Prostaglandin reductase 1

Details

Name
Prostaglandin reductase 1
Kind
protein
Synonyms
  • 15-oxoprostaglandin 13-reductase
  • D3T-inducible gene 1 protein
  • DIG-1
  • Dithiolethione-inducible gene 1 protein
  • Leukotriene B4 12-hydroxydehydrogenase
  • LTB4DH
  • NAD(P)H-dependent alkenal/one oxidoreductase
  • PRG-1
Gene Name
PTGR1
UniProtKB Entry
Q14914Swiss-Prot
Organism
Humans
NCBI Taxonomy ID
9606
Amino acid sequence
>lcl|BSEQ0007280|Prostaglandin reductase 1
MVRTKTWTLKKHFVGYPTNSDFELKTAELPPLKNGEVLLEALFLTVDPYMRVAAKRLKEG
DTMMGQQVAKVVESKNVALPKGTIVLASPGWTTHSISDGKDLEKLLTEWPDTIPLSLALG
TVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAVGSDEKVA
YLQKLGFDVVFNYKTVESLEETLKKASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAICG
AISTYNRTGPLPPGPPPEIVIYQELRMEAFVVYRWQGDARQKALKDLLKWVLEGKIQYKE
YIIEGFENMPAAFMGMLKGDNLGKTIVKA
Number of residues
329
Molecular Weight
35869.64
Theoretical pI
8.53
GO Classification
Functions
13-lipoxin reductase activity / 2-alkenal reductase (NADPH) activity / leukotriene B4 12-hydroxy dehydrogenase activity
Processes
leukotriene B4 metabolic process / lipoxin A4 metabolic process / prostaglandin metabolic process
General Function
NAD(P)H-dependent oxidoreductase involved in metabolic inactivation of pro- and anti-inflammatory eicosanoids: prostaglandins (PG), leukotrienes (LT) and lipoxins (LX) (PubMed:25619643). Catalyzes with high efficiency the reduction of the 13,14 double bond of 15-oxoPGs, including 15-oxo-PGE1, 15-oxo-PGE2, 15-oxo-PGF1-alpha and 15-oxo-PGF2-alpha (PubMed:25619643). Catalyzes with lower efficiency the oxidation of the hydroxyl group at C12 of LTB4 and its derivatives, converting them into biologically less active 12-oxo-LTB4 metabolites (By similarity) (PubMed:25619643). Reduces 15-oxo-LXA4 to 13,14 dihydro-15-oxo-LXA4, enhancing neutrophil recruitment at the inflammatory site (By similarity). May play a role in metabolic detoxification of alkenals and ketones. Reduces alpha,beta-unsaturated alkenals and ketones, particularly those with medium-chain length, showing highest affinity toward (2E)-decenal and (3E)-3-nonen-2-one (PubMed:25619643). May inactivate 4-hydroxy-2-nonenal, a cytotoxic lipid constituent of oxidized low-density lipoprotein particles (By similarity)
Specific Function
13-lipoxin reductase activity
Pfam Domain Function
Signal Regions
Not Available
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0012647|Prostaglandin reductase 1 (PTGR1)
ATGGTTCGTACTAAGACATGGACCCTGAAGAAGCACTTTGTTGGCTATCCTACTAATAGT
GACTTTGAGTTGAAGACAGCTGAGCTCCCACCCTTAAAAAATGGAGAGGTCCTGCTTGAA
GCTTTGTTCCTCACCGTGGATCCCTACATGAGAGTGGCAGCCAAAAGATTGAAGGAAGGT
GATACAATGATGGGGCAGCAAGTGGCCAAAGTTGTGGAAAGTAAAAATGTAGCCCTACCA
AAAGGAACTATTGTACTGGCTTCTCCAGGCTGGACAACGCACTCCATTTCTGATGGGAAA
GATCTGGAAAAGCTGCTGACAGAGTGGCCAGACACAATACCACTGTCTTTGGCTCTGGGG
ACAGTTGGCATGCCAGGCCTGACTGCCTACTTTGGCCTACTTGAAATCTGTGGTGTGAAG
GGTGGAGAAACAGTGATGGTTAATGCAGCAGCTGGAGCTGTGGGCTCAGTCGTGGGGCAG
ATTGCAAAGCTCAAGGGCTGCAAAGTTGTTGGAGCAGTAGGGTCTGATGAAAAGGTTGCC
TACCTTCAAAAGCTTGGATTTGATGTCGTCTTTAACTACAAGACGGTAGAGTCTTTGGAA
GAAACCTTGAAGAAAGCGTCTCCTGATGGTTATGATTGTTATTTTGATAATGTAGGTGGA
GAGTTTTCAAACACTGTTATCGGCCAGATGAAGAAATTTGGAAGGATTGCCATATGTGGA
GCCATCTCTACATATAACAGAACCGGCCCACTTCCCCCAGGCCCACCCCCAGAGATTGTT
ATCTATCAGGAGCTTCGCATGGAAGCTTTTGTCGTCTACCGCTGGCAAGGAGATGCCCGC
CAAAAAGCTCTGAAGGACTTGCTGAAATGGGTCTTAGAGGGTAAAATCCAGTACAAGGAA
TATATCATTGAAGGATTTGAAAACATGCCAGCTGCATTTATGGGAATGCTGAAAGGAGAT
AATTTGGGGAAGACAATAGTGAAAGCATGA
Chromosome Location
9
Locus
9q31.3
External Identifiers
ResourceLink
UniProtKB IDQ14914
UniProtKB Entry NamePTGR1_HUMAN
GenBank Protein ID23271371
GenBank Gene IDBC035228
GeneCard IDPTGR1
HGNC IDHGNC:18429
PDB ID(s)1ZSV, 2Y05
KEGG IDhsa:22949
NCBI Gene ID22949
General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [Article]
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  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  4. Yokomizo T, Ogawa Y, Uozumi N, Kume K, Izumi T, Shimizu T: cDNA cloning, expression, and mutagenesis study of leukotriene B4 12-hydroxydehydrogenase. J Biol Chem. 1996 Feb 2;271(5):2844-50. [Article]
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Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
Nicotinamide adenine dinucleotide phosphateexperimentalunknowntargetDetails
(5E,13E)-11-HYDROXY-9,15-DIOXOPROSTA-5,13-DIEN-1-OIC ACIDexperimentalunknowntargetDetails
p-Coumaric acidexperimentalunknowntargetDetails
Elafibranorapproved, investigationalunknownenzymesubstrateDetails