Reviewed, UniProtKB/Swiss-Prot O60760 (PTGD2_HUMAN)

Names and origin

Protein names

Recommended name:
    Glutathione-requiring prostaglandin D synthase
    EC=5.3.99.2
Alternative name(s):
    Glutathione-dependent PGD synthetase
    Prostaglandin-H2 D-isomerase
    Hematopoietic prostaglandin D synthase
      Short name=H-PGDS

Gene names

Name:	PTGDS2
Synonyms:	PGDS

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	199 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
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.
Cofactor	Glutathione.
Subcellular location	Cytoplasm.
Tissue specificity	Expressed in a number of megakaryocytic cell lines but not in platelets. Also expressed in placenta.
Developmental stage	Highest levels in immature megakaryocytic cells. Disappears after final differentiation to platelets.
Induction	By 12-O-tetradecanoylphorbol-13-acetate (TPA).
Sequence similarities	Belongs to the GST superfamily. Sigma family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis Prostaglandin biosynthesis
Cellular component	Cytoplasm
Molecular function	Isomerase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	locomotory behavior Traceable author statement. Source: ProtInc prostaglandin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW signal transduction Ref.4 Non-traceable author statement. Source: ProtInc
Cellular component	cytoplasm Ref.4 Traceable author statement. Source: ProtInc
Molecular function	prostaglandin-D synthase activity Ref.4 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 199

198

Glutathione-requiring prostaglandin D synthase

PRO_0000185934

Regions

Domain

2 – 79

78

GST N-terminal

Domain

81 – 199

119

GST C-terminal

Secondary structure

1

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.

.

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199

Helix Strand Turn

Details...

Beta strand

4 – 12

9

Helix

13 – 15

3

Helix

16 – 24

9

Beta strand

30 – 34

5

Helix

36 – 38

3

Helix

39 – 43

5

Beta strand

53 – 56

4

Beta strand

59 – 62

4

Helix

64 – 72

9

Helix

82 – 100

19

Helix

109 – 121

13

Helix

123 – 135

13

Beta strand

139 – 142

4

Helix

148 – 163

16

Turn

165 – 170

6

Helix

172 – 182

11

Helix

185 – 193

9

Sequences

	Sequence		Length	Mass (Da)
	O60760-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: A4ED2476B16CC5C3	FASTA	199	23,344
	10 20 30 40 50 60 MPNYKLTYFN MRGRAEIIRY IFAYLDIQYE DHRIEQADWP EIKSTLPFGK IPILEVDGLT 70 80 90 100 110 120 LHQSLAIARY LTKNTDLAGN TEMEQCHVDA IVDTLDDFMS CFPWAEKKQD VKEQMFNELL 130 140 150 160 170 180 TYNAPHLMQD LDTYLGGREW LIGNSVTWAD FYWEICSTTL LVFKPDLLDN HPRLVTLRKK 190 VQAIPAVANW IKRRPQTKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and chromosomal localization of human and mouse genes for hematopoietic prostaglandin D synthase." Kanaoka Y., Fujimori K., Kikuno R., Sakaguchi Y., Urade Y., Hayaishi O. Eur. J. Biochem. 267:3315-3322(2000) [PubMed: 10824118] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Tissue: Placenta.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[3]	"Induction of hematopoietic prostaglandin D synthase in human megakaryocytic cells by phorbol ester." Suzuki T., Watanabe K., Kanaoka Y., Sato T., Hayaishi O. Biochem. Biophys. Res. Commun. 241:288-293(1997) [PubMed: 9425264] [Abstract] Cited for: CHARACTERIZATION. Tissue: Megakaryocyte.
[4]	"Prostaglandin D synthase in human megakaryoblastic cells." Mahmud I., Ueda N., Yamaguchi H., Yamashita R., Yamamoto S., Kanaoka Y., Urade Y., Hayaishi O. J. Biol. Chem. 272:28263-28266(1997) [PubMed: 9353279] [Abstract] Cited for: CHARACTERIZATION. Tissue: Megakaryocyte.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

D82073 mRNA. Translation: BAA25545.1.
AB008830 Genomic DNA. Translation: BAA96854.1.
BC020734 mRNA. Translation: AAH20734.1.

IPI

IPI00219303.

RefSeq

NP_055300.1.

UniGene

Hs.128433

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IYH	X-ray	1.70	A/B/C/D	2-198	[»]
1IYI	X-ray	1.80	A/B/C/D	2-198	[»]
1V40	X-ray	1.90	A/B/C/D	2-198	[»]
2CVD	X-ray	1.45	A/B/C/D	2-198	[»]
2VCQ	X-ray	1.95	A/B/C/D	1-199	[»]
2VCW	X-ray	1.95	A/B/C/D	1-199	[»]
2VCX	X-ray	2.10	A/B/C/D	1-199	[»]
2VCZ	X-ray	1.95	A/B/C/D	1-199	[»]
2VD0	X-ray	2.20	A/B/C/D	1-199	[»]
2VD1	X-ray	2.25	A/B/C/D	1-199	[»]
3EE2	X-ray	1.91	A/B	1-199	[»]

ModBase

Search...

Proteomic databases

PRIDE

O60760.

Genome annotation databases

Ensembl

ENSG00000163106. Homo sapiens. [Contig view]

GeneID

27306.

KEGG

hsa:27306.

UCSC

uc003hte.1. human.

Organism-specific databases

GeneCards

GC04M095522.

H-InvDB

HIX0020826.

MIM

602598. gene.

Phylogenomic databases

HOGENOM

O60760.

HOVERGEN

O60760.

OMA

O60760. PDLLDIH.

Enzyme and pathway databases

BRENDA

5.3.99.2. 247.

Gene expression databases

ArrayExpress

O60760.

Bgee

O60760.

GermOnline

ENSG00000163106. Homo sapiens.

Family and domain databases

InterPro

IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR004046. GST_C.
IPR012335. Thioredoxin_fold.
[Graphical view]

Gene3D

G3DSA:1.20.1050.10. GST_C_like. 1 hit.
G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

Pfam

PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]

PROSITE

PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

BindingDB

O60760.

DrugBank

DB00143. Glutathione.

NextBio

50305.

SOURCE

Search...

Entry information

Entry name

PTGD2_HUMAN

Accession

Primary (citable) accession number: O60760

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 23, 2007
Last modified:	July 7, 2009
This is version 88 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)