ID   CBR1_HUMAN              Reviewed;         277 AA.
AC   P16152; B2RBZ7; B4DFK7; Q3LHW8;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   11-DEC-2019, entry version 212.
DE   RecName: Full=Carbonyl reductase [NADPH] 1;
DE            EC=1.1.1.184;
DE   AltName: Full=15-hydroxyprostaglandin dehydrogenase [NADP(+)];
DE            EC=1.1.1.197;
DE   AltName: Full=NADPH-dependent carbonyl reductase 1;
DE   AltName: Full=Prostaglandin 9-ketoreductase;
DE   AltName: Full=Prostaglandin-E(2) 9-reductase;
DE            EC=1.1.1.189;
DE   AltName: Full=Short chain dehydrogenase/reductase family 21C member 1;
GN   Name=CBR1; Synonyms=CBR, CRN, SDR21C1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Placenta;
RX   PubMed=3141401;
RA   Wermuth B., Bohren K.M., Heinemann G., von Wartburg J.-P., Gabbay K.H.;
RT   "Human carbonyl reductase. Nucleotide sequence analysis of a cDNA and amino
RT   acid sequence of the encoded protein.";
RL   J. Biol. Chem. 263:16185-16188(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Mammary gland;
RX   PubMed=2182121; DOI=10.1016/0167-4781(90)90050-c;
RA   Forrest G.L., Akman S., Krutzik S., Paxton R.J., Sparkes R.S., Doroshow J.,
RA   Felsted R.L., Mohandas T., Bachur N.R.;
RT   "Induction of a human carbonyl reductase gene located on chromosome 21.";
RL   Biochim. Biophys. Acta 1048:149-155(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX   PubMed=1921984;
RA   Forrest G.L., Akman S., Doroshow J., Rivera H., Kaplan W.D.;
RT   "Genomic sequence and expression of a cloned human carbonyl reductase gene
RT   with daunorubicin reductase activity.";
RL   Mol. Pharmacol. 40:502-507(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX   PubMed=9740676; DOI=10.1006/geno.1998.5380;
RA   Watanabe K., Sugawara C., Ono A., Fukuzumi Y., Itakura S., Yamazaki M.,
RA   Tashiro H., Osoegawa K., Soeda E., Nomura T.;
RT   "Mapping of a novel human carbonyl reductase, CBR3, and ribosomal
RT   pseudogenes to human chromosome 21q22.2.";
RL   Genomics 52:95-100(1998).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RA   Terada T., Mizobuchi H.;
RT   "Human fetal brain carbonyl reductases.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA   Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA   LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Hippocampus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANT SER-131.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10830953; DOI=10.1038/35012518;
RA   Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA   Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA   Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA   Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA   Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA   Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA   Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA   Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA   Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA   Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA   Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT   "The DNA sequence of human chromosome 21.";
RL   Nature 405:311-319(2000).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [12]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [13]
RP   PARTIAL PROTEIN SEQUENCE, AND POST-TRANSLATIONAL MODIFICATION AT LYS-239.
RX   PubMed=8421682; DOI=10.1073/pnas.90.2.502;
RA   Krook M., Ghosh D., Stroemberg R., Carlquist M., Joernvall H.;
RT   "Carboxyethyllysine in a protein: native carbonyl reductase/NADP(+)-
RT   dependent prostaglandin dehydrogenase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:502-506(1993).
RN   [14]
RP   ACTIVITY REGULATION, AND FUNCTION.
RX   PubMed=18449627; DOI=10.1007/s11095-008-9592-5;
RA   Gonzalez-Covarrubias V., Kalabus J.L., Blanco J.G.;
RT   "Inhibition of polymorphic human carbonyl reductase 1 (CBR1) by the
RT   cardioprotectant flavonoid 7-monohydroxyethyl rutoside (monoHER).";
RL   Pharm. Res. 25:1730-1734(2008).
RN   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (1.24 ANGSTROMS) OF 2-276 IN COMPLEX WITH THE
RP   SYNTHETIC INHIBITOR HYDROXY-PP AND NADP, IDENTIFICATION BY MASS
RP   SPECTROMETRY, PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
RX   PubMed=15799708; DOI=10.1371/journal.pbio.0030128;
RA   Tanaka M., Bateman R., Rauh D., Vaisberg E., Ramachandani S., Zhang C.,
RA   Hansen K.C., Burlingame A.L., Trautman J.K., Shokat K.M., Adams C.L.;
RT   "An unbiased cell morphology-based screen for new, biologically active
RT   small molecules.";
RL   PLoS Biol. 3:E128-E128(2005).
RN   [18]
RP   X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 2-277 IN COMPLEX WITH NADP AND
RP   FORMALDEHYDE-GLUTATHIONE ADDUCT, AND FUNCTION.
RX   PubMed=17912391; DOI=10.1039/b707602a;
RA   Bateman R., Rauh D., Shokat K.M.;
RT   "Glutathione traps formaldehyde by formation of a bicyclo[4.4.1]undecane
RT   adduct.";
RL   Org. Biomol. Chem. 5:3363-3367(2007).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 2-277 IN COMPLEX WITH NADP,
RP   SUBSTRATE ANALOGS, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=18826943; DOI=10.1074/jbc.m807125200;
RA   Bateman R.L., Rauh D., Tavshanjian B., Shokat K.M.;
RT   "Human carbonyl reductase 1 is an S-nitrosoglutathione reductase.";
RL   J. Biol. Chem. 283:35756-35762(2008).
RN   [20]
RP   VARIANT ILE-88, CHARACTERIZATION OF VARIANT ILE-88, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND ACTIVITY REGULATION.
RX   PubMed=17344335; DOI=10.1124/dmd.107.014779;
RA   Gonzalez-Covarrubias V., Ghosh D., Lakhman S.S., Pendyala L., Blanco J.G.;
RT   "A functional genetic polymorphism on human carbonyl reductase 1 (CBR1
RT   V88I) impacts on catalytic activity and NADPH binding affinity.";
RL   Drug Metab. Dispos. 35:973-980(2007).
CC   -!- FUNCTION: NADPH-dependent reductase with broad substrate specificity.
CC       Catalyzes the reduction of a wide variety of carbonyl compounds
CC       including quinones, prostaglandins, menadione, plus various
CC       xenobiotics. Catalyzes the reduction of the antitumor anthracyclines
CC       doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol
CC       and daunorubicinol. Can convert prostaglandin E2 to prostaglandin F2-
CC       alpha. Can bind glutathione, which explains its higher affinity for
CC       glutathione-conjugated substrates. Catalyzes the reduction of S-
CC       nitrosoglutathione. {ECO:0000269|PubMed:15799708,
CC       ECO:0000269|PubMed:17912391, ECO:0000269|PubMed:18449627,
CC       ECO:0000269|PubMed:18826943}.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + prostaglandin F2alpha = H(+) + NADPH + prostaglandin
CC         E2; Xref=Rhea:RHEA:24508, ChEBI:CHEBI:15378, ChEBI:CHEBI:57404,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:606564;
CC         EC=1.1.1.189;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + prostaglandin E1 = 15-oxo-prostaglandin E1 + H(+) +
CC         NADPH; Xref=Rhea:RHEA:11636, ChEBI:CHEBI:15378, ChEBI:CHEBI:57397,
CC         ChEBI:CHEBI:57401, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.197;
CC   -!- ACTIVITY REGULATION: Inhibited by quercetin, rutenin and its
CC       derivatives. {ECO:0000269|PubMed:17344335,
CC       ECO:0000269|PubMed:18449627}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=30 uM for S-nitrosoglutathione {ECO:0000269|PubMed:17344335,
CC         ECO:0000269|PubMed:18826943};
CC         KM=22 uM for menadione {ECO:0000269|PubMed:17344335,
CC         ECO:0000269|PubMed:18826943};
CC         KM=309 uM for prostaglandin E2 {ECO:0000269|PubMed:17344335,
CC         ECO:0000269|PubMed:18826943};
CC         KM=173 uM for daunorubicin {ECO:0000269|PubMed:17344335,
CC         ECO:0000269|PubMed:18826943};
CC         KM=247 uM for NADPH {ECO:0000269|PubMed:17344335,
CC         ECO:0000269|PubMed:18826943};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15799708,
CC       ECO:0000269|PubMed:17912391, ECO:0000269|PubMed:18826943}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P16152-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P16152-2; Sequence=VSP_054796, VSP_054797;
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/cbr1/";
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; J04056; AAA52070.1; -; mRNA.
DR   EMBL; M62420; AAA17881.1; -; Genomic_DNA.
DR   EMBL; AB003151; BAA33498.1; -; Genomic_DNA.
DR   EMBL; AP000688; BAA89424.1; -; Genomic_DNA.
DR   EMBL; AB124848; BAE45940.1; -; mRNA.
DR   EMBL; BT019843; AAV38646.1; -; mRNA.
DR   EMBL; CR541708; CAG46509.1; -; mRNA.
DR   EMBL; AK294142; BAG57468.1; -; mRNA.
DR   EMBL; AK314879; BAG37394.1; -; mRNA.
DR   EMBL; EF141836; ABK97430.1; -; Genomic_DNA.
DR   EMBL; AP001724; BAA95508.1; -; Genomic_DNA.
DR   EMBL; CH471079; EAX09754.1; -; Genomic_DNA.
DR   EMBL; CH471079; EAX09755.1; -; Genomic_DNA.
DR   EMBL; BC002511; AAH02511.1; -; mRNA.
DR   EMBL; BC015640; AAH15640.1; -; mRNA.
DR   CCDS; CCDS13641.1; -. [P16152-1]
DR   CCDS; CCDS68202.1; -. [P16152-2]
DR   PIR; A61271; RDHUCB.
DR   RefSeq; NP_001273718.1; NM_001286789.1. [P16152-2]
DR   RefSeq; NP_001748.1; NM_001757.3. [P16152-1]
DR   PDB; 1WMA; X-ray; 1.24 A; A=2-277.
DR   PDB; 2PFG; X-ray; 1.54 A; A=2-277.
DR   PDB; 3BHI; X-ray; 2.27 A; A=2-277.
DR   PDB; 3BHJ; X-ray; 1.77 A; A=2-277.
DR   PDB; 3BHM; X-ray; 1.80 A; A=2-277.
DR   PDB; 4Z3D; X-ray; 1.80 A; A/B/C/D=2-277.
DR   PDBsum; 1WMA; -.
DR   PDBsum; 2PFG; -.
DR   PDBsum; 3BHI; -.
DR   PDBsum; 3BHJ; -.
DR   PDBsum; 3BHM; -.
DR   PDBsum; 4Z3D; -.
DR   SMR; P16152; -.
DR   BioGrid; 107319; 47.
DR   DIP; DIP-33136N; -.
DR   IntAct; P16152; 33.
DR   MINT; P16152; -.
DR   STRING; 9606.ENSP00000290349; -.
DR   BindingDB; P16152; -.
DR   ChEMBL; CHEMBL5586; -.
DR   DrugBank; DB03556; 2-(2-{2-[2-(2-{2-[2-(2-Ethoxy-Ethoxy)-Ethoxy]-Ethoxy}-Ethoxy)-Ethoxy]-Ethoxy}-Ethoxy)-Ethanol, Polyethyleneglycol Peg400.
DR   DrugBank; DB04463; 3-(4-Amino-1-Tert-Butyl-1h-Pyrazolo[3,4-D]Pyrimidin-3-Yl)Phenol.
DR   DrugBank; DB00414; Acetohexamide.
DR   DrugBank; DB06263; Amrubicin.
DR   DrugBank; DB11672; Curcumin.
DR   DrugBank; DB14635; Curcumin sulfate.
DR   DrugBank; DB12161; Deutetrabenazine.
DR   DrugBank; DB00997; Doxorubicin.
DR   DrugBank; DB00502; Haloperidol.
DR   DrugBank; DB03394; Heptaethylene glycol.
DR   DrugBank; DB01046; Lubiprostone.
DR   DrugBank; DB04216; Quercetin.
DR   DrugBank; DB02709; Resveratrol.
DR   DrugBank; DB01698; Rutin.
DR   DrugBank; DB05197; Sofalcone.
DR   DrugBank; DB04844; Tetrabenazine.
DR   DrugCentral; P16152; -.
DR   GuidetoPHARMACOLOGY; 1383; -.
DR   iPTMnet; P16152; -.
DR   PhosphoSitePlus; P16152; -.
DR   SwissPalm; P16152; -.
DR   BioMuta; CBR1; -.
DR   DMDM; 118519; -.
DR   REPRODUCTION-2DPAGE; IPI00295386; -.
DR   UCD-2DPAGE; P16152; -.
DR   CPTAC; CPTAC-329; -.
DR   CPTAC; CPTAC-330; -.
DR   EPD; P16152; -.
DR   jPOST; P16152; -.
DR   MassIVE; P16152; -.
DR   MaxQB; P16152; -.
DR   PaxDb; P16152; -.
DR   PeptideAtlas; P16152; -.
DR   PRIDE; P16152; -.
DR   ProteomicsDB; 4051; -.
DR   ProteomicsDB; 53298; -. [P16152-1]
DR   TopDownProteomics; P16152-1; -. [P16152-1]
DR   DNASU; 873; -.
DR   Ensembl; ENST00000290349; ENSP00000290349; ENSG00000159228. [P16152-1]
DR   Ensembl; ENST00000530908; ENSP00000434613; ENSG00000159228. [P16152-2]
DR   GeneID; 873; -.
DR   KEGG; hsa:873; -.
DR   UCSC; uc002yvb.3; human. [P16152-1]
DR   CTD; 873; -.
DR   DisGeNET; 873; -.
DR   EuPathDB; HostDB:ENSG00000159228.12; -.
DR   GeneCards; CBR1; -.
DR   HGNC; HGNC:1548; CBR1.
DR   HPA; HPA018433; -.
DR   MIM; 114830; gene.
DR   neXtProt; NX_P16152; -.
DR   OpenTargets; ENSG00000159228; -.
DR   PharmGKB; PA26121; -.
DR   eggNOG; KOG1208; Eukaryota.
DR   eggNOG; COG1028; LUCA.
DR   GeneTree; ENSGT00510000046499; -.
DR   InParanoid; P16152; -.
DR   KO; K00079; -.
DR   OMA; IRVTNAM; -.
DR   OrthoDB; 1259665at2759; -.
DR   PhylomeDB; P16152; -.
DR   TreeFam; TF329359; -.
DR   BRENDA; 1.1.1.184; 2681.
DR   Reactome; R-HSA-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR   SABIO-RK; P16152; -.
DR   ChiTaRS; CBR1; human.
DR   EvolutionaryTrace; P16152; -.
DR   GeneWiki; CBR1; -.
DR   GenomeRNAi; 873; -.
DR   Pharos; P16152; Tchem.
DR   PRO; PR:P16152; -.
DR   Proteomes; UP000005640; Chromosome 21.
DR   RNAct; P16152; protein.
DR   Bgee; ENSG00000159228; Expressed in 227 organ(s), highest expression level in duodenum.
DR   ExpressionAtlas; P16152; baseline and differential.
DR   Genevisible; P16152; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
DR   GO; GO:0047021; F:15-hydroxyprostaglandin dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004090; F:carbonyl reductase (NADPH) activity; IDA:UniProtKB.
DR   GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IDA:UniProtKB.
DR   GO; GO:0050221; F:prostaglandin-E2 9-reductase activity; TAS:Reactome.
DR   GO; GO:0019371; P:cyclooxygenase pathway; TAS:Reactome.
DR   GO; GO:0017144; P:drug metabolic process; IDA:UniProtKB.
DR   GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB.
DR   GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
DR   GO; GO:0042373; P:vitamin K metabolic process; IDA:UniProtKB.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
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   3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW   Direct protein sequencing; NADP; Oxidoreductase; Phosphoprotein;
KW   Polymorphism; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000244|PubMed:19413330"
FT   CHAIN           2..277
FT                   /note="Carbonyl reductase [NADPH] 1"
FT                   /id="PRO_0000054602"
FT   NP_BIND         10..34
FT                   /note="NADP"
FT                   /evidence="ECO:0000269|PubMed:15799708,
FT                   ECO:0000269|PubMed:17912391, ECO:0000269|PubMed:18826943"
FT   NP_BIND         63..64
FT                   /note="NADP"
FT                   /evidence="ECO:0000269|PubMed:15799708,
FT                   ECO:0000269|PubMed:17912391, ECO:0000269|PubMed:18826943"
FT   NP_BIND         194..198
FT                   /note="NADP"
FT                   /evidence="ECO:0000269|PubMed:15799708,
FT                   ECO:0000269|PubMed:17912391, ECO:0000269|PubMed:18826943"
FT   NP_BIND         231..233
FT                   /note="NADP"
FT                   /evidence="ECO:0000269|PubMed:15799708,
FT                   ECO:0000269|PubMed:17912391, ECO:0000269|PubMed:18826943"
FT   REGION          95..97
FT                   /note="Glutathione binding"
FT   REGION          193..194
FT                   /note="Glutathione binding"
FT   ACT_SITE        194
FT                   /note="Proton acceptor"
FT   BINDING         90
FT                   /note="NADP; via carbonyl oxygen"
FT                   /evidence="ECO:0000269|PubMed:15799708,
FT                   ECO:0000269|PubMed:17912391, ECO:0000269|PubMed:18826943"
FT   BINDING         106
FT                   /note="Glutathione"
FT   BINDING         140
FT                   /note="Substrate"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000244|PubMed:19413330"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P47727"
FT   MOD_RES         30
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48758"
FT   MOD_RES         239
FT                   /note="N6-1-carboxyethyl lysine"
FT                   /evidence="ECO:0000269|PubMed:8421682"
FT   VAR_SEQ         133..173
FT                   /note="GRVVNVSSIMSVRALKSCSPELQQKFRSETITEEELVGLMN -> ASCVLSA
FT                   WSCLSQNPSGGKSKPLAWFTEMSIICRCLTLGPF (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_054796"
FT   VAR_SEQ         174..277
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_054797"
FT   VARIANT         88
FT                   /note="V -> I (reduced affinity for NADPH and reduced
FT                   activity towards daunorubicin and prostaglandin E2;
FT                   dbSNP:rs1143663)"
FT                   /evidence="ECO:0000269|PubMed:17344335"
FT                   /id="VAR_059053"
FT   VARIANT         131
FT                   /note="P -> S (in dbSNP:rs41557318)"
FT                   /evidence="ECO:0000269|Ref.9"
FT                   /id="VAR_031706"
FT   STRAND          7..12
FT                   /evidence="ECO:0000244|PDB:1WMA"
FT   HELIX           16..28
FT                   /evidence="ECO:0000244|PDB:1WMA"
FT   STRAND          29..39
FT                   /evidence="ECO:0000244|PDB:1WMA"
FT   HELIX           40..52
FT                   /evidence="ECO:0000244|PDB:1WMA"
FT   STRAND          58..61
FT                   /evidence="ECO:0000244|PDB:1WMA"
FT   HELIX           67..81
FT                   /evidence="ECO:0000244|PDB:1WMA"
FT   STRAND          82..89
FT                   /evidence="ECO:0000244|PDB:1WMA"
FT   HELIX           103..114
FT                   /evidence="ECO:0000244|PDB:1WMA"
FT   HELIX           116..125
FT                   /evidence="ECO:0000244|PDB:1WMA"
FT   HELIX           126..128
FT                   /evidence="ECO:0000244|PDB:1WMA"
FT   STRAND          129..138
FT                   /evidence="ECO:0000244|PDB:1WMA"
FT   HELIX           141..148
FT                   /evidence="ECO:0000244|PDB:1WMA"
FT   HELIX           152..159
FT                   /evidence="ECO:0000244|PDB:1WMA"
FT   HELIX           165..180
FT                   /evidence="ECO:0000244|PDB:1WMA"
FT   TURN            184..188
FT                   /evidence="ECO:0000244|PDB:1WMA"
FT   HELIX           193..215
FT                   /evidence="ECO:0000244|PDB:1WMA"
FT   STRAND          222..227
FT                   /evidence="ECO:0000244|PDB:1WMA"
FT   TURN            234..236
FT                   /evidence="ECO:0000244|PDB:1WMA"
FT   HELIX           244..247
FT                   /evidence="ECO:0000244|PDB:1WMA"
FT   HELIX           249..255
FT                   /evidence="ECO:0000244|PDB:1WMA"
FT   STRAND          268..270
FT                   /evidence="ECO:0000244|PDB:1WMA"
FT   STRAND          273..275
FT                   /evidence="ECO:0000244|PDB:1WMA"
SQ   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
//