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Protein

Prostaglandin-H2 D-isomerase

Gene

Ptgds

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 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.8 Publications

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.2 Publications

Kineticsi

  1. KM=0.8 µM for prostaglandin H21 Publication
  1. Vmax=5.9 µmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei65Nucleophile1

GO - Molecular functioni

  • fatty acid binding Source: MGI
  • prostaglandin-D synthase activity Source: UniProtKB
  • retinoid binding Source: UniProtKB
  • small molecule binding Source: InterPro
  • transporter activity Source: UniProtKB

GO - Biological processi

  • negative regulation of male germ cell proliferation Source: MGI
  • prostaglandin biosynthetic process Source: UniProtKB
  • regulation of circadian sleep/wake cycle, sleep Source: UniProtKB
  • response to glucocorticoid Source: Ensembl
  • 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

Enzyme and pathway databases

BRENDAi5.3.99.2. 3474.
ReactomeiR-MMU-2162123. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).

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:
L-PGDS
Short name:
PGD2 synthase
Short name:
PGDS2
Gene namesi
Name:Ptgds
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:99261. Ptgds.

Subcellular locationi

  • 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).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Golgi apparatus, Membrane, Nucleus, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi45S → A: Reduces enzyme activity by about half. Reduces enzyme activity tenfold; when associated with A-67 and A-81. 1 Publication1
Mutagenesisi65C → A: Loss of enzyme activity. No effect on ligand binding. 1 Publication1
Mutagenesisi67T → A: Reduces enzyme activity by about half. Reduces enzyme activity tenfold; when associated with A-45 and A-81. 1 Publication1
Mutagenesisi81S → A: Slightly reduced enzyme activity. half. Reduces enzyme activity tenfold; when associated with A-45 and A-67. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL4334.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24By similarityAdd BLAST24
ChainiPRO_000001794725 – 189Prostaglandin-H2 D-isomeraseAdd BLAST165

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei25Pyrrolidone carboxylic acidBy similarity1
Glycosylationi51N-linked (GlcNAc...)By similarity1
Glycosylationi78N-linked (GlcNAc...)By similarity1
Disulfide bondi89 ↔ 1861 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiO09114.
PeptideAtlasiO09114.
PRIDEiO09114.

PTM databases

PhosphoSitePlusiO09114.

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. In the male reproductive system, it is expressed in the testis, efferent ducts and epididymis, and is secreted into the seminal fluid. In the eye, it is expressed in the pigmented epithelium of the retina and the nonpigmented epithelium of the ciliary body, and secreted into the aqueous humor. Low levels detected in various tissue fluids such as serum, normal urine, ascitic fluid and tear fluid. Also found in a number of other organs including the ear, heart and lung.4 Publications

Developmental stagei

Initially detected at 14.5 dpc in the mesenchymal cells of the brain. Later in development, observed in the choroid plexus and within single cells in the brain.

Inductioni

By IL-1 beta and thyroid hormone. Probably induced by dexamethasone, dihydrotestosterone, progesterone, retinoic acid and retinal. Repressed by the Notch-Hes signaling pathway.1 Publication

Gene expression databases

BgeeiENSMUSG00000015090.
CleanExiMM_PTGDS.
GenevisibleiO09114. MM.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000015234.

Chemistry databases

BindingDBiO09114.

Structurei

Secondary structure

1189
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi27 – 29Combined sources3
Helixi36 – 39Combined sources4
Beta strandi41 – 50Combined sources10
Helixi55 – 58Combined sources4
Turni59 – 61Combined sources3
Beta strandi66 – 71Combined sources6
Beta strandi75 – 85Combined sources11
Beta strandi89 – 98Combined sources10
Beta strandi104 – 107Combined sources4
Beta strandi110 – 113Combined sources4
Beta strandi116 – 124Combined sources9
Turni125 – 127Combined sources3
Beta strandi128 – 134Combined sources7
Turni137 – 140Combined sources4
Beta strandi144 – 154Combined sources11
Helixi157 – 169Combined sources13
Helixi174 – 176Combined sources3
Beta strandi177 – 179Combined sources3
Beta strandi184 – 187Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CZTX-ray2.00A25-189[»]
2CZUX-ray2.10A/B25-189[»]
2E4JNMR-A25-189[»]
2KTDNMR-A25-189[»]
2RQ0NMR-A25-189[»]
ProteinModelPortaliO09114.
SMRiO09114.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO09114.

Family & Domainsi

Domaini

Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.3 Publications

Sequence similaritiesi

Belongs to the calycin superfamily. Lipocalin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410II11. Eukaryota.
ENOG4111YRI. LUCA.
GeneTreeiENSGT00620000088005.
HOGENOMiHOG000231660.
HOVERGENiHBG106490.
InParanoidiO09114.
KOiK01830.
OMAiKGPGQDF.
OrthoDBiEOG091G0NAJ.
PhylomeDBiO09114.
TreeFamiTF336103.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022272. Lipocalin_CS.
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.
PROSITEiPS00213. LIPOCALIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O09114-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAALRMLWMG LVLLGLLGFP QTPAQGHDTV QPNFQQDKFL GRWYSAGLAS
60 70 80 90 100
NSSWFREKKA VLYMCKTVVA PSTEGGLNLT STFLRKNQCE TKIMVLQPAG
110 120 130 140 150
APGHYTYSSP HSGSIHSVSV VEANYDEYAL LFSRGTKGPG QDFRMATLYS
160 170 180
RTQTLKDELK EKFTTFSKAQ GLTEEDIVFL PQPDKCIQE
Length:189
Mass (Da):21,066
Last modified:July 1, 1997 - v1
Checksum:iC2C0B3E3B5928643
GO
Isoform 2 (identifier: O09114-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-63: Missing.

Note: No experimental confirmation available.
Show »
Length:126
Mass (Da):13,941
Checksum:i7F9FEDCFBEFF99A6
GO

Sequence cautioni

The sequence BAA21769 differs from that shown. Reason: Frameshift at position 47.Curated

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0410291 – 63Missing in isoform 2. 1 PublicationAdd BLAST63

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X89222 mRNA. Translation: CAA61506.1.
Y10138 Genomic DNA. Translation: CAA71226.1.
AB006361 mRNA. Translation: BAA21769.1. Frameshift.
D83329 Genomic DNA. Translation: BAA74461.1.
AK131859 mRNA. Translation: BAE20833.1.
CH466542 Genomic DNA. Translation: EDL08250.1.
CH466542 Genomic DNA. Translation: EDL08251.1.
BC038083 mRNA. Translation: AAH38083.1.
BC043015 mRNA. Translation: AAH43015.1.
CCDSiCCDS38074.1. [O09114-1]
PIRiS57748.
RefSeqiNP_032989.2. NM_008963.2. [O09114-1]
XP_006497849.1. XM_006497786.3. [O09114-1]
XP_006497850.1. XM_006497787.3. [O09114-1]
UniGeneiMm.1008.

Genome annotation databases

EnsembliENSMUST00000015234; ENSMUSP00000015234; ENSMUSG00000015090. [O09114-1]
ENSMUST00000114251; ENSMUSP00000109889; ENSMUSG00000015090. [O09114-1]
ENSMUST00000114259; ENSMUSP00000109897; ENSMUSG00000015090. [O09114-1]
GeneIDi19215.
KEGGimmu:19215.
UCSCiuc008isf.1. mouse. [O09114-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X89222 mRNA. Translation: CAA61506.1.
Y10138 Genomic DNA. Translation: CAA71226.1.
AB006361 mRNA. Translation: BAA21769.1. Frameshift.
D83329 Genomic DNA. Translation: BAA74461.1.
AK131859 mRNA. Translation: BAE20833.1.
CH466542 Genomic DNA. Translation: EDL08250.1.
CH466542 Genomic DNA. Translation: EDL08251.1.
BC038083 mRNA. Translation: AAH38083.1.
BC043015 mRNA. Translation: AAH43015.1.
CCDSiCCDS38074.1. [O09114-1]
PIRiS57748.
RefSeqiNP_032989.2. NM_008963.2. [O09114-1]
XP_006497849.1. XM_006497786.3. [O09114-1]
XP_006497850.1. XM_006497787.3. [O09114-1]
UniGeneiMm.1008.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CZTX-ray2.00A25-189[»]
2CZUX-ray2.10A/B25-189[»]
2E4JNMR-A25-189[»]
2KTDNMR-A25-189[»]
2RQ0NMR-A25-189[»]
ProteinModelPortaliO09114.
SMRiO09114.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000015234.

Chemistry databases

BindingDBiO09114.
ChEMBLiCHEMBL4334.

PTM databases

PhosphoSitePlusiO09114.

Proteomic databases

PaxDbiO09114.
PeptideAtlasiO09114.
PRIDEiO09114.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000015234; ENSMUSP00000015234; ENSMUSG00000015090. [O09114-1]
ENSMUST00000114251; ENSMUSP00000109889; ENSMUSG00000015090. [O09114-1]
ENSMUST00000114259; ENSMUSP00000109897; ENSMUSG00000015090. [O09114-1]
GeneIDi19215.
KEGGimmu:19215.
UCSCiuc008isf.1. mouse. [O09114-1]

Organism-specific databases

CTDi5730.
MGIiMGI:99261. Ptgds.

Phylogenomic databases

eggNOGiENOG410II11. Eukaryota.
ENOG4111YRI. LUCA.
GeneTreeiENSGT00620000088005.
HOGENOMiHOG000231660.
HOVERGENiHBG106490.
InParanoidiO09114.
KOiK01830.
OMAiKGPGQDF.
OrthoDBiEOG091G0NAJ.
PhylomeDBiO09114.
TreeFamiTF336103.

Enzyme and pathway databases

BRENDAi5.3.99.2. 3474.
ReactomeiR-MMU-2162123. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).

Miscellaneous databases

EvolutionaryTraceiO09114.
PROiO09114.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000015090.
CleanExiMM_PTGDS.
GenevisibleiO09114. MM.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022272. Lipocalin_CS.
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.
PROSITEiPS00213. LIPOCALIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPTGDS_MOUSE
AccessioniPrimary (citable) accession number: O09114
Secondary accession number(s): O09157
, O35091, Q3V2G5, Q62169
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: November 2, 2016
This is version 148 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.