PRG-1
EC 1.3.1.-
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
D3T-inducible gene 1 protein
DIG-1

Gene name

	Name:	Ptgr1
	Synonyms:	Dig1, Ltb4dh

From

Rattus norvegicus (Rat)

[TaxID: 10116]

Taxonomy

Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.

Protein existence

2: Evidence at transcript level;

References

[1]	NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION BY DITHIOLETHIONE. STRAIN=Fischer 344; DOI=10.1093/carcin/17.11.2297; PubMed=8968041 [NCBI, ExPASy, EBI, Israel, Japan] Primiano T., Gastel J.A., Kensler T.W., Sutter T.R.; "Isolation of cDNAs representing dithiolethione-responsive genes."; Carcinogenesis 17:2297-2303(1996).
[2]	SEQUENCE REVISION. Kensler T.W.; Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Ovary; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).

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.
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.
SUBUNIT: Monomer or homodimer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
INDUCTION: Up-regulated by 1,2-dithiole-3-thione (D3T).
SIMILARITY: Belongs to the NADP-dependent oxidoreductase L4BD family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U66322; AAB88912.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC089775; AAH89775.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_620218.1; -.

UniGene

Rn.10656

3D structure databases

SMR

P97584; 1-329.

ModBase

P97584.

Organism-specific databases

RGD

621195; Ltb4dh.

Gene expression databases

ArrayExpress

P97584; -.

GermOnline

ENSRNOG00000015072; Rattus norvegicus.

Family and domain databases

InterPro

IPR002085; AlcDHase_SF_Zn.
IPR013149; AlcDHase_Zn-bd.
IPR014190; B4_12hDHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

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

PANTHER

PTHR11695; ADH_Sf_Zn; 1.

Pfam

PF00107; ADH_zinc_N; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR02825; B4_12hDH; 1.

BLOCKS

P97584.

Genome annotation databases

Ensembl

ENSRNOG00000015072; Rattus norvegicus. [Contig view]

GeneID

192227; -.

KEGG

rno:192227; -.

Phylogenomic databases

HOVERGEN

P97584; -.

Other

ProtoNet

P97584.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cytoplasm; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 329`	`329`	`Prostaglandin reductase 1.`	`PRO_0000218069`
`NP_BIND`	`149 166`	`18`	`NADP (Potential).`
`COMPBIAS`	`250 257`	`8`	`Pro-rich.`
`BINDING`	`178 178`		`NADP (By similarity).`
`BINDING`	`193 193`		`NADP (By similarity).`
`BINDING`	`217 217`		`NADP (By similarity).`
`BINDING`	`245 245`		`NADP (By similarity).`
`BINDING`	`321 321`		`NADP (By similarity).`

Sequence information

Length: 329 AA [This is the length of the unprocessed precursor]

Molecular weight: 35718 Da [This is the MW of the unprocessed precursor]

CRC64: 8E91165086A05BA9 [This is a checksum on the sequence]

        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

P97584 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools