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Reviewed, UniProtKB/Swiss-Prot Q91YR9 (PTGR1_MOUSE)

Last modified June 16, 2009. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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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
Gene names
Name: Ptgr1
Synonyms: Ltb4dh
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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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.

Sequence similarities

Belongs to the NADP-dependent oxidoreductase L4BD family.

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Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 329329Prostaglandin reductase 1
PRO_0000218066

Regions

Nucleotide binding149 – 16618NADP Potential

Sites

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

Experimental info

Sequence conflict2981C → Y in AAH14865. Ref.2
Sequence conflict3011Y → H in AAH14865. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
Q91YR9-1 [UniParc].

Last modified August 16, 2005. Version 2.
Checksum: FD0CA4682DB493D8

FASTA32935,560
        10         20         30         40         50         60 
MVQAKSWTLK KHFEGFPTDG NFELKTTELP PLNNGEVLLE ALFLSVDPYM RVAAKKLKEG 

        70         80         90        100        110        120 
DRMMGEQVAR VVESKNSAFP KGTIVAALLG WTSHSISDGN GLTKLPVEWP DKLPLSLALG 

       130        140        150        160        170        180 
TVGMPGLTAY FGLLDICGVK GGETVMVSAA AGAVGSVVGQ IAKLKGCKVV GTAGSDEKVA 

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

       250        260        270        280        290        300 
AISQYNRTGP CPQGPAPEVV IYQQLRMEGF IVNRWQGEVR QKALTELMNW VSEGKVQCHE 

       310        320 
YVTEGFEKMP AAFMGMLKGE NLGKTIVKA

« Hide

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References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo, Liver, Testis and Urinary bladder.
[2]"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].
Strain: FVB/N.
Tissue: Mammary tumor.

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Cross-references

Sequence databases

AK010888 mRNA. Translation: BAB27248.1.
AK011962 mRNA. Translation: BAB27941.1.
AK035425 mRNA. Translation: BAC29060.1.
AK134440 mRNA. Translation: BAE22145.1.
AK166835 mRNA. Translation: BAE39057.1.
BC014865 mRNA. Translation: AAH14865.1.
IPIIPI00131887.
RefSeqNP_080244.1.
UniGeneMm.34497

3D structure databases

HSSPHSSP built from PDB template 1PQW based on UniProtKB P96202.
SMRQ91YR9. Positions 1-329.
ModBaseSearch...

PTM databases

PhosphoSiteQ91YR9.

2-D gel databases

REPRODUCTION-2DPAGEQ91YR9.

Proteomic databases

PRIDEQ91YR9.

Genome annotation databases

EnsemblENSMUSG00000028378. Mus musculus. [Contig view]
GeneID67103.
KEGGmmu:67103.

Organism-specific databases

MGIMGI:1914353. Ptgr1.

Phylogenomic databases

HOGENOMQ91YR9.
HOVERGENQ91YR9.
OMAQ91YR9. WQGEVRQ.

Enzyme and pathway databases

BRENDA1.3.1.48. 244.
1.3.1.74. 244.

Gene expression databases

ArrayExpressQ91YR9.
BgeeQ91YR9.
GermOnlineENSMUSG00000028378. Mus musculus.

Family and domain databases

InterProIPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR014190. B4_12hDH.
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

NextBio323584.
SOURCESearch...

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Entry information

Entry namePTGR1_MOUSE
AccessionPrimary (citable) accession number: Q91YR9
Secondary accession number(s): Q3TKT6, Q9CPS1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: August 16, 2005
Last modified: June 16, 2009
This is version 60 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

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