PTGDS_URSAR
ID PTGDS_URSAR Reviewed; 191 AA.
AC Q29562;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Prostaglandin-H2 D-isomerase;
DE EC=5.3.99.2 {ECO:0000250|UniProtKB:P41222};
DE AltName: Full=Glutathione-independent PGD synthase;
DE AltName: Full=Lipocalin-type prostaglandin-D synthase;
DE AltName: Full=Prostaglandin-D2 synthase;
DE Short=PGD2 synthase;
DE Short=PGDS;
DE Short=PGDS2;
DE Flags: Precursor;
GN Name=PTGDS;
OS Ursus arctos (Brown bear) (Grizzly bear).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9644;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Arachnoid membrane;
RA Irikura D., Maruyama T., Kanaoka Y., Urade Y.;
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin
CC involved in smooth muscle contraction/relaxation and a potent inhibitor
CC of platelet aggregation. Involved in a variety of CNS functions, such
CC as sedation, NREM sleep and PGE2-induced allodynia, and may have an
CC anti-apoptotic role in oligodendrocytes. Binds small non-substrate
CC lipophilic molecules, including biliverdin, bilirubin, retinal,
CC retinoic acid and thyroid hormone, and may act as a scavenger for
CC harmful hydrophobic molecules and as a secretory retinoid and thyroid
CC hormone transporter. Possibly involved in development and maintenance
CC of the blood-brain, blood-retina, blood-aqueous humor and blood-testis
CC barrier. It is likely to play important roles in both maturation and
CC maintenance of the central nervous system and male reproductive system
CC (By similarity). Involved in PLA2G3-dependent maturation of mast cells.
CC PLA2G3 is secreted by immature mast cells and acts on nearby
CC fibroblasts upstream to PTDGS to synthesize PGD2, which in turn
CC promotes mast cell maturation and degranulation via PTGDR (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:O09114,
CC ECO:0000250|UniProtKB:P41222}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=prostaglandin H2 = prostaglandin D2; Xref=Rhea:RHEA:10600,
CC ChEBI:CHEBI:57405, ChEBI:CHEBI:57406; EC=5.3.99.2;
CC Evidence={ECO:0000250|UniProtKB:P41222};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P41222}.
CC -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P41222}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P41222}. Golgi apparatus
CC {ECO:0000250|UniProtKB:P41222}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P41222}. Secreted
CC {ECO:0000250|UniProtKB:P41222}. Note=Detected on rough endoplasmic
CC reticulum of arachnoid and menigioma cells. Localized to the nuclear
CC envelope, Golgi apparatus, secretory vesicles and spherical cytoplasmic
CC structures in arachnoid trabecular cells, and to circular cytoplasmic
CC structures in meningeal macrophages and perivascular microglial cells.
CC In oligodendrocytes, localized to the rough endoplasmic reticulum and
CC nuclear envelope. In retinal pigment epithelial cells, localized to
CC distinct cytoplasmic domains including the perinuclear region. Also
CC secreted. {ECO:0000250|UniProtKB:P41222}.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC ligands in its interior. {ECO:0000250|UniProtKB:P41222}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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DR EMBL; D82047; BAA11520.1; -; mRNA.
DR AlphaFoldDB; Q29562; -.
DR SMR; Q29562; -.
DR PRIDE; Q29562; -.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0004667; F:prostaglandin-D synthase activity; ISS:UniProtKB.
DR GO; GO:0005501; F:retinoid binding; ISS:UniProtKB.
DR GO; GO:0036094; F:small molecule binding; IEA:InterPro.
DR GO; GO:0043303; P:mast cell degranulation; IEA:UniProtKB-KW.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; ISS:UniProtKB.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR002345; Lipocalin.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR InterPro; IPR002972; PstgldnD_synth.
DR PANTHER; PTHR11430; PTHR11430; 1.
DR PANTHER; PTHR11430:SF86; PTHR11430:SF86; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR SUPFAM; SSF50814; SSF50814; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Disulfide bond; Endoplasmic reticulum; Fatty acid biosynthesis;
KW Fatty acid metabolism; Glycoprotein; Golgi apparatus; Isomerase;
KW Lipid biosynthesis; Lipid metabolism; Mast cell degranulation; Membrane;
KW Nucleus; Prostaglandin biosynthesis; Prostaglandin metabolism;
KW Pyrrolidone carboxylic acid; Secreted; Signal; Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..191
FT /note="Prostaglandin-H2 D-isomerase"
FT /id="PRO_0000017952"
FT ACT_SITE 65
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P41222"
FT MOD_RES 25
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P22057"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT DISULFID 89..186
FT /evidence="ECO:0000250|UniProtKB:O09114"
SQ SEQUENCE 191 AA; 21415 MW; 117387F7B94B9EE3 CRC64;
MAALHTLWMG LVLLGVLGVL QTQAQVQVSL QPNFQQDKFL GRWFTSGLAS NSSWFREKKK
VLSMCVSVVA PSADGGLNLT STFLRKEQCE TRTLLLRPAG TPGCYSYTSP HWGSTHDVWV
AMTDYDEYAL LYTTGTKGLG QDFHMATLYS RTQTPRAEIK EKFTTFAKTQ GFTEDAIVFL
PQTDKCMEEH K
