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P47727 (CBR1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Cbr1
Synonyms:Cbr
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length277 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 By similarity.

Catalytic activity

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.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processdrug metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

ovulation from ovarian follicle

Inferred from expression pattern PubMed 10642578. Source: RGD

peptidyl-lysine modification

Non-traceable author statement PubMed 10926830. Source: RGD

phylloquinone catabolic process

Inferred from direct assay PubMed 16359670. Source: RGD

response to gonadotropin stimulus

Inferred from expression pattern PubMed 12444039. Source: RGD

response to lipopolysaccharide

Inferred from expression pattern PubMed 12399253. Source: RGD

response to testosterone stimulus

Inferred from expression pattern PubMed 16457595. Source: RGD

vitamin K metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytosol

Traceable author statement Ref.1. Source: RGD

microvillus

Inferred from direct assay PubMed 16457595. Source: RGD

nucleus

Inferred from direct assay PubMed 16457595. Source: RGD

plasma membrane

Inferred from direct assay PubMed 16457595. Source: RGD

   Molecular_function15-hydroxyprostaglandin dehydrogenase (NADP+) activity

Inferred from electronic annotation. Source: EC

carbonyl reductase (NADPH) activity

Inferred from sequence or structural similarity. Source: UniProtKB

nucleotide binding

Inferred from electronic annotation. Source: InterPro

prostaglandin-E2 9-reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 277276Carbonyl reductase [NADPH] 1
PRO_0000054607

Regions

Nucleotide binding10 – 3425NADP By similarity
Nucleotide binding63 – 642NADP By similarity
Nucleotide binding194 – 1985NADP By similarity
Nucleotide binding231 – 2333NADP By similarity
Region95 – 973Glutathione binding By similarity
Region193 – 1942Glutathione binding By similarity

Sites

Active site1941Proton acceptor By similarity
Binding site901NADP; via carbonyl oxygen By similarity
Binding site1061Glutathione By similarity
Binding site1401Substrate By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity

Experimental info

Sequence conflict221V → T AA sequence Ref.4
Sequence conflict1351V → D AA sequence Ref.5
Sequence conflict1381V → H AA sequence Ref.5
Sequence conflict141 – 1444SVSL → GMSR in BAA19007. Ref.2
Sequence conflict1761I → V in AAI05894. Ref.3
Sequence conflict2131N → T in AAI05894. Ref.3
Sequence conflict2361A → T in BAA19007. Ref.2
Sequence conflict2391K → E in BAA19007. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P47727 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: B0F4738C40011B5B

FASTA27730,578
        10         20         30         40         50         60 
MSSDRPVALV TGANKGIGFA IVRDLCRKFL GDVVLTARDE SRGHEAVKQL QTEGLSPRFH 

        70         80         90        100        110        120 
QLDIDNPQSI RALRDFLLQE YGGLNVLVNN AGIAFKVVDP TPFHIQAEVT MKTNFFGTQD 

       130        140        150        160        170        180 
VCKELLPIIK PQGRVVNVSS SVSLRALKSC SPELQQKFRS ETITEEELVG LMNKFIEDAK 

       190        200        210        220        230        240 
KGVHAKEGWP NSAYGVTKIG VTVLSRIYAR KLNEERREDK ILLNACCPGW VRTDMAGPKA 

       250        260        270 
TKSPEEGAET PVYLALLPPG AEGPHGQFVQ DKKVEPW

« Hide

References

« Hide 'large scale' references
[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, 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X84349 mRNA. Translation: CAA59088.1.
X95986 Genomic DNA. Translation: CAA65230.1.
D89069 mRNA. Translation: BAA19007.1.
BC105893 mRNA. Translation: AAI05894.1.
IPIIPI00331856.
PIRJC5284. S68982.
RefSeqNP_062043.1. NM_019170.2.
XP_003751064.1. XM_003751016.1.
XP_003751065.1. XM_003751017.1.
XP_003752521.1. XM_003752473.1.
UniGeneRn.3425.

3D structure databases

ProteinModelPortalP47727.
SMRP47727. Positions 7-277.
ModBaseSearch...

PTM databases

PhosphoSiteP47727.

Proteomic databases

PaxDbP47727.
PRIDEP47727.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000041838; ENSRNOP00000051107; ENSRNOG00000049693.
ENSRNOT00000042283; ENSRNOP00000043385; ENSRNOG00000047848.
GeneID100360507.
100912203.
29224.
KEGGrno:100360507.
rno:100912203.
rno:29224.
UCSCRGD:2286. rat.

Organism-specific databases

CTD873.
RGD2286. Cbr1.

Phylogenomic databases

eggNOGCOG1028.
GeneTreeENSGT00510000046499.
HOVERGENHBG001909.
InParanoidP47727.
KOK00079.
OrthoDBEOG4BP1CB.

Gene expression databases

ArrayExpressP47727.
GenevestigatorP47727.
GermOnlineENSRNOG00000032165. Rattus norvegicus.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio608431.

Entry information

Entry nameCBR1_RAT
AccessionPrimary (citable) accession number: P47727
Secondary accession number(s): O08558, Q3KR58
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents