CBR3_MOUSE
ID CBR3_MOUSE Reviewed; 277 AA.
AC Q8K354;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Carbonyl reductase [NADPH] 3;
DE EC=1.1.1.184 {ECO:0000250|UniProtKB:O75828};
DE AltName: Full=NADPH-dependent carbonyl reductase 3;
DE AltName: Full=Quinone reductase CBR3;
DE EC=1.6.5.10 {ECO:0000250|UniProtKB:O75828};
GN Name=Cbr3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, Czech II, and FVB/N-3;
RC TISSUE=Lung, Mammary gland, and Mammary tumor;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Lung, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of carbonyl compounds
CC to their corresponding alcohols. Has low NADPH-dependent oxidoreductase
CC activity. Acts on several orthoquinones, acts as well on non-quinone
CC compounds, such as isatin or on the anticancer drug oracin. Best
CC substrates for CBR3 is 1,2- naphthoquinone, hence could play a role in
CC protection against cytotoxicity of exogenous quinones. Exerts activity
CC toward ortho-quinones but not paraquinones. No endogenous substrate for
CC CBR3 except isatin has been identified. {ECO:0000250|UniProtKB:O75828}.
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; Evidence={ECO:0000250|UniProtKB:O75828};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19258;
CC Evidence={ECO:0000250|UniProtKB:O75828};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H(+) + NADPH = a quinol + NADP(+);
CC Xref=Rhea:RHEA:46164, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132124;
CC EC=1.6.5.10; Evidence={ECO:0000250|UniProtKB:O75828};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46165;
CC Evidence={ECO:0000250|UniProtKB:O75828};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O75828}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AK028150; BAC25778.1; -; mRNA.
DR EMBL; AC154449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466602; EDL03763.1; -; Genomic_DNA.
DR EMBL; BC028763; AAH28763.1; -; mRNA.
DR EMBL; BC087735; AAH87735.1; -; mRNA.
DR EMBL; BC096658; AAH96658.1; -; mRNA.
DR CCDS; CCDS28342.1; -.
DR RefSeq; NP_766635.1; NM_173047.3.
DR AlphaFoldDB; Q8K354; -.
DR SMR; Q8K354; -.
DR BioGRID; 225103; 3.
DR IntAct; Q8K354; 2.
DR MINT; Q8K354; -.
DR STRING; 10090.ENSMUSP00000047712; -.
DR iPTMnet; Q8K354; -.
DR PhosphoSitePlus; Q8K354; -.
DR EPD; Q8K354; -.
DR jPOST; Q8K354; -.
DR MaxQB; Q8K354; -.
DR PaxDb; Q8K354; -.
DR PeptideAtlas; Q8K354; -.
DR PRIDE; Q8K354; -.
DR ProteomicsDB; 279932; -.
DR Antibodypedia; 8258; 319 antibodies from 35 providers.
DR DNASU; 109857; -.
DR Ensembl; ENSMUST00000039620; ENSMUSP00000047712; ENSMUSG00000022947.
DR GeneID; 109857; -.
DR KEGG; mmu:109857; -.
DR UCSC; uc007zzs.2; mouse.
DR CTD; 874; -.
DR MGI; MGI:1309992; Cbr3.
DR VEuPathDB; HostDB:ENSMUSG00000022947; -.
DR eggNOG; KOG1208; Eukaryota.
DR GeneTree; ENSGT00940000162541; -.
DR HOGENOM; CLU_010194_9_0_1; -.
DR InParanoid; Q8K354; -.
DR OMA; RYINSRF; -.
DR OrthoDB; 1259665at2759; -.
DR PhylomeDB; Q8K354; -.
DR TreeFam; TF329359; -.
DR BRENDA; 1.1.1.184; 3474.
DR Reactome; R-MMU-211945; Phase I - Functionalization of compounds.
DR BioGRID-ORCS; 109857; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Cbr3; mouse.
DR PRO; PR:Q8K354; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8K354; protein.
DR Bgee; ENSMUSG00000022947; Expressed in epithelium of stomach and 202 other tissues.
DR ExpressionAtlas; Q8K354; baseline and differential.
DR Genevisible; Q8K354; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000253; F:3-keto sterol reductase activity; ISO:MGI.
DR GO; GO:0004090; F:carbonyl reductase (NADPH) activity; ISS:UniProtKB.
DR GO; GO:0070402; F:NADPH binding; ISO:MGI.
DR GO; GO:0008753; F:NADPH dehydrogenase (quinone) activity; ISS:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0050890; P:cognition; ISO:MGI.
DR GO; GO:0042376; P:phylloquinone catabolic process; ISO:MGI.
DR CDD; cd05324; carb_red_PTCR-like_SDR_c; 1.
DR InterPro; IPR045313; CBR1-like.
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 Acetylation; Cytoplasm; NADP; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P16152"
FT CHAIN 2..277
FT /note="Carbonyl reductase [NADPH] 3"
FT /id="PRO_0000415806"
FT ACT_SITE 194
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 10..34
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O75828"
FT BINDING 38..42
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O75828"
FT BINDING 63..64
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O75828"
FT BINDING 90
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O75828"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 194..198
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O75828"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P16152"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48758"
SQ SEQUENCE 277 AA; 30953 MW; EC6009AB9C83FACF CRC64;
MSSCSRVALV TGANKGIGFA ITRDLCRKFS GDVVLTARDE ARGRAAVQQL QAEGLSPRFH
QLDIDDPQSI RALRDFLRKE YGGLNVLVNN AGIAFRMDDP TPFDIQAEVT LKTNFFATRN
VCTELLPIMK PHGRVVNISS LQGLKALENC REDLQEKFRC DTLTEVDLVD LMKKFVEDTK
NEVHEREGWP DSAYGVSKLG VTVLTRILAR QLDEKRKADR ILLNACCPGW VKTDMARDQG
SRTVEEGAET PVYLALLPPD ATEPHGQLVR DKVVQTW
