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Showing Protein Prostaglandin-H2 D-isomerase (HMDBP01576)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 2 metabolites
Identification
HMDB Protein ID HMDBP01576
Secondary Accession Numbers
  • 6872
Name Prostaglandin-H2 D-isomerase
Synonyms
  1. Beta-trace protein
  2. Cerebrin-28
  3. Glutathione-independent PGD synthase
  4. Lipocalin-type prostaglandin-D synthase
  5. PGD2 synthase
  6. PGDS
  7. PGDS2
  8. Prostaglandin-D2 synthase
Gene Name PTGDS
Protein Type Enzyme
Biological Properties
General Function Involved in binding
Specific Function Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophopic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system.
Pathways
  • Acetaminophen Action Pathway
  • Acetylsalicylic Acid Action Pathway
  • Antipyrine Action Pathway
  • Antrafenine Action Pathway
  • Arachidonic acid metabolism
  • Arachidonic Acid Metabolism
  • Bromfenac Action Pathway
  • Carprofen Action Pathway
  • Celecoxib Action Pathway
  • Diclofenac Action Pathway
  • Diflunisal Action Pathway
  • Etodolac Action Pathway
  • Etoricoxib Action Pathway
  • Fenoprofen Action Pathway
  • Flurbiprofen Action Pathway
  • Ibuprofen Action Pathway
  • Indomethacin Action Pathway
  • Ketoprofen Action Pathway
  • Ketorolac Action Pathway
  • Leukotriene C4 Synthesis Deficiency
  • Lornoxicam Action Pathway
  • Lumiracoxib Action Pathway
  • Magnesium salicylate Action Pathway
  • Mefenamic Acid Action Pathway
  • Meloxicam Action Pathway
  • Nabumetone Action Pathway
  • Naproxen Action Pathway
  • Nepafenac Action Pathway
  • Oxaprozin Action Pathway
  • Phenylbutazone Action Pathway
  • Piroxicam Action Pathway
  • Rofecoxib Action Pathway
  • Salicylate-sodium Action Pathway
  • Salicylic Acid Action Pathway
  • Salsalate Action Pathway
  • Sulindac Action Pathway
  • Suprofen Action Pathway
  • Tenoxicam Action Pathway
  • Tiaprofenic Acid Action Pathway
  • Tolmetin Action Pathway
  • Trisalicylate-choline Action Pathway
  • Valdecoxib Action Pathway
Reactions
(5Z,13E,15S)-9-alpha,11-alpha-epidioxy-15-hydroxyprosta-5,13-dienoate → (5Z,13E,15S)-9-alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate details
Prostaglandin H2 → Prostaglandin D2 details
GO Classification
Biological Process
regulation of circadian sleep/wake cycle, sleep
response to glucocorticoid stimulus
prostaglandin biosynthetic process
Cellular Component
Golgi apparatus
perinuclear region of cytoplasm
nuclear membrane
extracellular space
rough endoplasmic reticulum
Function
binding
transporter activity
Molecular Function
retinoid binding
small molecule binding
fatty acid binding
transporter activity
prostaglandin-D synthase activity
Process
metabolic process
primary metabolic process
establishment of localization
transport
lipid metabolic process
Cellular Location
  1. Cytoplasm
  2. perinuclear region
  3. Secreted
  4. Golgi apparatus
  5. Nucleus membrane
  6. Rough endoplasmic reticulum
Gene Properties
Chromosome Location 9
Locus 9q34.2-q34.3
SNPs PTGDS
Gene Sequence 
>573 bp
ATGGCTACTCATCACACGCTGTGGATGGGACTGGCCCTGCTGGGGGTGCTGGGCGACCTG
CAGGCAGCACCGGAGGCCCAGGTCTCCGTGCAGCCCAACTTCCAGCAGGACAAGTTCCTG
GGGCGCTGGTTCAGCGCGGGCCTCGCCTCCAACTCGAGCTGGCTCCGGGAGAAGAAGGCG
GCGTTGTCCATGTGCAAGTCTGTGGTGGCCCCTGCCACGGATGGTGGCCTCAACCTGACC
TCCACCTTCCTCAGGAAAAACCAGTGTGAGACCCGAACCATGCTGCTGCAGCCCGCGGGG
TCCCTCGGCTCCTACAGCTACCGGAGTCCCCACTGGGGCAGCACCTACTCCGTGTCAGTG
GTGGAGACCGACTACGACCAGTACGCGCTGCTGTACAGCCAGGGCAGCAAGGGCCCTGGC
GAGGACTTCCGCATGGCCACCCTCTACAGCCGAACCCAGACCCCCAGGGCTGAGTTAAAG
GAGAAATTCACCGCCTTCTGCAAGGCCCAGGGCTTCACAGAGGATACCATTGTCTTCCTG
CCCCAAACCGATAAGTGCATGACGGAACAATAG
Protein Properties
Number of Residues 190
Molecular Weight 21028.665
Theoretical pI 7.796
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Prostaglandin-H2 D-isomerase
MATHHTLWMGLALLGVLGDLQAAPEAQVSVQPNFQQDKFLGRWFSAGLASNSSWLREKKA
ALSMCKSVVAPATDGGLNLTSTFLRKNQCETRTMLLQPAGSLGSYSYRSPHWGSTYSVSV
VETDYDQYALLYSQGSKGPGEDFRMATLYSRTQTPRAELKEKFTAFCKAQGFTEDTIVFL
PQTDKCMTEQ
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P41222
UniProtKB/Swiss-Prot Entry Name PTGDS_HUMAN
PDB IDs
GenBank Gene ID M61900
GeneCard ID PTGDS
GenAtlas ID PTGDS
HGNC ID HGNC:9592
References
General References
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  6. Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [PubMed:16303743 ]
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  8. Nagata A, Suzuki Y, Igarashi M, Eguchi N, Toh H, Urade Y, Hayaishi O: Human brain prostaglandin D synthase has been evolutionarily differentiated from lipophilic-ligand carrier proteins. Proc Natl Acad Sci U S A. 1991 May 1;88(9):4020-4. [PubMed:1902577 ]
  9. White DM, Mikol DD, Espinosa R, Weimer B, Le Beau MM, Stefansson K: Structure and chromosomal localization of the human gene for a brain form of prostaglandin D2 synthase. J Biol Chem. 1992 Nov 15;267(32):23202-8. [PubMed:1385416 ]
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  19. Yamashima T, Sakuda K, Tohma Y, Yamashita J, Oda H, Irikura D, Eguchi N, Beuckmann CT, Kanaoka Y, Urade Y, Hayaishi O: Prostaglandin D synthase (beta-trace) in human arachnoid and meningioma cells: roles as a cell marker or in cerebrospinal fluid absorption, tumorigenesis, and calcification process. J Neurosci. 1997 Apr 1;17(7):2376-82. [PubMed:9065498 ]
  20. Blodorn B, Mader M, Urade Y, Hayaishi O, Felgenhauer K, Bruck W: Choroid plexus: the major site of mRNA expression for the beta-trace protein (prostaglandin D synthase) in human brain. Neurosci Lett. 1996 May 10;209(2):117-20. [PubMed:8761996 ]
  21. Eguchi Y, Eguchi N, Oda H, Seiki K, Kijima Y, Matsu-ura Y, Urade Y, Hayaishi O: Expression of lipocalin-type prostaglandin D synthase (beta-trace) in human heart and its accumulation in the coronary circulation of angina patients. Proc Natl Acad Sci U S A. 1997 Dec 23;94(26):14689-94. [PubMed:9405674 ]
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  25. Hiraoka A, Seiki K, Oda H, Eguchi N, Urade Y, Tominaga I, Baba K: Charge microheterogeneity of the beta-trace proteins (lipocalin-type prostaglandin D synthase) in the cerebrospinal fluid of patients with neurological disorders analyzed by capillary isoelectrofocusing. Electrophoresis. 2001 Oct;22(16):3433-7. [PubMed:11669522 ]
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