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Protein

Prostaglandin reductase 2

Gene

Ptgr2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Functions as 15-oxo-prostaglandin 13-reductase and acts on 15-keto-PGE1, 15-keto-PGE2, 15-keto-PGE1-alpha and 15-keto-PGE2-alpha with highest activity towards 15-keto-PGE2. Overexpression represses transcriptional activity of PPARG and inhibits adipocyte differentiation (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei192 – 1921NADPBy similarity
Binding sitei208 – 2081NADPBy similarity
Binding sitei231 – 2311NADPBy similarity
Binding sitei337 – 3371NADPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi165 – 1684NADPBy similarity
Nucleotide bindingi253 – 2597NADPBy similarity
Nucleotide bindingi287 – 2893NADPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Prostaglandin reductase 2By similarity (EC:1.3.1.48By similarity)
Short name:
PRG-2By similarity
Alternative name(s):
15-oxoprostaglandin 13-reductaseBy similarity
Zinc-binding alcohol dehydrogenase domain-containing protein 1
Gene namesi
Name:Ptgr2By similarity
Synonyms:Zadh1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi1310518. Ptgr2.

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 351351Prostaglandin reductase 2PRO_0000343830Add
BLAST

Proteomic databases

PaxDbiQ5BK81.
PRIDEiQ5BK81.

Expressioni

Gene expression databases

GenevisibleiQ5BK81. RN.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000055851.

Structurei

3D structure databases

ProteinModelPortaliQ5BK81.
SMRiQ5BK81. Positions 1-350.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni99 – 1002Substrate bindingBy similarity
Regioni288 – 2903Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the NADP-dependent oxidoreductase L4BD family.Sequence analysis

Phylogenomic databases

eggNOGiKOG1196. Eukaryota.
COG2130. LUCA.
GeneTreeiENSGT00390000009335.
HOGENOMiHOG000294663.
HOVERGENiHBG055024.
InParanoidiQ5BK81.
KOiK13949.
OMAiESKHTNF.
OrthoDBiEOG7B31N5.
TreeFamiTF324201.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR002085. ADH_SF_Zn-type.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1Curated (identifier: Q5BK81-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MIIQRVVLDS RPGKNGNPVA ENFRVEEVSL PDTINEGQVR VRTLYLSVDP
60 70 80 90 100
YMRCKMNEET GADYLAPWQL AQVADGGGLG VIEESKHQKL AKGDFVTSFY
110 120 130 140 150
WPWQTKAILD GNGLEKVDPQ LVDGHLSYFL GAIGMPGLTS LIGVQEKGHV
160 170 180 190 200
SAGSNQTMVV SGAAGACGSL AGQIGHLLGC SRVVGICGTH EKCLFLTSEL
210 220 230 240 250
GFDAAVNYKT GNVAEQLREA CPDGVDVYFD NVGGDISNAV ISQMNQNSHI
260 270 280 290 300
ILCGQISQYN KDVPYPPPLP PAVEAIQKER NITRERFMVL NYKDRFEPGI
310 320 330 340 350
LQLSQWFKEG KLKIKETVAN GLENMGVAFQ SMMTGGNIGK QIVRISEDSS

P
Note: Gene prediction based on similarity to mouse ortholog.Curated
Length:351
Mass (Da):38,136
Last modified:July 22, 2008 - v2
Checksum:iF94578C4E45B47C6
GO
Isoform 21 Publication (identifier: Q5BK81-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     244-313: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:281
Mass (Da):29,897
Checksum:iF780BA7811AAAE7E
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei244 – 31370Missing in isoform 2. 1 PublicationVSP_052852Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03048578 Genomic DNA. No translation available.
AABR03050041 Genomic DNA. No translation available.
BC091173 mRNA. Translation: AAH91173.1.
RefSeqiNP_001015009.1. NM_001015009.1. [Q5BK81-2]
XP_006240388.1. XM_006240326.1. [Q5BK81-1]
XP_006240389.1. XM_006240327.1. [Q5BK81-1]
XP_006240390.1. XM_006240328.2. [Q5BK81-1]
UniGeneiRn.203285.

Genome annotation databases

EnsembliENSRNOT00000058095; ENSRNOP00000054903; ENSRNOG00000038166. [Q5BK81-2]
ENSRNOT00000059073; ENSRNOP00000055851; ENSRNOG00000038166. [Q5BK81-1]
GeneIDi299194.
KEGGirno:299194.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03048578 Genomic DNA. No translation available.
AABR03050041 Genomic DNA. No translation available.
BC091173 mRNA. Translation: AAH91173.1.
RefSeqiNP_001015009.1. NM_001015009.1. [Q5BK81-2]
XP_006240388.1. XM_006240326.1. [Q5BK81-1]
XP_006240389.1. XM_006240327.1. [Q5BK81-1]
XP_006240390.1. XM_006240328.2. [Q5BK81-1]
UniGeneiRn.203285.

3D structure databases

ProteinModelPortaliQ5BK81.
SMRiQ5BK81. Positions 1-350.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000055851.

Proteomic databases

PaxDbiQ5BK81.
PRIDEiQ5BK81.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000058095; ENSRNOP00000054903; ENSRNOG00000038166. [Q5BK81-2]
ENSRNOT00000059073; ENSRNOP00000055851; ENSRNOG00000038166. [Q5BK81-1]
GeneIDi299194.
KEGGirno:299194.

Organism-specific databases

CTDi145482.
RGDi1310518. Ptgr2.

Phylogenomic databases

eggNOGiKOG1196. Eukaryota.
COG2130. LUCA.
GeneTreeiENSGT00390000009335.
HOGENOMiHOG000294663.
HOVERGENiHBG055024.
InParanoidiQ5BK81.
KOiK13949.
OMAiESKHTNF.
OrthoDBiEOG7B31N5.
TreeFamiTF324201.

Miscellaneous databases

PROiQ5BK81.

Gene expression databases

GenevisibleiQ5BK81. RN.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR002085. ADH_SF_Zn-type.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway1 Publication.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: Brown NorwayImported.
    Tissue: HeartImported.

Entry informationi

Entry nameiPTGR2_RAT
AccessioniPrimary (citable) accession number: Q5BK81
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: July 22, 2008
Last modified: June 8, 2016
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.