ID   PTGDS_GORGO             Reviewed;         190 AA.
AC   Q8WNM1;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   24-JAN-2024, entry version 100.
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   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11948213; DOI=10.1093/jhered/92.6.469;
RA   Stauffer R.L., Walker A., Ryder O.A., Lyons-Weiler M., Hedges S.B.;
RT   "Human and ape molecular clocks and constraints on paleontological
RT   hypotheses.";
RL   J. Hered. 92:469-474(2001).
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; AF354637; AAL56241.1; -; mRNA.
DR   RefSeq; NP_001266620.1; NM_001279691.1.
DR   AlphaFoldDB; Q8WNM1; -.
DR   SMR; Q8WNM1; -.
DR   STRING; 9593.ENSGGOP00000004279; -.
DR   GlyCosmos; Q8WNM1; 2 sites, No reported glycans.
DR   GeneID; 101130674; -.
DR   KEGG; ggo:101130674; -.
DR   CTD; 5730; -.
DR   InParanoid; Q8WNM1; -.
DR   OrthoDB; 5266874at2759; -.
DR   Proteomes; UP000001519; 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; IEA:UniProtKB-SubCell.
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   CDD; cd19419; lipocalin_L-PGDS; 1.
DR   Gene3D; 2.40.128.20; -; 1.
DR   InterPro; IPR012674; Calycin.
DR   InterPro; IPR002345; Lipocalin.
DR   InterPro; IPR022272; Lipocalin_CS.
DR   InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR   PANTHER; PTHR11430; LIPOCALIN; 1.
DR   PANTHER; PTHR11430:SF86; PROSTAGLANDIN-H2 D-ISOMERASE; 1.
DR   Pfam; PF00061; Lipocalin; 1.
DR   PRINTS; PR00179; LIPOCALIN.
DR   PRINTS; PR01254; PGNDSYNTHASE.
DR   SUPFAM; SSF50814; Lipocalins; 1.
DR   PROSITE; PS00213; LIPOCALIN; 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   Reference proteome; Secreted; Signal; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250|UniProtKB:P41222"
FT   CHAIN           23..190
FT                   /note="Prostaglandin-H2 D-isomerase"
FT                   /id="PRO_0000017943"
FT   ACT_SITE        65
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P41222"
FT   CARBOHYD        51
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        78
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        89..186
FT                   /evidence="ECO:0000250|UniProtKB:O09114"
SQ   SEQUENCE   190 AA;  20985 MW;  B5F3549C1946F003 CRC64;
     MATHHTLWMG LALLGVLGDL QAAPEAQVSV QPNFQQDKFL GRWFSAGLAS NSSWLREKKA
     ALSMCKSVVA PAADGGLNLT STFLRKNQCE TRTMLLQTAG SLGSYSYRSP HWGSTYSVSV
     VETDYDQYAL LYSQGSKGPG EDFRMATLYS RTQTPRAELK EKFTAFCKAQ GFTEDTIVFL
     PQTDKCLTEQ
//