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Protein

Prostaglandin-H2 D-isomerase

Gene

PTGDS

Organism
Ovis aries (Sheep)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. 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 hydrophopic 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 (By similarity).By similarity

Catalytic activityi

(5Z,13E,15S)-9-alpha,11-alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E,15S)-9-alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei65 – 651NucleophileBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Prostaglandin biosynthesis, Prostaglandin metabolism, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Prostaglandin-H2 D-isomerase (EC:5.3.99.2)
Alternative name(s):
Glutathione-independent PGD synthase
Lipocalin-type prostaglandin-D synthase
Prostaglandin-D2 synthase
Short name:
PGD2 synthase
Short name:
PGDS
Short name:
PGDS2
Gene namesi
Name:PTGDS
OrganismiOvis aries (Sheep)
Taxonomic identifieri9940 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis
ProteomesiUP000002356 Componenti: Unplaced

Subcellular locationi

  • Rough endoplasmic reticulum By similarity
  • Nucleus membrane By similarity
  • Golgi apparatus By similarity
  • Cytoplasmperinuclear region By similarity
  • Secreted By similarity

  • 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 (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Golgi apparatus, Membrane, Nucleus, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424By similarityAdd
BLAST
Chaini25 – 191167Prostaglandin-H2 D-isomerasePRO_0000017951Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi51 – 511N-linked (GlcNAc...)By similarity
Glycosylationi78 – 781N-linked (GlcNAc...)By similarity
Disulfide bondi89 ↔ 186By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

In the male reproductive system, it is expressed in the testis and epididymis, and is secreted into the seminal fluid.3 Publications

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9XSM0.
SMRiQ9XSM0. Positions 30-188.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.By similarity

Sequence similaritiesi

Belongs to the calycin superfamily. Lipocalin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG106490.
KOiK01830.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002972. PstgldnD_synth.
[Graphical view]
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00179. LIPOCALIN.
PR01254. PGNDSYNTHASE.
SUPFAMiSSF50814. SSF50814. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9XSM0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATPNRPWMG LLLLGVLGVL QTPAPTEAAL QPNFEEDKFL GRWFTSGLAS
60 70 80 90 100
NSSWFLEKRK VLSMCKSEVA PAADGGLNVT STFLRKDQCE TRTLLLRPAG
110 120 130 140 150
PPGCYSYTSP HWSSTHEVSV AETDYETYAL LYTESVRGPG PDSLMATLYS
160 170 180 190
RTQTPRAEVK EKFTTFARSL GFTEEGIVFL PKTDKCMEVR T
Length:191
Mass (Da):21,183
Last modified:November 1, 1999 - v1
Checksum:iB7555070F8A54244
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ133642 mRNA. Translation: CAB40371.1.
RefSeqiNP_001009257.1. NM_001009257.1.
UniGeneiOar.691.

Genome annotation databases

GeneIDi443192.
KEGGioas:443192.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ133642 mRNA. Translation: CAB40371.1.
RefSeqiNP_001009257.1. NM_001009257.1.
UniGeneiOar.691.

3D structure databases

ProteinModelPortaliQ9XSM0.
SMRiQ9XSM0. Positions 30-188.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi443192.
KEGGioas:443192.

Organism-specific databases

CTDi5730.

Phylogenomic databases

HOVERGENiHBG106490.
KOiK01830.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002972. PstgldnD_synth.
[Graphical view]
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00179. LIPOCALIN.
PR01254. PGNDSYNTHASE.
SUPFAMiSSF50814. SSF50814. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Mammalian lipocalin-type prostaglandin D2 synthase in the fluids of the male genital tract: putative biochemical and physiological functions."
    Fouchecourt S., Charpigny G., Reinaud P., Dumont P., Dacheux J.-L.
    Biol. Reprod. 66:458-467(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  2. "Glutathione-independent prostaglandin D2 synthase in ram and stallion epididymal fluids: origin and regulation."
    Fouchecourt S., Dacheux F., Dacheux J.-L.
    Biol. Reprod. 60:558-566(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 29-45; 63-68 AND 100-107, TISSUE SPECIFICITY.
  3. "Astrocytes synthesize and secrete prostaglandin D synthetase in vitro."
    Giacomelli S., Leone M.-G., Grima J., Silvestrini B., Cheng C.Y.
    Biochim. Biophys. Acta 1310:269-276(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  4. "Prostaglandin d(2) synthase secreted in the caput epididymidis displays spatial and temporal delay between messenger RNA and protein expression during postnatal development."
    Fouchecourt S., Castella S., Dacheux F., Dacheux J.-L.
    Biol. Reprod. 68:174-179(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiPTGDS_SHEEP
AccessioniPrimary (citable) accession number: Q9XSM0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: January 7, 2015
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.