Q8VDQ1 (PTGR2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Prostaglandin reductase 2
Short name=PRG-2
EC=1.3.1.48

Alternative name(s):
15-oxoprostaglandin 13-reductase
Zinc-binding alcohol dehydrogenase domain-containing protein 1

Gene names

Name:	Ptgr2
Synonyms:	Zadh1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	351 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.3
Catalytic activity	11-alpha-hydroxy-9,15-dioxoprost-5-enoate + NAD(P)+ = (5Z)-(13E)-11-alpha-hydroxy-9,15-dioxoprosta-5,13-dienoate + NAD(P)H. Ref.3
Subunit structure	Monomer. Ref.4
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Widely expressed with highest levels in adipose tissues. Ref.3
Developmental stage	Highly expressed in the late phase of adipocyte differentiation (at protein level). Ref.3
Sequence similarities	Belongs to the NADP-dependent oxidoreductase L4BD family.
Biophysicochemical properties	Kinetic parameters: KM=49.6 µM for 15-keto-PGE2 Ref.3 KM=34.4 µM for 15-keto-PGE1 KM=108.8 µM for 15-keto-PGF2-alpha KM=59.2 µM for 15-keto-PGF2-beta KM=94.6 µM for NADPH Vmax=178.4 µmol/min/mg enzyme for 15-keto-PGE2 Vmax=115.0 µmol/min/mg enzyme for 15-keto-PGE1 Vmax=230.9 µmol/min/mg enzyme for 15-keto-PGF2-alpha Vmax=206.4 µmol/min/mg enzyme for 15-keto-PGF2-beta Vmax=144.7 µmol/min/mg enzyme for NADPH

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	prostaglandin metabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	mitochondrion Inferred from direct assay. Source: MGI
Molecular function	15-oxoprostaglandin 13-oxidase activity Inferred from sequence or structural similarity. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8VDQ1-1)

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.

Isoform 2 (identifier: Q8VDQ1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     314-316: VKE → FLF
     317-351: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 351

351

Prostaglandin reductase 2

PRO_0000218071

Regions

Nucleotide binding

165 – 168

4

NADP

Nucleotide binding

253 – 259

7

NADP

Nucleotide binding

287 – 289

3

NADP

Region

99 – 100

2

Substrate binding By similarity

Region

288 – 290

3

Substrate binding By similarity

Sites

Binding site

192

1

NADP

Binding site

208

1

NADP

Binding site

231

1

NADP

Binding site

337

1

NADP

Natural variations

Alternative sequence

314 – 316

3

VKE → FLF in isoform 2.

VSP_013528

Alternative sequence

317 – 351

35

Missing in isoform 2.

VSP_013529

Experimental info

Mutagenesis

259

1

Y → F: Significant reduction in catalytic efficiency. Ref.3

Sequence conflict

18

1

P → T in BAB32284. Ref.1

Sequence conflict

31

1

P → L in AAH21466. Ref.2

Sequence conflict

81

1

V → I in BAE26315. Ref.1

Sequence conflict

81

1

V → I in AAH21466. Ref.2

Sequence conflict

91

1

T → A in BAE26315. Ref.1

Sequence conflict

91

1

T → A in AAH21466. Ref.2

Sequence conflict

239

1

A → T in BAE26315. Ref.1

Sequence conflict

239

1

A → T in AAH21466. Ref.2

Sequence conflict

260 – 261

2

SN → NK in BAE26315. Ref.1

Sequence conflict

260 – 261

2

SN → NK in AAH21466. Ref.2

Sequence conflict

318

1

M → V in BAE26315. Ref.1

Sequence conflict

318

1

M → V in AAH21466. Ref.2

Secondary structure

1

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351

Helix Strand Turn

Details...

Beta strand

1 – 8

8

Helix

20 – 22

3

Beta strand

23 – 31

9

Beta strand

38 – 48

11

Helix

50 – 56

7

Beta strand

57 – 59

3

Beta strand

75 – 85

11

Beta strand

95 – 110

16

Helix

111 – 113

3

Beta strand

115 – 117

3

Helix

119 – 122

4

Helix

126 – 130

5

Turn

131 – 133

3

Helix

135 – 147

13

Beta strand

157 – 162

6

Helix

168 – 170

3

Helix

171 – 177

7

Beta strand

181 – 189

9

Helix

190 – 199

10

Beta strand

203 – 207

5

Helix

213 – 220

8

Beta strand

225 – 232

8

Helix

234 – 241

8

Beta strand

244 – 252

9

Helix

271 – 279

9

Beta strand

283 – 286

4

Helix

289 – 291

3

Helix

293 – 295

3

Helix

296 – 308

13

Beta strand

316 – 320

5

Helix

322 – 324

3

Helix

325 – 333

9

Beta strand

339 – 344

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 22, 2008. Version 2. Checksum: 2766871577A8022F	FASTA	351	38,015
	10 20 30 40 50 60 MIIQRVVLNS RPGKNGNPVA ENFRVEEFSL PDALNEGQVQ VRTLYLSVDP YMRCKMNEDT 70 80 90 100 110 120 GTDYLAPWQL AQVADGGGIG VVEESKHQKL TKGDFVTSFY WPWQTKAILD GNGLEKVDPQ 130 140 150 160 170 180 LVDGHLSYFL GAIGMPGLTS LIGVQEKGHI SAGSNQTMVV SGAAGACGSL AGQIGHLLGC 190 200 210 220 230 240 SRVVGICGTQ EKCLFLTSEL GFDAAVNYKT GNVAEQLREA CPGGVDVYFD NVGGDISNAV 250 260 270 280 290 300 ISQMNENSHI ILCGQISQYS NDVPYPPPLP PAVEAIRKER NITRERFTVL NYKDKFEPGI 310 320 330 340 350 LQLSQWFKEG KLKVKETMAK GLENMGVAFQ SMMTGGNVGK QIVCISEDSS L
	Isoform 2 [UniParc]. Checksum: 7699BA248C3E09D0	FASTA	316	34,449
	10 20 30 40 50 60 MIIQRVVLNS RPGKNGNPVA ENFRVEEFSL PDALNEGQVQ VRTLYLSVDP YMRCKMNEDT 70 80 90 100 110 120 GTDYLAPWQL AQVADGGGIG VVEESKHQKL TKGDFVTSFY WPWQTKAILD GNGLEKVDPQ 130 140 150 160 170 180 LVDGHLSYFL GAIGMPGLTS LIGVQEKGHI SAGSNQTMVV SGAAGACGSL AGQIGHLLGC 190 200 210 220 230 240 SRVVGICGTQ EKCLFLTSEL GFDAAVNYKT GNVAEQLREA CPGGVDVYFD NVGGDISNAV 250 260 270 280 290 300 ISQMNENSHI ILCGQISQYS NDVPYPPPLP PAVEAIRKER NITRERFTVL NYKDKFEPGI 310 LQLSQWFKEG KLKFLF

References

	« Hide 'large scale' referencesShow 'large scale' 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. , 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] (ISOFORMS 1 AND 2). Strain: C57BL/6J. Tissue: Cerebellum, Embryonic heart, Mammary gland and Medulla oblongata.
[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] (ISOFORM 1). Strain: Czech II. Tissue: Mammary tumor.
[3]	"Identification of a novel prostaglandin reductase reveals the involvement of prostaglandin E2 catabolism in regulation of peroxisome proliferator-activated receptor gamma activation." Chou W.-L., Chuang L.-M., Chou C.-C., Wang A.H.-J., Lawson J.A., FitzGerald G.A., Chang Z.-F. J. Biol. Chem. 282:18162-18172(2007) [PubMed: 17449869] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF TYR-259.
[4]	"Crystal structure of a putative NADPH-dependent oxidoreductase (GI: 18204011) from mouse at 2.10 A resolution." Levin I., Schwarzenbacher R., McMullan D., Abdubek P., Ambing E., Biorac T., Cambell J., Canaves J.M., Chiu H.-J., Dai X., Deacon A.M., DiDonato M., Elsliger M.-A., Godzik A., Grittini C., Grzechnik S.K., Hampton E., Jaroszewski L. , Karlak C., Klock H.E., Koesema E., Kreusch A., Kuhn P., Lesley S.A., McPhillips T.M., Miller M.D., Morse A., Moy K., Ouyang J., Page R., Quijano K., Reyes R., Robb A., Sims E., Spraggon G., Stevens R.C., van den Bedem H., Velasquez J., Vincent J., von Delft F., Wang X., West B., Wolf G., Xu Q., Hodgson K.O., Wooley J., Wilson I.A. Proteins 56:629-633(2004) [PubMed: 15229897] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SUBUNIT.
[5]	"Structural basis for catalytic and inhibitory mechanisms of human prostaglandin reductase PTGR2." Wu Y.H., Ko T.P., Guo R.T., Hu S.M., Chuang L.M., Wang A.H. Structure 16:1714-1723(2008) [PubMed: 19000823] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NADPH.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK036168 mRNA. Translation: BAC29329.1.
AK021033 mRNA. Translation: BAB32284.1.
AK145232 mRNA. Translation: BAE26315.1.
AK159932 mRNA. Translation: BAE35493.1.
AK168895 mRNA. Translation: BAE40712.1.
BC021466 mRNA. Translation: AAH21466.1.

IPI

IPI00134334.
IPI00556775.

RefSeq

NP_001239554.1. NM_001252625.1.
NP_084156.2. NM_029880.3.

UniGene

Mm.246127.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VJ1	X-ray	2.10	A	1-351	[»]
2ZB3	X-ray	2.00	A	1-351	[»]

ProteinModelPortal

Q8VDQ1.

SMR

Q8VDQ1. Positions 2-346.

ModBase

Search...

PTM databases

PhosphoSite

Q8VDQ1.

Proteomic databases

PRIDE

Q8VDQ1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000110290; ENSMUSP00000105919; ENSMUSG00000072946.
ENSMUST00000123614; ENSMUSP00000115704; ENSMUSG00000072946.
ENSMUST00000146377; ENSMUSP00000119981; ENSMUSG00000072946.
ENSMUST00000147363; ENSMUSP00000114766; ENSMUSG00000072946.

GeneID

77219.

KEGG

mmu:77219.

UCSC

uc007oep.1. mouse.

Organism-specific databases

CTD

145482.

MGI

MGI:1916372. Ptgr2.

Phylogenomic databases

eggNOG

roNOG16229.

GeneTree

ENSGT00390000009335.

HOGENOM

HBG753318.

HOVERGEN

HBG055024.

InParanoid

Q8VDQ1.

OMA

HELCPAG.

OrthoDB

EOG4S4PGG.

PhylomeDB

Q8VDQ1.

Gene expression databases

ArrayExpress

Q8VDQ1.

Bgee

Q8VDQ1.

Genevestigator

Q8VDQ1.

Family and domain databases

InterPro

IPR013149. ADH_C.
IPR002085. ADH_SF_Zn-type.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

KO

K13949.

PANTHER

PTHR11695. ADH_Sf_Zn. 1 hit.

Pfam

PF00107. ADH_zinc_N. 1 hit.
[Graphical view]

SUPFAM

SSF50129. GroES_like. 1 hit.

ProtoNet

Search...

Other

NextBio

346608.

SOURCE

Search...

Entry information

Entry name

PTGR2_MOUSE

Accession

Primary (citable) accession number: Q8VDQ1
Secondary accession number(s): Q3TG36 , Q3ULY3, Q8BZA2, Q9D1W8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	July 22, 2008
Last modified:	January 25, 2012
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program