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Protein

Carbonyl reductase [NADPH] 1

Gene

Cbr1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

Catalytic activityi

R-CHOH-R' + NADP+ = R-CO-R' + NADPH.
(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.
(13E)-(15S)-11-alpha,15-dihydroxy-9-oxoprost-13-enoate + NADP+ = (13E)-11-alpha-hydroxy-9,15-dioxoprost-13-enoate + NADPH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei90 – 901NADP; via carbonyl oxygenBy similarity
Binding sitei106 – 1061GlutathioneBy similarity
Binding sitei140 – 1401SubstrateBy similarity
Active sitei194 – 1941Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 3425NADPBy similarityAdd
BLAST
Nucleotide bindingi63 – 642NADPBy similarity
Nucleotide bindingi194 – 1985NADPBy similarity
Nucleotide bindingi231 – 2333NADPBy similarity

GO - Molecular functioni

GO - Biological processi

  • drug metabolic process Source: UniProtKB
  • ovulation from ovarian follicle Source: RGD
  • peptidyl-lysine modification Source: RGD
  • phylloquinone catabolic process Source: RGD
  • response to gonadotropin Source: RGD
  • response to lipopolysaccharide Source: RGD
  • response to testosterone Source: RGD
  • vitamin K metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Carbonyl reductase [NADPH] 1 (EC:1.1.1.184)
Alternative name(s):
15-hydroxyprostaglandin dehydrogenase [NADP(+)] (EC:1.1.1.197)
20-beta-hydroxysteroid dehydrogenase
NADPH-dependent carbonyl reductase 1
Prostaglandin 9-ketoreductase
Prostaglandin-E(2) 9-reductase (EC:1.1.1.189)
Gene namesi
Name:Cbr1
Synonyms:Cbr
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2286. Cbr1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: RGD
  • intracellular membrane-bounded organelle Source: RGD
  • microvillus Source: RGD
  • nucleus Source: RGD
  • plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 277276Carbonyl reductase [NADPH] 1PRO_0000054607Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei2 – 21PhosphoserineCombined sources
Modified residuei162 – 1621PhosphothreonineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP47727.
PRIDEiP47727.

PTM databases

iPTMnetiP47727.
PhosphoSiteiP47727.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi247902. 1 interaction.
IntActiP47727. 1 interaction.
STRINGi10116.ENSRNOP00000064050.

Structurei

3D structure databases

ProteinModelPortaliP47727.
SMRiP47727. Positions 7-277.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni95 – 973Glutathione bindingBy similarity
Regioni193 – 1942Glutathione bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1208. Eukaryota.
COG1028. LUCA.
HOVERGENiHBG001909.
InParanoidiP47727.
KOiK00079.
OrthoDBiEOG7PGDR4.
PhylomeDBiP47727.
TreeFamiTF329359.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P47727-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSDRPVALV TGANKGIGFA IVRDLCRKFL GDVVLTARDE SRGHEAVKQL
60 70 80 90 100
QTEGLSPRFH QLDIDNPQSI RALRDFLLQE YGGLNVLVNN AGIAFKVVDP
110 120 130 140 150
TPFHIQAEVT MKTNFFGTQD VCKELLPIIK PQGRVVNVSS SVSLRALKSC
160 170 180 190 200
SPELQQKFRS ETITEEELVG LMNKFIEDAK KGVHAKEGWP NSAYGVTKIG
210 220 230 240 250
VTVLSRIYAR KLNEERREDK ILLNACCPGW VRTDMAGPKA TKSPEEGAET
260 270
PVYLALLPPG AEGPHGQFVQ DKKVEPW
Length:277
Mass (Da):30,578
Last modified:January 23, 2007 - v2
Checksum:iB0F4738C40011B5B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221V → T AA sequence (Ref. 4) Curated
Sequence conflicti135 – 1351V → D AA sequence (PubMed:8198567).Curated
Sequence conflicti138 – 1381V → H AA sequence (PubMed:8198567).Curated
Sequence conflicti141 – 1444SVSL → GMSR in BAA19007 (PubMed:9015353).Curated
Sequence conflicti176 – 1761I → V in AAI05894 (PubMed:15489334).Curated
Sequence conflicti213 – 2131N → T in AAI05894 (PubMed:15489334).Curated
Sequence conflicti236 – 2361A → T in BAA19007 (PubMed:9015353).Curated
Sequence conflicti239 – 2391K → E in BAA19007 (PubMed:9015353).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X84349 mRNA. Translation: CAA59088.1.
X95986 Genomic DNA. Translation: CAA65230.1.
D89069 mRNA. Translation: BAA19007.1.
BC105893 mRNA. Translation: AAI05894.1.
PIRiS68982. JC5284.
RefSeqiNP_062043.1. NM_019170.2.
UniGeneiRn.3425.

Genome annotation databases

GeneIDi29224.
KEGGirno:29224.
UCSCiRGD:2286. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X84349 mRNA. Translation: CAA59088.1.
X95986 Genomic DNA. Translation: CAA65230.1.
D89069 mRNA. Translation: BAA19007.1.
BC105893 mRNA. Translation: AAI05894.1.
PIRiS68982. JC5284.
RefSeqiNP_062043.1. NM_019170.2.
UniGeneiRn.3425.

3D structure databases

ProteinModelPortaliP47727.
SMRiP47727. Positions 7-277.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247902. 1 interaction.
IntActiP47727. 1 interaction.
STRINGi10116.ENSRNOP00000064050.

PTM databases

iPTMnetiP47727.
PhosphoSiteiP47727.

Proteomic databases

PaxDbiP47727.
PRIDEiP47727.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29224.
KEGGirno:29224.
UCSCiRGD:2286. rat.

Organism-specific databases

CTDi873.
RGDi2286. Cbr1.

Phylogenomic databases

eggNOGiKOG1208. Eukaryota.
COG1028. LUCA.
HOVERGENiHBG001909.
InParanoidiP47727.
KOiK00079.
OrthoDBiEOG7PGDR4.
PhylomeDBiP47727.
TreeFamiTF329359.

Miscellaneous databases

NextBioi608431.
PROiP47727.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of carbonyl reductase from rat testis."
    Wermuth B., Maeder-Heinemann G., Ernst E.
    Eur. J. Biochem. 228:473-479(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: Sprague-Dawley.
    Tissue: Testis.
  2. "Identification of two closely related genes, inducible and noninducible carbonyl reductases in the rat ovary."
    Aoki H., Okada T., Mizutani T., Numata Y., Minegishi T., Miyamoto K.
    Biochem. Biophys. Res. Commun. 230:518-523(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Spleen.
  4. Lubec G., Diao W., Afjehi-Sadat L., Chen W.-Q.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 6-14; 17-24 AND 59-71, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus and Spinal cord.
  5. "A novel 34 kDa glutathione-binding protein in mature rat ovary."
    Toft E., Soederstroem M., Ahlberg M.B., DePierre J.W.
    Biochem. Biophys. Res. Commun. 201:149-154(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 104-138.
  6. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCBR1_RAT
AccessioniPrimary (citable) accession number: P47727
Secondary accession number(s): O08558, Q3KR58
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: April 13, 2016
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.