P16152; -.
BioMuta; CBR1; -.
DMDM; 118519; -.
REPRODUCTION-2DPAGE; IPI00295386; -.
UCD-2DPAGE; P16152; -.
EPD; P16152; -.
MaxQB; P16152; -.
PaxDb; P16152; -.
PeptideAtlas; P16152; -.
PRIDE; P16152; -.
TopDownProteomics; P16152-1; -. [P16152-1]
DNASU; 873; -.
Ensembl; ENST00000290349; ENSP00000290349; ENSG00000159228. [P16152-1]
Ensembl; ENST00000530908; ENSP00000434613; ENSG00000159228. [P16152-2]
GeneID; 873; -.
KEGG; hsa:873; -.
UCSC; uc002yvb.3; human. [P16152-1]
CTD; 873; -.
DisGeNET; 873; -.
EuPathDB; HostDB:ENSG00000159228.12; -.
GeneCards; CBR1; -.
HGNC; HGNC:1548; CBR1.
HPA; HPA018433; -.
MIM; 114830; gene.
neXtProt; NX_P16152; -.
OpenTargets; ENSG00000159228; -.
PharmGKB; PA26121; -.
eggNOG; KOG1208; Eukaryota.
eggNOG; COG1028; LUCA.
GeneTree; ENSGT00510000046499; -.
HOVERGEN; HBG001909; -.
InParanoid; P16152; -.
KO; K00079; -.
OMA; TENSMEN; -.
OrthoDB; EOG091G0V7L; -.
PhylomeDB; P16152; -.
TreeFam; TF329359; -.
BRENDA; 1.1.1.184; 2681.
Reactome; R-HSA-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
SABIO-RK; P16152; -.
EvolutionaryTrace; P16152; -.
GeneWiki; CBR1; -.
GenomeRNAi; 873; -.
PRO; PR:P16152; -.
Proteomes; UP000005640; Chromosome 21.
Bgee; ENSG00000159228; -.
CleanEx; HS_CBR1; -.
ExpressionAtlas; P16152; baseline and differential.
Genevisible; P16152; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:1903561; C:extracellular vesicle; IDA:UniProtKB.
GO; GO:0047021; F:15-hydroxyprostaglandin dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
GO; GO:0004090; F:carbonyl reductase (NADPH) activity; IDA:UniProtKB.
GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IDA:UniProtKB.
GO; GO:0050221; F:prostaglandin-E2 9-reductase activity; TAS:Reactome.
GO; GO:0019371; P:cyclooxygenase pathway; TAS:Reactome.
GO; GO:0017144; P:drug metabolic process; IDA:UniProtKB.
GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB.
GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
GO; GO:0042373; P:vitamin K metabolic process; IDA:UniProtKB.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020904; Sc_DH/Rdtase_CS.
InterPro; IPR002347; SDR_fam.
Pfam; PF00106; adh_short; 1.
PRINTS; PR00081; GDHRDH.
PRINTS; PR00080; SDRFAMILY.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00061; ADH_SHORT; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; NADP; Oxidoreductase;
Phosphoprotein; Polymorphism; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 277 Carbonyl reductase [NADPH] 1.
/FTId=PRO_0000054602.
NP_BIND 10 34 NADP. {ECO:0000269|PubMed:15799708,
ECO:0000269|PubMed:17912391,
ECO:0000269|PubMed:18826943}.
NP_BIND 63 64 NADP. {ECO:0000269|PubMed:15799708,
ECO:0000269|PubMed:17912391,
ECO:0000269|PubMed:18826943}.
NP_BIND 194 198 NADP. {ECO:0000269|PubMed:15799708,
ECO:0000269|PubMed:17912391,
ECO:0000269|PubMed:18826943}.
NP_BIND 231 233 NADP. {ECO:0000269|PubMed:15799708,
ECO:0000269|PubMed:17912391,
ECO:0000269|PubMed:18826943}.
REGION 95 97 Glutathione binding.
REGION 193 194 Glutathione binding.
ACT_SITE 194 194 Proton acceptor.
BINDING 90 90 NADP; via carbonyl oxygen.
{ECO:0000269|PubMed:15799708,
ECO:0000269|PubMed:17912391,
ECO:0000269|PubMed:18826943}.
BINDING 106 106 Glutathione.
BINDING 140 140 Substrate.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000250|UniProtKB:P47727}.
MOD_RES 30 30 Phosphoserine.
{ECO:0000250|UniProtKB:P48758}.
MOD_RES 239 239 N6-1-carboxyethyl lysine.
{ECO:0000269|PubMed:8421682}.
VAR_SEQ 133 173 GRVVNVSSIMSVRALKSCSPELQQKFRSETITEEELVGLMN
-> ASCVLSAWSCLSQNPSGGKSKPLAWFTEMSIICRCLTL
GPF (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054796.
VAR_SEQ 174 277 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054797.
VARIANT 88 88 V -> I (reduced affinity for NADPH and
reduced activity towards daunorubicin and
prostaglandin E2; dbSNP:rs1143663).
{ECO:0000269|PubMed:17344335}.
/FTId=VAR_059053.
VARIANT 131 131 P -> S (in dbSNP:rs41557318).
{ECO:0000269|Ref.9}.
/FTId=VAR_031706.
STRAND 7 12 {ECO:0000244|PDB:1WMA}.
HELIX 16 28 {ECO:0000244|PDB:1WMA}.
STRAND 29 39 {ECO:0000244|PDB:1WMA}.
HELIX 40 52 {ECO:0000244|PDB:1WMA}.
STRAND 58 61 {ECO:0000244|PDB:1WMA}.
HELIX 67 81 {ECO:0000244|PDB:1WMA}.
STRAND 82 89 {ECO:0000244|PDB:1WMA}.
HELIX 103 114 {ECO:0000244|PDB:1WMA}.
HELIX 116 125 {ECO:0000244|PDB:1WMA}.
HELIX 126 128 {ECO:0000244|PDB:1WMA}.
STRAND 129 138 {ECO:0000244|PDB:1WMA}.
HELIX 141 148 {ECO:0000244|PDB:1WMA}.
HELIX 152 159 {ECO:0000244|PDB:1WMA}.
HELIX 165 180 {ECO:0000244|PDB:1WMA}.
TURN 184 188 {ECO:0000244|PDB:1WMA}.
HELIX 193 215 {ECO:0000244|PDB:1WMA}.
STRAND 222 227 {ECO:0000244|PDB:1WMA}.
TURN 234 236 {ECO:0000244|PDB:1WMA}.
HELIX 244 247 {ECO:0000244|PDB:1WMA}.
HELIX 249 255 {ECO:0000244|PDB:1WMA}.
STRAND 268 270 {ECO:0000244|PDB:1WMA}.
STRAND 273 275 {ECO:0000244|PDB:1WMA}.
SEQUENCE 277 AA; 30375 MW; 51A5A495EB4F4EC3 CRC64;
MSSGIHVALV TGGNKGIGLA IVRDLCRLFS GDVVLTARDV TRGQAAVQQL QAEGLSPRFH
QLDIDDLQSI RALRDFLRKE YGGLDVLVNN AGIAFKVADP TPFHIQAEVT MKTNFFGTRD
VCTELLPLIK PQGRVVNVSS IMSVRALKSC SPELQQKFRS ETITEEELVG LMNKFVEDTK
KGVHQKEGWP SSAYGVTKIG VTVLSRIHAR KLSEQRKGDK ILLNACCPGW VRTDMAGPKA
TKSPEEGAET PVYLALLPPD AEGPHGQFVS EKRVEQW


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