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Protein

Carbonyl reductase [NADPH] 1

Gene

CBR1

Organism
Sus scrofa (Pig)
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 similarity1 Publication

Catalytic activityi

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

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 – 34NADP1 PublicationAdd BLAST25
Nucleotide bindingi63 – 64NADPBy similarity2
Nucleotide bindingi194 – 198NADPBy similarity5
Nucleotide bindingi231 – 233NADPBy similarity3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BRENDAi1.1.1.184. 6170.
1.1.1.189. 6170.

Chemistry databases

SwissLipidsiSLP:000001473.

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, CRN
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000546042 – 289Carbonyl reductase [NADPH] 1Add BLAST288

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei2PhosphoserineBy similarity1
Modified residuei162PhosphothreonineBy similarity1
Modified residuei239N6-1-carboxyethyl lysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PeptideAtlasiQ28960.
PRIDEiQ28960.

Expressioni

Developmental stagei

Highly expressed in testis from newborns. After 30 days the levels are markedly decreased.1 Publication

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1289
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 12Combined sources6
Helixi16 – 28Combined sources13
Beta strandi30 – 39Combined sources10
Helixi40 – 51Combined sources12
Turni52 – 54Combined sources3
Beta strandi58 – 61Combined sources4
Helixi67 – 81Combined sources15
Beta strandi82 – 89Combined sources8
Helixi103 – 114Combined sources12
Helixi116 – 125Combined sources10
Helixi126 – 128Combined sources3
Beta strandi129 – 138Combined sources10
Helixi142 – 149Combined sources8
Helixi152 – 159Combined sources8
Helixi165 – 180Combined sources16
Turni184 – 188Combined sources5
Helixi193 – 215Combined sources23
Helixi217 – 219Combined sources3
Beta strandi222 – 227Combined sources6
Beta strandi230 – 233Combined sources4
Turni234 – 236Combined sources3
Helixi244 – 247Combined sources4
Helixi249 – 255Combined sources7
Beta strandi268 – 270Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1N5DX-ray2.30A2-289[»]
ProteinModelPortaliQ28960.
SMRiQ28960.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ28960.

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG001909.
InParanoidiQ28960.
KOiK00079.

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.

Q28960-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSNTRVALV TGANKGIGFA IVRDLCRQFA GDVVLTARDV ARGQAAVKQL
60 70 80 90 100
QAEGLSPRFH QLDIIDLQSI RALCDFLRKE YGGLDVLVNN AAIAFQLDNP
110 120 130 140 150
TPFHIQAELT MKTNFMGTRN VCTELLPLIK PQGRVVNVSS TEGVRALNEC
160 170 180 190 200
SPELQQKFKS ETITEEELVG LMNKFVEDTK NGVHRKEGWS DSTYGVTKIG
210 220 230 240 250
VSVLSRIYAR KLREQRAGDK ILLNACCPGW VRTDMGGPKA PKSPEVGAET
260 270 280
PVYLALLPSD AEGPHGQFVT DKKVVEWGVP PESYPWVNA
Length:289
Mass (Da):31,693
Last modified:January 23, 2007 - v3
Checksum:i47A587FFE3F682C2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80709 mRNA. Translation: AAA30980.1.
PIRiA42912.
RefSeqiNP_999238.1. NM_214073.1.
UniGeneiSsc.55707.

Genome annotation databases

GeneIDi397143.
KEGGissc:397143.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80709 mRNA. Translation: AAA30980.1.
PIRiA42912.
RefSeqiNP_999238.1. NM_214073.1.
UniGeneiSsc.55707.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1N5DX-ray2.30A2-289[»]
ProteinModelPortaliQ28960.
SMRiQ28960.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

SwissLipidsiSLP:000001473.

Proteomic databases

PeptideAtlasiQ28960.
PRIDEiQ28960.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397143.
KEGGissc:397143.

Organism-specific databases

CTDi873.

Phylogenomic databases

HOVERGENiHBG001909.
InParanoidiQ28960.
KOiK00079.

Enzyme and pathway databases

BRENDAi1.1.1.184. 6170.
1.1.1.189. 6170.

Miscellaneous databases

EvolutionaryTraceiQ28960.

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_PIG
AccessioniPrimary (citable) accession number: Q28960
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 99 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.