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O02853 (PTGDS_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. 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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length191 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. Ref.1

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, expressed in the testis, epididymis and prostate, and secreted into the seminal fluid. Ref.1 Ref.3 Ref.4

Developmental stage

During spermatogenesis, expression is low in the round spermatids of stages I-II before increasing to peak in the elongating spermatids of stages III-VII. Decreased expression observed in stage VIII.

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
   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.1. 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_functionfatty acid binding

Inferred from electronic annotation. Source: Ensembl

prostaglandin-D synthase activity

Inferred from sequence or structural similarity. Source: UniProtKB

retinoid binding

Inferred from sequence or structural similarity. Source: UniProtKB

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 – 2828 Ref.1
Chain29 – 191163Prostaglandin-H2 D-isomerase
PRO_0000017940

Sites

Active site651Nucleophile By similarity

Amino acid modifications

Glycosylation511N-linked (GlcNAc...) By similarity
Glycosylation781N-linked (GlcNAc...) By similarity
Disulfide bond89 ↔ 186 By similarity

Sequences

Sequence LengthMass (Da)Tools
O02853 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 3B55675987B7A4C4

FASTA19121,229
        10         20         30         40         50         60 
MATPNRLWMA LLLLGVLGVL QTPAPAQAAL QPNFEEDKFL GRWFTSGLAS NSSWFLEKKK 

        70         80         90        100        110        120 
VLSMCKSVVA PAADGGLNLT STFLRKDQCE TRTLLLRPAG PPGCYSYTSP HWSSTHEVSV 

       130        140        150        160        170        180 
AETDYETYAL LYTEGVRGPG QDFRMATLYS RSQNPRAEVK EHFTTFAKSL GFTEEGIVFL 

       190 
PKTDKCMEEH P 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a fertility-associated protein in bull seminal plasma as lipocalin-type prostaglandin D synthase."
Gerena R.L., Irikura D., Urade Y., Eguchi N., Chapman D.A., Killian G.J.
Biol. Reprod. 58:826-833(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-48, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
Tissue: Brain.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal pons and Hypothalamus.
[3]"Immunocytochemical localization of lipocalin-type prostaglandin D synthase in the bull testis and epididymis and on ejaculated sperm."
Gerena R.L., Irikura D., Eguchi N., Urade Y., Killian G.J.
Biol. Reprod. 62:547-556(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[4]"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: TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB004647 mRNA. Translation: BAA20431.1.
BC133435 mRNA. Translation: AAI33436.1.
BC133438 mRNA. Translation: AAI33439.1.
BC133445 mRNA. Translation: AAI33446.1.
BC142082 mRNA. Translation: AAI42083.1.
RefSeqNP_777216.1. NM_174791.4.
UniGeneBt.1645.

3D structure databases

ProteinModelPortalO02853.
SMRO02853. Positions 30-189.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBO02853.
ChEMBLCHEMBL4651.

Proteomic databases

PaxDbO02853.
PRIDEO02853.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000020065; ENSBTAP00000020065; ENSBTAG00000015074.
GeneID286858.
KEGGbta:286858.

Organism-specific databases

CTD5730.

Phylogenomic databases

eggNOGNOG45731.
GeneTreeENSGT00620000088005.
HOGENOMHOG000231660.
HOVERGENHBG106490.
InParanoidO02853.
KOK01830.
OMAPGQDFRM.
OrthoDBEOG78PVBH.
TreeFamTF336103.

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...

Other

NextBio20806507.

Entry information

Entry namePTGDS_BOVIN
AccessionPrimary (citable) accession number: O02853
Secondary accession number(s): A2VDW5, A5PJE8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 1, 1997
Last modified: April 16, 2014
This is version 109 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