PTGDS
entrez
5730
canonical
uniprot
P41222
canonical
ensembl
ENSG00000107317
resolver
ensembl
ENSG00000284341
resolver
ensp
ENSP00000360687
resolver
ensp
ENSP00000435033
resolver
ensp
ENSP00000521810
resolver
ensp
ENSP00000521815
resolver
ensp
ENSP00000521817
resolver
ensp
ENSP00000521820
resolver
ensp
ENSP00000521821
resolver
ensp
ENSP00000625019
resolver
enst
ENST00000371625
resolver
enst
ENST00000471521
resolver
enst
ENST00000851751
resolver
enst
ENST00000851756
resolver
enst
ENST00000851758
resolver
enst
ENST00000851761
resolver
enst
ENST00000851762
resolver
enst
ENST00000954960
resolver
genesymbol
PTGDS
resolver
genesymbol_syn
PDS
resolver
hgnc
HGNC:9592
resolver
uniprot
A0A024R8G3
resolver
uniprot
B2R727
resolver
uniprot
Q5SQ10
resolver
uniprot
Q7M4P3
resolver
uniprot
Q9UC22
resolver
uniprot
Q9UCC9
resolver
uniprot
Q9UCD9
resolver
uniprot_entry
A0A024R8G3_HUMAN
resolver
uniprot_entry
PTGDS_HUMAN
resolver
uniprot_sec
B2R727
resolver
uniprot_sec
Q5SQ10
resolver
uniprot_sec
Q7M4P3
resolver
uniprot_sec
Q9UC22
resolver
uniprot_sec
Q9UCC9
resolver
uniprot_sec
Q9UCD9
resolver
amino_acid_sequence
MATHHTLWMGLALLGVLGDLQAAPEAQVSVQPNFQQDKFLGRWFSAGLASNSSWLREKKAALSMCKSVVAPATDGGLNLTSTFLRKNQCETRTMLLQPAGSLGSYSYRSPHWGSTYSVSVVETDYDQYALLYSQGSKGPGEDFRMATLYSRTQTPRAELKEKFTAFCKAQGFTEDTIVFLPQTDKCMTEQ
uniprot
proteins
ec_number
5.3.99.2
uniprot
proteins
function
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). Can also, catalyze the conversion of PGH3 (derived from eicosapentaenoate (EPA, C20:5n-3)) to PGD3, though PGH2 remains the preferred substrate (PubMed:17519235). {ECO:0000250|UniProtKB:O09114, ECO:0000269|PubMed:17519235, ECO:0000269|PubMed:20667974, ECO:0000269|PubMed:9475419}.
uniprot
proteins
mass_dalton
21029
uniprot
proteins
mutagenesis
MUTAGEN 59; /note="K->A: Increases enzyme activity about two-fold."; /evidence="ECO:0000269|PubMed:20667974"; MUTAGEN 64; /note="M->A: Reduces enzyme activity almost ten-fold."; /evidence="ECO:0000269|PubMed:20667974"; MUTAGEN 65; /note="C->A: Loss of enzyme activity."; /evidence="ECO:0000269|PubMed:20667974"; MUTAGEN 79; /note="L->A: Reduces enzyme activity over ten-fold."; /evidence="ECO:0000269|PubMed:20667974"; MUTAGEN 83; /note="F->A: Reduces enzyme activity about five-fold."; /evidence="ECO:0000269|PubMed:20667974"; MUTAGEN 131; /note="L->A: Reduces enzyme activity almost ten-fold."; /evidence="ECO:0000269|PubMed:20667974"; MUTAGEN 149; /note="Y->A: Increases enzyme activity about two-fold."; /evidence="ECO:0000269|PubMed:20667974
uniprot
proteins
post_translational_modification
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. {ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:23234360, ECO:0000269|PubMed:7692978, ECO:0000269|PubMed:8336134}.
uniprot
proteins
protein_family
Calycin superfamily
uniprot
proteins
protein_family
Lipocalin family
uniprot
proteins
pubmed
10462696
uniprot
proteins
pubmed
11287775
uniprot
proteins
pubmed
11669522
uniprot
proteins
pubmed
11882588
uniprot
proteins
pubmed
1385416
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16303743
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
1726844
uniprot
proteins
pubmed
17519235
uniprot
proteins
pubmed
1902577
uniprot
proteins
pubmed
19139490
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19838169
uniprot
proteins
pubmed
20667974
uniprot
proteins
pubmed
22171320
uniprot
proteins
pubmed
23234360
uniprot
proteins
pubmed
7689714
uniprot
proteins
pubmed
7692978
uniprot
proteins
pubmed
8336134
uniprot
proteins
pubmed
8336140
uniprot
proteins
pubmed
8599604
uniprot
proteins
pubmed
8674187
uniprot
proteins
pubmed
8761996
uniprot
proteins
pubmed
9065498
uniprot
proteins
pubmed
9162076
uniprot
proteins
pubmed
9405674
uniprot
proteins
pubmed
9475419
uniprot
proteins
pubmed
9844724
uniprot
proteins
sequence_length
190
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Rough endoplasmic reticulum {ECO:0000269|PubMed:9065498}. Nucleus membrane {ECO:0000269|PubMed:9065498}. Golgi apparatus {ECO:0000269|PubMed:9065498}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:9065498}. Secreted {ECO:0000269|PubMed:9065498}. Note=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.
uniprot
proteins