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Protein

Prostaglandin-H2 D-isomerase

Gene

PTGDS

Organism
Homo sapiens (Human)
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.2 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.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei65Nucleophile1

GO - Molecular functioni

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

GO - Biological processi

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

BioCyciMetaCyc:HS02989-MONOMER.
ZFISH:HS02989-MONOMER.
BRENDAi5.3.99.2. 2681.
ReactomeiR-HSA-2162123. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).

Chemistry databases

SwissLipidsiSLP:000000141.

Names & Taxonomyi

Protein namesi
Recommended name:
Prostaglandin-H2 D-isomerase (EC:5.3.99.2)
Alternative name(s):
Beta-trace protein
Cerebrin-28
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
Synonyms:PDS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:9592. PTGDS.

Subcellular locationi

  • Rough endoplasmic reticulum 1 Publication
  • Nucleus membrane 1 Publication
  • Golgi apparatus 1 Publication
  • Cytoplasmperinuclear region 1 Publication
  • Secreted 1 Publication

  • 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.

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • extracellular space Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • nuclear membrane Source: UniProtKB-SubCell
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • rough endoplasmic reticulum Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi59K → A: Increases enzyme activity about two-fold. 1 Publication1
Mutagenesisi64M → A: Reduces enzyme activity almost ten-fold. 1 Publication1
Mutagenesisi65C → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi79L → A: Reduces enzyme activity over ten-fold. 1 Publication1
Mutagenesisi83F → A: Reduces enzyme activity about five-fold. 1 Publication1
Mutagenesisi131L → A: Reduces enzyme activity almost ten-fold. 1 Publication1
Mutagenesisi149Y → A: Increases enzyme activity about two-fold. 1 Publication1

Organism-specific databases

DisGeNETi5730.
OpenTargetsiENSG00000107317.
PharmGKBiPA33945.

Chemistry databases

ChEMBLiCHEMBL3430865.

Polymorphism and mutation databases

BioMutaiPTGDS.
DMDMi730305.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 227 PublicationsAdd BLAST22
ChainiPRO_000001794523 – 190Prostaglandin-H2 D-isomeraseAdd BLAST168

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi29O-linked (GalNAc...)1 Publication1
Glycosylationi51N-linked (GlcNAc...) (complex)3 Publications1
Glycosylationi78N-linked (GlcNAc...) (complex)5 Publications1
Disulfide bondi89 ↔ 186By similarity

Post-translational modificationi

N- and O-glycosylated. Both N-glycosylation recognition sites are almost quantitatively occupied by N-glycans of the biantennary complex type, with a considerable proportion of structures bearing a bisecting GlcNAc. N-glycan at Asn-78: dHex1Hex5HexNAc4. Agalacto structure as well as sialylated and nonsialylated oligosaccharides bearing alpha2-3- and/or alpha2-6-linked NeuNAc are present.8 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP41222.
PeptideAtlasiP41222.
PRIDEiP41222.

2D gel databases

UCD-2DPAGEP41222.

PTM databases

iPTMnetiP41222.
PhosphoSitePlusiP41222.
UniCarbKBiP41222.

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. Abundantly expressed in the heart. In the male reproductive system, it is expressed in the testis, epididymis and prostate, and is secreted into the seminal fluid. Expressed in the eye and secreted into the aqueous humor. Lower 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 ovary, fimbriae of the fallopian tubes, kidney, leukocytes.9 Publications

Developmental stagei

Expression in the amniotic fluid increases dramatically during weeks 12 to 25 of pregnancy. Levels decrease slowly after 25 weeks.1 Publication

Inductioni

By IL1B/interleukin-1 beta and thyroid hormone. Probably induced by dexamethasone, dihydrotestosterone (DHT), progesterone, retinoic acid and retinal. Repressed by the Notch-Hes signaling pathway.1 Publication

Gene expression databases

BgeeiENSG00000107317.
CleanExiHS_PTGDS.
ExpressionAtlasiP41222. baseline and differential.
GenevisibleiP41222. HS.

Organism-specific databases

HPAiCAB009916.
HPA004938.

Interactioni

Subunit structurei

Monomer.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
KRTAP10-7P604093EBI-948821,EBI-10172290

Protein-protein interaction databases

BioGridi111702. 20 interactors.
IntActiP41222. 15 interactors.
MINTiMINT-2862256.
STRINGi9606.ENSP00000360687.

Chemistry databases

BindingDBiP41222.

Structurei

Secondary structure

1190
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi36 – 39Combined sources4
Beta strandi41 – 51Combined sources11
Helixi53 – 60Combined sources8
Beta strandi62 – 71Combined sources10
Beta strandi75 – 85Combined sources11
Beta strandi88 – 98Combined sources11
Beta strandi104 – 108Combined sources5
Turni110 – 112Combined sources3
Beta strandi115 – 123Combined sources9
Beta strandi125 – 138Combined sources14
Helixi139 – 142Combined sources4
Beta strandi144 – 154Combined sources11
Helixi157 – 169Combined sources13
Helixi174 – 176Combined sources3
Beta strandi177 – 179Combined sources3
Beta strandi184 – 186Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WWPX-ray2.00A/B23-190[»]
3O19X-ray1.66A29-190[»]
3O22X-ray1.40A29-190[»]
3O2YX-ray1.70A/B29-190[»]
4IMNX-ray2.09A23-190[»]
4IMOX-ray1.88A23-190[»]
4ORRX-ray1.40A1-190[»]
4ORSX-ray1.40A/B1-190[»]
4ORUX-ray1.55A/B1-190[»]
4ORWX-ray1.66A/B1-190[»]
4ORXX-ray1.60A/B1-190[»]
4ORYX-ray1.80A/B/C/D/E/F/G/H1-190[»]
4OS0X-ray1.75A/B1-190[»]
4OS3X-ray1.40A/B1-190[»]
4OS8X-ray1.69A/B1-190[»]
ProteinModelPortaliP41222.
SMRiP41222.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP41222.

Family & Domainsi

Domaini

Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.1 Publication

Sequence similaritiesi

Belongs to the calycin superfamily. Lipocalin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410II11. Eukaryota.
ENOG4111YRI. LUCA.
GeneTreeiENSGT00620000088005.
HOVERGENiHBG106490.
InParanoidiP41222.
KOiK01830.
OMAiKGPGQDF.
PhylomeDBiP41222.
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]

Sequencei

Sequence statusi: Complete.

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

P41222-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATHHTLWMG LALLGVLGDL QAAPEAQVSV QPNFQQDKFL GRWFSAGLAS
60 70 80 90 100
NSSWLREKKA ALSMCKSVVA PATDGGLNLT STFLRKNQCE TRTMLLQPAG
110 120 130 140 150
SLGSYSYRSP HWGSTYSVSV VETDYDQYAL LYSQGSKGPG EDFRMATLYS
160 170 180 190
RTQTPRAELK EKFTAFCKAQ GFTEDTIVFL PQTDKCMTEQ
Length:190
Mass (Da):21,029
Last modified:February 1, 1995 - v1
Checksum:iDF35FE48AD0D5EF3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti25E → P AA sequence (PubMed:8336140).Curated1
Sequence conflicti33N → L AA sequence (PubMed:9844724).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00427356R → Q.Corresponds to variant rs11552179dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61900 mRNA. Translation: AAA36494.2.
M98538, M98537 Genomic DNA. Translation: AAB51074.1.
AY026356 mRNA. Translation: AAK07679.1.
DQ297141 Genomic DNA. Translation: ABB84464.1.
AK312817 mRNA. Translation: BAG35674.1.
AK075333 mRNA. Translation: BAG52113.1.
AL807752 Genomic DNA. Translation: CAI12758.1.
CH471090 Genomic DNA. Translation: EAW88321.1.
BC005939 mRNA. Translation: AAH05939.1.
BT019921 mRNA. Translation: AAV38724.1.
BT019922 mRNA. Translation: AAV38725.1.
CCDSiCCDS7019.1.
PIRiA44455.
PH1567.
RefSeqiNP_000945.3. NM_000954.5.
UniGeneiHs.446429.

Genome annotation databases

EnsembliENST00000371625; ENSP00000360687; ENSG00000107317.
ENST00000471521; ENSP00000435033; ENSG00000107317.
GeneIDi5730.
KEGGihsa:5730.
UCSCiuc004cke.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61900 mRNA. Translation: AAA36494.2.
M98538, M98537 Genomic DNA. Translation: AAB51074.1.
AY026356 mRNA. Translation: AAK07679.1.
DQ297141 Genomic DNA. Translation: ABB84464.1.
AK312817 mRNA. Translation: BAG35674.1.
AK075333 mRNA. Translation: BAG52113.1.
AL807752 Genomic DNA. Translation: CAI12758.1.
CH471090 Genomic DNA. Translation: EAW88321.1.
BC005939 mRNA. Translation: AAH05939.1.
BT019921 mRNA. Translation: AAV38724.1.
BT019922 mRNA. Translation: AAV38725.1.
CCDSiCCDS7019.1.
PIRiA44455.
PH1567.
RefSeqiNP_000945.3. NM_000954.5.
UniGeneiHs.446429.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WWPX-ray2.00A/B23-190[»]
3O19X-ray1.66A29-190[»]
3O22X-ray1.40A29-190[»]
3O2YX-ray1.70A/B29-190[»]
4IMNX-ray2.09A23-190[»]
4IMOX-ray1.88A23-190[»]
4ORRX-ray1.40A1-190[»]
4ORSX-ray1.40A/B1-190[»]
4ORUX-ray1.55A/B1-190[»]
4ORWX-ray1.66A/B1-190[»]
4ORXX-ray1.60A/B1-190[»]
4ORYX-ray1.80A/B/C/D/E/F/G/H1-190[»]
4OS0X-ray1.75A/B1-190[»]
4OS3X-ray1.40A/B1-190[»]
4OS8X-ray1.69A/B1-190[»]
ProteinModelPortaliP41222.
SMRiP41222.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111702. 20 interactors.
IntActiP41222. 15 interactors.
MINTiMINT-2862256.
STRINGi9606.ENSP00000360687.

Chemistry databases

BindingDBiP41222.
ChEMBLiCHEMBL3430865.
SwissLipidsiSLP:000000141.

PTM databases

iPTMnetiP41222.
PhosphoSitePlusiP41222.
UniCarbKBiP41222.

Polymorphism and mutation databases

BioMutaiPTGDS.
DMDMi730305.

2D gel databases

UCD-2DPAGEP41222.

Proteomic databases

PaxDbiP41222.
PeptideAtlasiP41222.
PRIDEiP41222.

Protocols and materials databases

DNASUi5730.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371625; ENSP00000360687; ENSG00000107317.
ENST00000471521; ENSP00000435033; ENSG00000107317.
GeneIDi5730.
KEGGihsa:5730.
UCSCiuc004cke.4. human.

Organism-specific databases

CTDi5730.
DisGeNETi5730.
GeneCardsiPTGDS.
HGNCiHGNC:9592. PTGDS.
HPAiCAB009916.
HPA004938.
MIMi176803. gene.
neXtProtiNX_P41222.
OpenTargetsiENSG00000107317.
PharmGKBiPA33945.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410II11. Eukaryota.
ENOG4111YRI. LUCA.
GeneTreeiENSGT00620000088005.
HOVERGENiHBG106490.
InParanoidiP41222.
KOiK01830.
OMAiKGPGQDF.
PhylomeDBiP41222.
TreeFamiTF336103.

Enzyme and pathway databases

BioCyciMetaCyc:HS02989-MONOMER.
ZFISH:HS02989-MONOMER.
BRENDAi5.3.99.2. 2681.
ReactomeiR-HSA-2162123. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).

Miscellaneous databases

ChiTaRSiPTGDS. human.
EvolutionaryTraceiP41222.
GeneWikiiProstaglandin_D2_synthase.
GenomeRNAii5730.
PROiP41222.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000107317.
CleanExiHS_PTGDS.
ExpressionAtlasiP41222. baseline and differential.
GenevisibleiP41222. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: P41222
Secondary accession number(s): B2R727
, Q5SQ10, Q7M4P3, Q9UC22, Q9UCC9, Q9UCD9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 30, 2016
This is version 169 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

It has been proposed that the urinary and serum levels may provide a sensitive indicator of renal damage in diabetes mellitus and hypertension. Elevated levels in the coronary circulation may also be associated with angina. Changes in charge and molecular weight microheterogeneity, due to modification of the N-linked oligosaccharides, may be associated with neurodegenerative disease and multiple sclerosis. Detected in meningioma but not in other brain tumors and may be considered a specific cell marker for meningioma. Expression levels in amniotic fluid are altered in abnormal pregnancies. Levels are lower in pregnancies with trisomic fetuses and fetuses with renal abnormalities.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.