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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)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 – 3425NADP1 PublicationAdd
BLAST
Nucleotide bindingi63 – 642NADPBy similarity
Nucleotide bindingi194 – 1985NADPBy similarity
Nucleotide bindingi231 – 2333NADPBy similarity

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

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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 289288Carbonyl reductase [NADPH] 1PRO_0000054604Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei162 – 1621PhosphothreonineBy similarity
Modified residuei239 – 2391N6-1-carboxyethyl lysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

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

1
289
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 126Combined sources
Helixi16 – 2813Combined sources
Beta strandi30 – 3910Combined sources
Helixi40 – 5112Combined sources
Turni52 – 543Combined sources
Beta strandi58 – 614Combined sources
Helixi67 – 8115Combined sources
Beta strandi82 – 898Combined sources
Helixi103 – 11412Combined sources
Helixi116 – 12510Combined sources
Helixi126 – 1283Combined sources
Beta strandi129 – 13810Combined sources
Helixi142 – 1498Combined sources
Helixi152 – 1598Combined sources
Helixi165 – 18016Combined sources
Turni184 – 1885Combined sources
Helixi193 – 21523Combined sources
Helixi217 – 2193Combined sources
Beta strandi222 – 2276Combined sources
Beta strandi230 – 2334Combined sources
Turni234 – 2363Combined sources
Helixi244 – 2474Combined sources
Helixi249 – 2557Combined sources
Beta strandi268 – 2703Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N5DX-ray2.30A2-289[»]
ProteinModelPortaliQ28960.
SMRiQ28960. Positions 2-289.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ28960.

Family & Domainsi

Region

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

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1N5DX-ray2.30A2-289[»]
ProteinModelPortaliQ28960.
SMRiQ28960. Positions 2-289.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

SwissLipidsiSLP:000001473.

Proteomic databases

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...

Publicationsi

  1. "Pig testicular 20-beta-hydroxysteroid dehydrogenase exhibits carbonyl reductase-like structure and activity: cDNA cloning of pig testicular 2-beta-hydroxysteroid dehydrogenase."
    Tanaka M., Ohno S., Nakajin S., Shinoda M., Nagahama Y.
    J. Biol. Chem. 267:13451-13455(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 80-111; 113-127; 131-152; 160-174; 187-211; 221-239 AND 243-272, FUNCTION, DEVELOPMENTAL STAGE.
  2. "Porcine carbonyl reductase. Structural basis for a functional monomer in short chain dehydrogenases/reductases."
    Ghosh D., Sawicki M., Pletnev V., Erman M., Ohno S., Nakajin S., Duax W.L.
    J. Biol. Chem. 276:18457-18463(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH NADP, SUBUNIT STRUCTURE.

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: April 13, 2016
This is version 96 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.