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Protein

Prostaglandin-H2 D-isomerase

Gene

PTGDS

Organism
Sus scrofa (Pig)
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 sitei63 – 631NucleophileBy similarity

GO - Molecular functioni

  1. prostaglandin-D synthase activity Source: UniProtKB
  2. retinoid binding Source: UniProtKB
  3. small molecule binding Source: InterPro
  4. transporter activity Source: UniProtKB

GO - Biological processi

  1. prostaglandin biosynthetic process Source: UniProtKB
  2. regulation of circadian sleep/wake cycle, sleep Source: UniProtKB
  3. transport Source: UniProtKB
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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227 Componenti: Unplaced

Subcellular locationi

  1. Rough endoplasmic reticulum By similarity
  2. Nucleus membrane By similarity
  3. Golgi apparatus By similarity
  4. Cytoplasmperinuclear region By similarity
  5. Secreted By similarity

  6. 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

  1. extracellular region Source: UniProtKB
  2. Golgi apparatus Source: UniProtKB
  3. nuclear membrane Source: UniProtKB-SubCell
  4. perinuclear region of cytoplasm Source: UniProtKB-SubCell
  5. rough endoplasmic reticulum Source: UniProtKB
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 – 189165Prostaglandin-H2 D-isomerasePRO_0000017948Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251Pyrrolidone carboxylic acidBy similarity
Glycosylationi49 – 491N-linked (GlcNAc...)By similarity
Glycosylationi76 – 761N-linked (GlcNAc...)By similarity
Disulfide bondi87 ↔ 184By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Expressioni

Tissue specificityi

Abundant in the brain and CNS, where it is expressed in tissues of the blood-brain barrier and secreted into the cerebro-spinal fluid.2 Publications

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ29095.
SMRiQ29095. Positions 27-187.
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.
InParanoidiQ29095.
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.

Q29095-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATPSSLWLG LALLGTLGVL QTPAQASLQP NFQEDKFLGR WFTSGLASNS
60 70 80 90 100
SWFLEKKKVL SMCKSLVAPA PDGGFNLTST FLRKDQCVTR TLMLRPAGPP
110 120 130 140 150
GCYSYTSPHG GSNLEVSVVE TDYKNYALLH TESGPSPGPA FRMATLYSRS
160 170 180
QAPGAAVREK FTAFAKARGF TEDGIVFLPR NEKCLEEHE
Length:189
Mass (Da):20,568
Last modified:November 1, 1996 - v1
Checksum:iA46560DF77E33E72
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92979 mRNA. Translation: CAA63556.1.
RefSeqiNP_999393.1. NM_214228.1.
UniGeneiSsc.16187.

Genome annotation databases

GeneIDi397456.
KEGGissc:397456.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92979 mRNA. Translation: CAA63556.1.
RefSeqiNP_999393.1. NM_214228.1.
UniGeneiSsc.16187.

3D structure databases

ProteinModelPortaliQ29095.
SMRiQ29095. Positions 27-187.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiQ29095.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397456.
KEGGissc:397456.

Organism-specific databases

CTDi5730.

Phylogenomic databases

HOVERGENiHBG106490.
InParanoidiQ29095.
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. "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.

Entry informationi

Entry nameiPTGDS_PIG
AccessioniPrimary (citable) accession number: Q29095
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: March 4, 2015
This is version 97 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.