Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q29562 (PTGDS_URSAR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 83. 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
OrganismUrsus arctos (Brown bear) (Grizzly bear)
Taxonomic identifier9644 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaUrsidaeUrsus

Protein attributes

Sequence length191 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.

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
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

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 – 191167Prostaglandin-H2 D-isomerase
PRO_0000017952

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 ↔ 186 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q29562 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 117387F7B94B9EE3

FASTA19121,415
        10         20         30         40         50         60 
MAALHTLWMG LVLLGVLGVL QTQAQVQVSL QPNFQQDKFL GRWFTSGLAS NSSWFREKKK 

        70         80         90        100        110        120 
VLSMCVSVVA PSADGGLNLT STFLRKEQCE TRTLLLRPAG TPGCYSYTSP HWGSTHDVWV 

       130        140        150        160        170        180 
AMTDYDEYAL LYTTGTKGLG QDFHMATLYS RTQTPRAEIK EKFTTFAKTQ GFTEDAIVFL 

       190 
PQTDKCMEEH K 

« Hide

References

[1]Irikura D., Maruyama T., Kanaoka Y., Urade Y.
Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Arachnoid membrane.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D82047 mRNA. Translation: BAA11520.1.

3D structure databases

ProteinModelPortalQ29562.
SMRQ29562. Positions 24-189.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG106490.

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_URSAR
AccessionPrimary (citable) accession number: Q29562
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 83 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