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Details on Person UniProt:P41222 PTGDS
| Class:Id | ReferenceGeneProduct:61608 |
|---|---|
| _chainChangeLog | signal peptide:1-22 added on Fri February 6 2015;chain:23-190 added on Fri February 6 2015 |
| _displayName | UniProt:P41222 PTGDS |
| _timestamp | 2024-11-03 20:02:42 |
| chain | signal peptide:1-22 chain:23-190 |
| checksum | DF35FE48AD0D5EF3 |
| comment | FUNCTION Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation (PubMed:20667974). 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 hydrophobic 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 (PubMed:20667974, PubMed:9475419). Involved in PLA2G3-dependent maturation of mast cells. PLA2G3 is secreted by immature mast cells and acts on nearby fibroblasts upstream to PTDGS to synthesize PGD2, which in turn promotes mast cell maturation and degranulation via PTGDR (By similarity).CATALYTIC ACTIVITY prostaglandin H2 = prostaglandin D2SUBUNIT Monomer.INTERACTION Detected on rough endoplasmic reticulum of arachnoid and menigioma cells. Localized to the nuclear envelope, Golgi apparatus, secretory vesicles and spherical cytoplasmic structures in arachnoid trabecular cells, and to circular cytoplasmic structures in meningeal macrophages and perivascular microglial cells. In oligodendrocytes, localized to the rough endoplasmic reticulum and nuclear envelope. In retinal pigment epithelial cells, localized to distinct cytoplasmic domains including the perinuclear region. Also secreted.TISSUE SPECIFICITY Abundant in the brain and CNS, where it is expressed in tissues of the blood-brain barrier and secreted into the cerebro-spinal fluid. Abundantly expressed in the heart. In the male reproductive system, it is expressed in the testis, epididymis and prostate, and is secreted into the seminal fluid. Expressed in the eye and secreted into the aqueous humor. Lower levels detected in various tissue fluids such as serum, normal urine, ascitic fluid and tear fluid. Also found in a number of other organs including ovary, fimbriae of the fallopian tubes, kidney, leukocytes.DEVELOPMENTAL STAGE Expression in the amniotic fluid increases dramatically during weeks 12 to 25 of pregnancy. Levels decrease slowly after 25 weeks.INDUCTION By IL1B/interleukin-1 beta and thyroid hormone. Probably induced by dexamethasone, dihydrotestosterone (DHT), progesterone, retinoic acid and retinal. Repressed by the Notch-Hes signaling pathway.DOMAIN Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.PTM N- and O-glycosylated. Both N-glycosylation recognition sites are almost quantitatively occupied by N-glycans of the biantennary complex type, with a considerable proportion of structures bearing a bisecting GlcNAc. N-glycan at Asn-78: dHex1Hex5HexNAc4. Agalacto structure as well as sialylated and nonsialylated oligosaccharides bearing alpha2-3- and/or alpha2-6-linked NeuNAc are present.MISCELLANEOUS It has been proposed that the urinary and serum levels may provide a sensitive indicator of renal damage in diabetes mellitus and hypertension. Elevated levels in the coronary circulation may also be associated with angina. Changes in charge and molecular weight microheterogeneity, due to modification of the N-linked oligosaccharides, may be associated with neurodegenerative disease and multiple sclerosis. Detected in meningioma but not in other brain tumors and may be considered a specific cell marker for meningioma. Expression levels in amniotic fluid are altered in abnormal pregnancies. Levels are lower in pregnancies with trisomic fetuses and fetuses with renal abnormalities.SIMILARITY Belongs to the calycin superfamily. Lipocalin family. |
| description | recommendedName: Prostaglandin-H2 D-isomerase ecNumber evidence="9"5.3.99.2 alternativeName: Beta-trace protein alternativeName: Cerebrin-28 alternativeName: Glutathione-independent PGD synthase alternativeName: Lipocalin-type prostaglandin-D synthase shortName evidence="25"L-PGDS alternativeName: Prostaglandin-D2 synthase shortName: PGD2 synthase shortName: PGDS shortName: PGDS2 |
| geneName | PTGDS PDS |
| identifier | P41222 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Cytoplasm Direct protein sequencing Disulfide bond Endoplasmic reticulum Fatty acid biosynthesis Fatty acid metabolism Glycoprotein Golgi apparatus Isomerase Lipid biosynthesis Lipid metabolism Mast cell degranulation Membrane Nucleus Prostaglandin biosynthesis Prostaglandin metabolism Proteomics identification Reference proteome Secreted Signal Transport |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 |
| name | PTGDS |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8996814] ENSEMBL:ENSG00000107317 PTGDS [Homo sapiens] |
| secondaryIdentifier | PTGDS_HUMAN B2R727 Q5SQ10 Q7M4P3 Q9UC22 Q9UCC9 Q9UCD9 |
| sequenceLength | 190 |
| species | [Species:48887] Homo sapiens |
| (referenceEntity) | [EntityWithAccessionedSequence:2142814] PTGDS [endoplasmic reticulum membrane] [Homo sapiens] |
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No pathways have been reviewed or authored by UniProt:P41222 PTGDS (61608)
