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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)DescriptionActionsGraphical viewLength
Binding sitei90NADP; via carbonyl oxygenBy similarity1
Binding sitei106GlutathioneBy similarity1
Binding sitei140SubstrateBy similarity1
Active sitei194Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 34NADPBy similarityAdd BLAST25
Nucleotide bindingi63 – 64NADPBy similarity2
Nucleotide bindingi194 – 198NADPBy similarity5
Nucleotide bindingi231 – 233NADPBy similarity3

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000546072 – 277Carbonyl reductase [NADPH] 1Add BLAST276

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei2PhosphoserineCombined sources1
Modified residuei162PhosphothreonineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP47727.
PRIDEiP47727.

PTM databases

iPTMnetiP47727.
PhosphoSitePlusiP47727.

Expressioni

Gene expression databases

BgeeiENSRNOG00000047848.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi247902. 1 interactor.
IntActiP47727. 1 interactor.
STRINGi10116.ENSRNOP00000064050.

Structurei

3D structure databases

ProteinModelPortaliP47727.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni95 – 97Glutathione bindingBy similarity3
Regioni193 – 194Glutathione bindingBy similarity2

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1208. Eukaryota.
COG1028. LUCA.
HOVERGENiHBG001909.
InParanoidiP47727.
KOiK00079.
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)DescriptionActionsGraphical viewLength
Sequence conflicti22V → T AA sequence (Ref. 4) Curated1
Sequence conflicti135V → D AA sequence (PubMed:8198567).Curated1
Sequence conflicti138V → H AA sequence (PubMed:8198567).Curated1
Sequence conflicti141 – 144SVSL → GMSR in BAA19007 (PubMed:9015353).Curated4
Sequence conflicti176I → V in AAI05894 (PubMed:15489334).Curated1
Sequence conflicti213N → T in AAI05894 (PubMed:15489334).Curated1
Sequence conflicti236A → T in BAA19007 (PubMed:9015353).Curated1
Sequence conflicti239K → E in BAA19007 (PubMed:9015353).Curated1

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247902. 1 interactor.
IntActiP47727. 1 interactor.
STRINGi10116.ENSRNOP00000064050.

PTM databases

iPTMnetiP47727.
PhosphoSitePlusiP47727.

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.
PhylomeDBiP47727.
TreeFamiTF329359.

Miscellaneous databases

PROiP47727.

Gene expression databases

BgeeiENSRNOG00000047848.

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...

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: November 2, 2016
This is version 133 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.