PTGDS_BOVIN
ID PTGDS_BOVIN Reviewed; 191 AA.
AC O02853; A2VDW5; A5PJE8;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Prostaglandin-H2 D-isomerase;
DE EC=5.3.99.2 {ECO:0000269|PubMed:9510973};
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-48, CATALYTIC ACTIVITY,
RP TISSUE SPECIFICITY, AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=9510973; DOI=10.1095/biolreprod58.3.826;
RA Gerena R.L., Irikura D., Urade Y., Eguchi N., Chapman D.A., Killian G.J.;
RT "Identification of a fertility-associated protein in bull seminal plasma as
RT lipocalin-type prostaglandin D synthase.";
RL Biol. Reprod. 58:826-833(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons, and Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=10684794; DOI=10.1095/biolreprod62.3.547;
RA Gerena R.L., Irikura D., Eguchi N., Urade Y., Killian G.J.;
RT "Immunocytochemical localization of lipocalin-type prostaglandin D synthase
RT in the bull testis and epididymis and on ejaculated sperm.";
RL Biol. Reprod. 62:547-556(2000).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=11804963; DOI=10.1095/biolreprod66.2.458;
RA Fouchecourt S., Charpigny G., Reinaud P., Dumont P., Dacheux J.-L.;
RT "Mammalian lipocalin-type prostaglandin D2 synthase in the fluids of the
RT male genital tract: putative biochemical and physiological functions.";
RL Biol. Reprod. 66:458-467(2002).
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 (PubMed:9510973). Involved in a variety of CNS
CC functions, such as sedation, NREM sleep and PGE2-induced allodynia, and
CC may have an anti-apoptotic role in oligodendrocytes. Binds small non-
CC substrate lipophilic molecules, including biliverdin, bilirubin,
CC retinal, retinoic acid and thyroid hormone, and may act as a scavenger
CC for harmful hydrophobic molecules and as a secretory retinoid and
CC thyroid hormone transporter. Possibly involved in development and
CC maintenance of the blood-brain, blood-retina, blood-aqueous humor and
CC blood-testis barrier. It is likely to play important roles in both
CC maturation and maintenance of the central nervous system and male
CC reproductive system (By similarity). Involved in PLA2G3-dependent
CC maturation of mast cells. PLA2G3 is secreted by immature mast cells and
CC acts on nearby fibroblasts upstream to PTDGS to synthesize PGD2, which
CC in turn promotes mast cell maturation and degranulation via PTGDR (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:O09114,
CC ECO:0000250|UniProtKB:P41222, ECO:0000269|PubMed:9510973}.
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:0000269|PubMed:9510973};
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 -!- TISSUE SPECIFICITY: In the male reproductive system, expressed in the
CC testis, epididymis and prostate, and secreted into the seminal fluid.
CC {ECO:0000269|PubMed:10684794, ECO:0000269|PubMed:11804963,
CC ECO:0000269|PubMed:9510973}.
CC -!- DEVELOPMENTAL STAGE: During spermatogenesis, expression is low in the
CC round spermatids of stages I-II before increasing to peak in the
CC elongating spermatids of stages III-VII. Decreased expression observed
CC in stage VIII.
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; AB004647; BAA20431.1; -; mRNA.
DR EMBL; BC133435; AAI33436.1; -; mRNA.
DR EMBL; BC133438; AAI33439.1; -; mRNA.
DR EMBL; BC133445; AAI33446.1; -; mRNA.
DR EMBL; BC142082; AAI42083.1; -; mRNA.
DR RefSeq; NP_777216.1; NM_174791.4.
DR AlphaFoldDB; O02853; -.
DR SMR; O02853; -.
DR IntAct; O02853; 1.
DR STRING; 9913.ENSBTAP00000020065; -.
DR BindingDB; O02853; -.
DR ChEMBL; CHEMBL4651; -.
DR PaxDb; O02853; -.
DR PeptideAtlas; O02853; -.
DR Ensembl; ENSBTAT00000020065; ENSBTAP00000020065; ENSBTAG00000015074.
DR GeneID; 286858; -.
DR KEGG; bta:286858; -.
DR CTD; 5730; -.
DR VEuPathDB; HostDB:ENSBTAG00000015074; -.
DR eggNOG; ENOG502S6GK; Eukaryota.
DR GeneTree; ENSGT01050000244979; -.
DR HOGENOM; CLU_094061_1_1_1; -.
DR InParanoid; O02853; -.
DR OMA; WFREKKS; -.
DR OrthoDB; 1341030at2759; -.
DR TreeFam; TF336103; -.
DR Reactome; R-BTA-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR PRO; PR:O02853; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000015074; Expressed in pigment epithelium of eye and 104 other tissues.
DR ExpressionAtlas; O02853; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IDA: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:0044793; P:negative regulation by host of viral process; IDA:AgBase.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IDA:AgBase.
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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Disulfide bond;
KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Glycoprotein; Golgi apparatus; Isomerase; Lipid biosynthesis;
KW Lipid metabolism; Mast cell degranulation; Membrane; Nucleus;
KW Prostaglandin biosynthesis; Prostaglandin metabolism; Reference proteome;
KW Secreted; Signal; Transport.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:9510973"
FT CHAIN 29..191
FT /note="Prostaglandin-H2 D-isomerase"
FT /id="PRO_0000017940"
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: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; 21229 MW; 3B55675987B7A4C4 CRC64;
MATPNRLWMA LLLLGVLGVL QTPAPAQAAL QPNFEEDKFL GRWFTSGLAS NSSWFLEKKK
VLSMCKSVVA PAADGGLNLT STFLRKDQCE TRTLLLRPAG PPGCYSYTSP HWSSTHEVSV
AETDYETYAL LYTEGVRGPG QDFRMATLYS RSQNPRAEVK EHFTTFAKSL GFTEEGIVFL
PKTDKCMEEH P
