ID   PTGDS_CANLF             Reviewed;         191 AA.
AC   Q9XS65;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 134.
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   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-9.
RC   TISSUE=Brain;
RA   Nakau H., Nakajima H., Urade Y., Fujimori K., Oda H., Seiki K.;
RT   "Dog lipocalin-type prostaglandin D synthase cDNA.";
RL   Submitted (MAY-1999) 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   -!- PTM: N- and O-glycosylated. Both N-glycosylation recognition sites are
CC       almost quantitatively occupied by N-glycans of the biantennary complex
CC       type, with a considerable proportion of structures bearing a bisecting
CC       GlcNAc. N-glycan at Asn-78: dHex1Hex5HexNAc4. Agalacto structure as
CC       well as sialylated and nonsialylated oligosaccharides bearing alpha2-
CC       3- and/or alpha2-6-linked NeuNAc are present.
CC       {ECO:0000250|UniProtKB:P41222}.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC       {ECO:0000305}.
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DR   EMBL; AB026988; BAA77690.1; -; mRNA.
DR   RefSeq; NP_001003131.1; NM_001003131.1.
DR   AlphaFoldDB; Q9XS65; -.
DR   SMR; Q9XS65; -.
DR   STRING; 9612.ENSCAFP00000043090; -.
DR   PaxDb; Q9XS65; -.
DR   PRIDE; Q9XS65; -.
DR   GeneID; 403740; -.
DR   KEGG; cfa:403740; -.
DR   CTD; 5730; -.
DR   eggNOG; ENOG502S6GK; Eukaryota.
DR   HOGENOM; CLU_094061_1_1_1; -.
DR   InParanoid; Q9XS65; -.
DR   OrthoDB; 1341030at2759; -.
DR   Proteomes; UP000002254; Unplaced.
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; Reference proteome; Secreted; Signal;
KW   Transport.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000250|UniProtKB:P41222"
FT   CHAIN           25..191
FT                   /note="Prostaglandin-H2 D-isomerase"
FT                   /id="PRO_0000017941"
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"
FT   VARIANT         9
FT                   /note="L -> R"
FT                   /evidence="ECO:0000269|Ref.1"
SQ   SEQUENCE   191 AA;  21142 MW;  05DD17A63001C256 CRC64;
     MGALCTLWLG LVLLGVLGAL QTSAQAQVSL QPNFQQDKFL GRWFTSGLAS NSSWFREKKN
     VLSMCMSVVA PTADGGLNLT STFLRKDQCE TRTLLLRPAG TPGCYSYTSP HWGSTHDVWV
     VATNYEEYAL LYTAGSKGLG QDFHMATLYS RTQTPKAEIK EKFSTFAKTQ GFTEDAIVFL
     PQTDKCMEEN K