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O97921 (PTGDS_HORSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PTGDS
OrganismEquus caballus (Horse) [Reference proteome]
Taxonomic identifier9796 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus

Protein attributes

Sequence length194 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

(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.

Subunit structure

Monomer By similarity.

Subcellular location

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.

Tissue specificity

In the male reproductive system, it is expressed in the testis and epididymis, and is secreted into the seminal fluid. Ref.2

Domain

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

Sequence similarities

Belongs to the calycin superfamily. Lipocalin family.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
Prostaglandin biosynthesis
Prostaglandin metabolism
Transport
   Cellular componentCytoplasm
Endoplasmic reticulum
Golgi apparatus
Membrane
Nucleus
Secreted
   DomainSignal
   Molecular functionIsomerase
   PTMDisulfide bond
Glycoprotein
Pyrrolidone carboxylic acid
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processprostaglandin biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of circadian sleep/wake cycle, sleep

Inferred from sequence or structural similarity. Source: UniProtKB

transport

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular region

Inferred from direct assay Ref.2. Source: UniProtKB

extracellular space

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

rough endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionprostaglandin-D synthase activity

Inferred from sequence or structural similarity. Source: UniProtKB

retinoid binding

Inferred from sequence or structural similarity. Source: UniProtKB

small molecule binding

Inferred from electronic annotation. Source: InterPro

transporter activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 By similarity
Chain25 – 194170Prostaglandin-H2 D-isomerase
PRO_0000017944

Sites

Active site651Nucleophile By similarity

Amino acid modifications

Modified residue251Pyrrolidone carboxylic acid By similarity
Glycosylation511N-linked (GlcNAc...) By similarity
Glycosylation781N-linked (GlcNAc...) By similarity
Disulfide bond89 ↔ 189 By similarity

Experimental info

Sequence conflict115 – 1217VHEVSVV → PHEMSMM AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
O97921 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: C6E271A540877994

FASTA19421,669
        10         20         30         40         50         60 
MAASHTLWMG LVLLGVLGVL QTRAQAQPSL QPNFQQDKFL GRWFTSGLAS NSSWFREKKK 

        70         80         90        100        110        120 
VLSMCTSVVA PTADGGFNLT STFLRKDQCE TRTLLLQPAG PPGCYSYTSP HWGMVHEVSV 

       130        140        150        160        170        180 
VETDYEEYAL LYTHAESTKG LGGQDFRMAT LYSRVQSPRP EVKEKFSTFA KAQGFTEDAI 

       190 
VFLPQTDKCM EEHN 

« Hide

References

[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].
[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 108-122, TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ133469 mRNA. Translation: CAB38173.1.
RefSeqNP_001075337.1. NM_001081868.1.
UniGeneEca.12658.

3D structure databases

ProteinModelPortalO97921.
SMRO97921. Positions 24-192.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9796.ENSECAP00000007190.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100067921.
KEGGecb:100067921.

Organism-specific databases

CTD5730.

Phylogenomic databases

eggNOGNOG45731.
HOVERGENHBG106490.
KOK01830.

Family and domain databases

Gene3D2.40.128.20. 1 hit.
InterProIPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002972. PstgldnD_synth.
[Graphical view]
PfamPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSPR00179. LIPOCALIN.
PR01254. PGNDSYNTHASE.
SUPFAMSSF50814. SSF50814. 1 hit.
ProtoNetSearch...

Entry information

Entry namePTGDS_HORSE
AccessionPrimary (citable) accession number: O97921
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families