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Q29095 (PTGDS_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 93. 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
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length189 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

Abundant in the brain and CNS, where it is expressed in tissues of the blood-brain barrier and secreted into the cerebro-spinal fluid. Ref.1 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 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 – 189165Prostaglandin-H2 D-isomerase
PRO_0000017948

Sites

Active site631Nucleophile By similarity

Amino acid modifications

Modified residue251Pyrrolidone carboxylic acid By similarity
Glycosylation491N-linked (GlcNAc...) By similarity
Glycosylation761N-linked (GlcNAc...) By similarity
Disulfide bond87 ↔ 184 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q29095 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: A46560DF77E33E72

FASTA18920,568
        10         20         30         40         50         60 
MATPSSLWLG LALLGTLGVL QTPAQASLQP NFQEDKFLGR WFTSGLASNS SWFLEKKKVL 

        70         80         90        100        110        120 
SMCKSLVAPA PDGGFNLTST FLRKDQCVTR TLMLRPAGPP GCYSYTSPHG GSNLEVSVVE 

       130        140        150        160        170        180 
TDYKNYALLH TESGPSPGPA FRMATLYSRS QAPGAAVREK FTAFAKARGF TEDGIVFLPR 


NEKCLEEHE 

« Hide

References

[1]"Constitutive secretion of beta-trace protein by cultivated porcine choroid plexus epithelial cells: elucidation of its complete amino acid and cDNA sequences."
Hoffmann A., Gath U., Gross G., Lauber J., Getclaff R., Hillwig S., Galla H.J., Conradt H.S.
J. Cell. Physiol. 169:235-241(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 27-58; 61-94; 96-123; 125-147; 150-158; 161-166; 169-180 AND 184-189, TISSUE SPECIFICITY.
[2]"Choroid plexus: the major site of mRNA expression for the beta-trace protein (prostaglandin D synthase) in human brain."
Bloedorn B., Maeder M., Urade Y., Hayaishi O., Felgenhauer K., Brueck W.
Neurosci. Lett. 209:117-120(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X92979 mRNA. Translation: CAA63556.1.
RefSeqNP_999393.1. NM_214228.1.
UniGeneSsc.16187.

3D structure databases

ProteinModelPortalQ29095.
SMRQ29095. Positions 27-187.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBQ29095.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID397456.
KEGGssc:397456.

Organism-specific databases

CTD5730.

Phylogenomic databases

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_PIG
AccessionPrimary (citable) accession number: Q29095
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 93 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