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Reviewed, UniProtKB/Swiss-Prot P97584 (PTGR1_RAT)

Last modified February 9, 2010. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Prostaglandin reductase 1
      Short name=PRG-1
    EC=1.3.1.-
Alternative name(s):
    NADP-dependent leukotriene B4 12-hydroxydehydrogenase
    EC=1.3.1.74
    15-oxoprostaglandin 13-reductase
    EC=1.3.1.48
    Dithiolethione-inducible gene 1 protein
      Short name=D3T-inducible gene 1 protein
      Short name=DIG-1
Gene names
Name: Ptgr1
Synonyms: Dig1, Ltb4dh
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Functions as 15-oxo-prostaglandin 13-reductase and acts on 15-oxo-PGE1, 15-oxo-PGE2 and 15-oxo-PGE2-alpha. Has no activity towards PGE1, PGE2 and PGE2-alpha. Catalyzes the conversion of leukotriene B4 into its biologically less active metabolite, 12-oxo-leukotriene B4. This is an initial and key step of metabolic inactivation of leukotriene B4 By similarity.

Catalytic activity

n-alkanal + NAD(P)+ = alk-2-enal + NAD(P)H.

11-alpha-hydroxy-9,15-dioxoprost-5-enoate + NAD(P)+ = (5Z)-(13E)-11-alpha-hydroxy-9,15-dioxoprosta-5,13-dienoate + NAD(P)H.

Subunit structure

Monomer or homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Induction

Up-regulated by 1,2-dithiole-3-thione (D3T). Ref.1

Sequence similarities

Belongs to the NADP-dependent oxidoreductase L4BD family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

response to toxin Ref.1

Inferred from expression pattern. Source: RGD

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function15-oxoprostaglandin 13-oxidase activity

Inferred from electronic annotation. Source: EC

2-alkenal reductase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 329329Prostaglandin reductase 1
PRO_0000218069

Regions

Nucleotide binding149 – 16618NADP Potential
Compositional bias250 – 2578Pro-rich

Sites

Binding site1781NADP By similarity
Binding site1931NADP By similarity
Binding site2171NADP By similarity
Binding site2451NADP By similarity
Binding site3211NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
P97584-1 [UniParc].

Last modified May 1, 2000. Version 3.
Checksum: 8E91165086A05BA9

FASTA32935,718
        10         20         30         40         50         60 
MVQAKTWTLK KHFEGFPTDS NFELRTTELP PLNNGEVLLE ALFLSVDPYM RVAAKKLKEG 

        70         80         90        100        110        120 
DSMMGEQVAR VVESKNSAFP TGTIVVALLG WTSHSISDGN GLRKLPAEWP DKLPLSLALG 

       130        140        150        160        170        180 
TVGMPGLTAY FGLLDICGLK GGETVLVNAA AGAVGSVVGQ IAKLKGCKVV GTAGSDEKVA 

       190        200        210        220        230        240 
YLKKLGFDVA FNYKTVKSLE EALRTASPDG YDCYFDNVGG EFSNTVILQM KTFGRIAICG 

       250        260        270        280        290        300 
AISQYNRTGP CPPGPSPEVI IYQQLRMEGF IVTRWQGEVR QKALTDLMNW VSEGKIRYHE 

       310        320 
YITEGFEKMP AAFMGMLKGD NLGKTIVKA 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of cDNAs representing dithiolethione-responsive genes."
Primiano T., Gastel J.A., Kensler T.W., Sutter T.R.
Carcinogenesis 17:2297-2303(1996) [PubMed: 8968041] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION BY DITHIOLETHIONE.
Strain: Fischer 344.
[2]Kensler T.W.
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Ovary.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U66322 mRNA. Translation: AAB88912.2.
BC089775 mRNA. Translation: AAH89775.1.
IPIIPI00203443.
RefSeqNP_620218.1.
UniGeneRn.10656

3D structure databases

SMRP97584. Positions 1-329.
ModBaseSearch...

Proteomic databases

PRIDEP97584.

Genome annotation databases

EnsemblENSRNOT00000020335; ENSRNOP00000020335; ENSRNOG00000015072; Rattus norvegicus. [Genome view]
GeneID192227.
KEGGrno:192227.
UCSCNM_138863. rat.

Organism-specific databases

CTD192227.
RGD621195. Ltb4dh.

Phylogenomic databases

eggNOGroNOG16469.
HOVERGENP97584.
InParanoidP97584.
PhylomeDBP97584.

Enzyme and pathway databases

BRENDA1.3.1.48. 248.
1.3.1.74. 248.

Gene expression databases

ArrayExpressP97584.
GenevestigatorP97584.
GermOnlineENSRNOG00000015072. Rattus norvegicus.

Family and domain databases

InterProIPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR014190. B4_12hDH.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF00107. ADH_zinc_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR02825. B4_12hDH. 1 hit.
ProtoNetSearch...

Other Resources

NextBio622836.

Entry information

Entry namePTGR1_RAT
AccessionPrimary (citable) accession number: P97584
Secondary accession number(s): Q5EBD3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: May 1, 2000
Last modified: February 9, 2010
This is version 68 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents