P41222 (PTGDS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	PTGDS
Synonyms:	PDS

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	190 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. 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. Ref.16 Ref.34
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. Ref.34
Subunit structure	Monomer. Ref.34
Subcellular location	Rough endoplasmic reticulum. Nucleus membrane. Golgi apparatus. Cytoplasm › perinuclear region. Secreted. 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. Ref.21
Tissue specificity	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. Ref.13 Ref.16 Ref.17 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25
Developmental stage	Expression in the amniotic fluid increases dramatically during weeks 12 to 25 of pregnancy. Levels decrease slowly after 25 weeks. Ref.19
Induction	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. Ref.26
Domain	Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior. Ref.34
Post-translational modification	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. Ref.12 Ref.13 Ref.32 Ref.33
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.
Sequence similarities	Belongs to the calycin superfamily. Lipocalin family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism Prostaglandin biosynthesis Prostaglandin metabolism Transport
Cellular component	Cytoplasm Endoplasmic reticulum Golgi apparatus Membrane Nucleus Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Isomerase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	prostaglandin biosynthetic process Inferred from direct assay Ref.34. Source: UniProtKB regulation of circadian sleep/wake cycle, sleep Inferred from sequence or structural similarity. Source: UniProtKB response to glucocorticoid stimulus Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi apparatus Inferred from sequence or structural similarity. Source: UniProtKB extracellular space Inferred from direct assay PubMed 19878301. 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 direct assay Ref.21. Source: UniProtKB
Molecular_function	fatty acid binding Inferred from direct assay Ref.34. Source: UniProtKB prostaglandin-D synthase activity Inferred from direct assay Ref.34. 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18

Chain

23 – 190

168

Prostaglandin-H2 D-isomerase

PRO_0000017945

Sites

Active site

65

1

Nucleophile

Amino acid modifications

Glycosylation

29

1

O-linked (GalNAc...) Ref.33

Glycosylation

51

1

N-linked (GlcNAc...) (complex) Ref.12 Ref.30 Ref.31

Glycosylation

78

1

N-linked (GlcNAc...) (complex) Ref.12 Ref.29 Ref.31 Ref.32

Disulfide bond

89 ↔ 186

By similarity

Natural variations

Natural variant

56

1

R → Q.
Corresponds to variant rs11552179 [ dbSNP | Ensembl ].

VAR_004273

Experimental info

Mutagenesis

59

1

K → A: Increases enzyme activity about two-fold. Ref.34

Mutagenesis

64

1

M → A: Reduces enzyme activity almost ten-fold. Ref.34

Mutagenesis

65

1

C → A: Loss of enzyme activity. Ref.34

Mutagenesis

79

1

L → A: Reduces enzyme activity over ten-fold. Ref.34

Mutagenesis

83

1

F → A: Reduces enzyme activity about five-fold. Ref.34

Mutagenesis

131

1

L → A: Reduces enzyme activity almost ten-fold. Ref.34

Mutagenesis

149

1

Y → A: Increases enzyme activity about two-fold. Ref.34

Sequence conflict

25

1

E → P AA sequence Ref.18

Sequence conflict

33

1

N → L AA sequence Ref.17

Secondary structure

1

.

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.

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190

Helix Strand Turn

Details...

Helix

36 – 39

4

Beta strand

41 – 51

11

Helix

53 – 60

8

Beta strand

62 – 71

10

Beta strand

75 – 85

11

Beta strand

88 – 98

11

Beta strand

104 – 108

5

Turn

110 – 113

4

Beta strand

115 – 123

9

Beta strand

125 – 138

14

Helix

139 – 142

4

Beta strand

144 – 154

11

Helix

157 – 169

13

Helix

174 – 176

3

Beta strand

177 – 179

3

Beta strand

184 – 186

3

Sequences

	Sequence		Length	Mass (Da)
	P41222 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: DF35FE48AD0D5EF3	FASTA	190	21,029
	10 20 30 40 50 60 MATHHTLWMG LALLGVLGDL QAAPEAQVSV QPNFQQDKFL GRWFSAGLAS NSSWLREKKA 70 80 90 100 110 120 ALSMCKSVVA PATDGGLNLT STFLRKNQCE TRTMLLQPAG SLGSYSYRSP HWGSTYSVSV 130 140 150 160 170 180 VETDYDQYAL LYSQGSKGPG EDFRMATLYS RTQTPRAELK EKFTAFCKAQ GFTEDTIVFL 190 PQTDKCMTEQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human brain prostaglandin D synthase has been evolutionarily differentiated from lipophilic-ligand carrier proteins." Nagata A., Suzuki Y., Igarashi M., Eguchi N., Toh H., Urade Y., Hayaishi O. Proc. Natl. Acad. Sci. U.S.A. 88:4020-4024(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	Nagata A., Suzuki Y., Igarashi M., Eguchi N., Toh H., Urade Y., Hayaishi O. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 12; 16; 19; 36; 56; 73; 77; 99; 100; 127 AND 176.
[3]	"Structure and chromosomal localization of the human gene for a brain form of prostaglandin D2 synthase." White D.M., Mikol D.D., Espinosa R., Weimer B., le Beau M.M., Stefansson K. J. Biol. Chem. 267:23202-23208(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Brain.
[4]	"cDNA cloning and sequence analysis of prostaglandin D synthase in human testis." Lu J.C., Li X.Y., Huang Y.F., Zhang X.R. (In) Robaire B., Chemes H., Morales C.R. (eds.); Andrology in the 21st century, pp.189-193, Medimond Publishing Company Inc., Englewood (2001) Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis.
[5]	SeattleSNPs variation discovery resource Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[7]	"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries." Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T. DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[9]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Prostate.
[12]	"Purification and chemical characterization of beta-trace protein from human cerebrospinal fluid: its identification as prostaglandin D synthase." Hoffmann A., Conradt H.S., Gross G., Nimtz M., Lottspeich F., Wurster U. J. Neurochem. 61:451-456(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-190, GLYCOSYLATION AT ASN-51 AND ASN-78. Tissue: Cerebrospinal fluid.
[13]	"Identification of a brain-specific human cerebrospinal fluid glycoprotein, beta-trace protein." Harrington M.G., Aebersold R., Martin B.M., Merril C.R., Hood L. Appl. Theor. Electrophor. 3:229-234(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-37; 67-77; 117-126 AND 169-178, TISSUE SPECIFICITY, GLYCOSYLATION. Tissue: Cerebrospinal fluid.
[14]	"Purification and N-terminal sequence of beta-trace, a protein abundant in human cerebrospinal fluid." Zahn M., Maeder M., Schmidt B., Bollensen E., Felgenhauer K. Neurosci. Lett. 154:93-95(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-50. Tissue: Cerebrospinal fluid.
[15]	"Isolation and amino terminal sequence of beta-trace, a novel protein from human cerebrospinal fluid." Kuruvilla A.P., Hochwald G.M., Ghiso J., Castano E.M., Pizzolato M., Frangione B. Brain Res. 565:337-340(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-41. Tissue: Cerebrospinal fluid.
[16]	"Lipocalin-type prostaglandin D synthase in human male reproductive organs and seminal plasma." Tokugawa Y., Kunishige I., Kubota Y., Shimoya K., Nobunaga T., Kimura T., Saji F., Murata Y., Eguchi N., Oda H., Urade Y., Hayaishi O. Biol. Reprod. 58:600-607(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-38, FUNCTION, TISSUE SPECIFICITY. Tissue: Seminal plasma.
[17]	"Quantification of prostaglandin D synthetase in cerebrospinal fluid: a potential marker for brain tumor." Saso L., Leone M.G., Sorrentino C., Giacomelli S., Silvestrini B., Grima J., Li J.C.H., Samy E., Mruk D., Cheng C.Y. Biochem. Mol. Biol. Int. 46:643-656(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-35, TISSUE SPECIFICITY, USE AS A MARKER FOR BRAIN TUMOR.
[18]	"Micropurification of two human cerebrospinal fluid proteins by high performance electrophoresis chromatography." Leone M.G., Saso L., Del Vecchio A., Mo M., Silvestrini B., Cheng C.Y. J. Neurochem. 61:533-540(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-34. Tissue: Cerebrospinal fluid.
[19]	"Prostaglandin D2 synthase: a component of human amniotic fluid and its association with fetal abnormalities." Melegos D.N., Yu H., Diamandis E.P. Clin. Chem. 42:1042-1050(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 30-44, DEVELOPMENTAL STAGE, EXPRESSION IN ABNORMAL PREGNANCIES. Tissue: Amniotic fluid.
[20]	"Astrocytes synthesize and secrete prostaglandin D synthetase in vitro." Giacomelli S., Leone M.-G., Grima J., Silvestrini B., Cheng C.Y. Biochim. Biophys. Acta 1310:269-276(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 58-73 AND 123-140, TISSUE SPECIFICITY. Tissue: Cerebrospinal fluid.
[21]	"Prostaglandin D synthase (beta-trace) in human arachnoid and meningioma cells: roles as a cell marker or in cerebrospinal fluid absorption, tumorigenesis, and calcification process." Yamashima T., Sakuda K., Tohma Y., Yamashita J., Oda H., Irikura D., Eguchi N., Beuckmann C.T., Kanaoka Y., Urade Y., Hayaishi O. J. Neurosci. 17:2376-2382(1997) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, USE AS A MARKER FOR MENINGIOMA.
[22]	"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.
[23]	"Expression of lipocalin-type prostaglandin D synthase (beta-trace) in human heart and its accumulation in the coronary circulation of angina patients." Eguchi Y., Eguchi N., Oda H., Seiki K., Kijima Y., Matsu-ura Y., Urade Y., Hayaishi O. Proc. Natl. Acad. Sci. U.S.A. 94:14689-14694(1997) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[24]	"Expression of the beta-trace protein in human pachymeninx as revealed by in situ hybridization and immunocytochemistry." Bloedorn B., Brueck W., Tumani H., Michel U., Rieckmann P., Althans N., Maeder M. J. Neurosci. Res. 57:730-734(1999) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[25]	"Lipocalin-type prostaglandin D synthase in essential hypertension." Hirawa N., Uehara Y., Yamakado M., Toya Y., Gomi T., Ikeda T., Eguchi Y., Takagi M., Oda H., Seiki K., Urade Y., Umemura S. Hypertension 39:449-454(2002) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, USE AS A MARKER FOR RENAL INJURY IN HYPERTENSION.
[26]	"Beta-trace gene expression is regulated by a core promoter and a distal thyroid hormone response element." White D.M., Takeda T., DeGroot L.J., Stefansson K., Arnason B.G.W. J. Biol. Chem. 272:14387-14393(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY THYROID HORMONE.
[27]	"Charge microheterogeneity of the beta-trace proteins (lipocalin-type prostaglandin D synthase) in the cerebrospinal fluid of patients with neurological disorders analyzed by capillary isoelectrofocusing." Hiraoka A., Seiki K., Oda H., Eguchi N., Urade Y., Tominaga I., Baba K. Electrophoresis 22:3433-3437(2001) [PubMed] [Europe PMC] [Abstract] Cited for: USE AS A MARKER FOR NEUROLOGICAL DISORDERS.
[28]	"Urinary prostaglandin D synthase (beta-trace) excretion increases in the early stage of diabetes mellitus." Hirawa N., Uehara Y., Ikeda T., Gomi T., Hamano K., Totsuka Y., Yamakado M., Takagi M., Eguchi N., Oda H., Seiki K., Nakajima H., Urade Y. Nephron 87:321-327(2001) [PubMed] [Europe PMC] [Abstract] Cited for: USE AS A MARKER FOR RENAL INJURY IN DIABETES MELLITUS.
[29]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78, MASS SPECTROMETRY. Tissue: Plasma.
[30]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-51, MASS SPECTROMETRY. Tissue: Liver.
[31]	"Enrichment of glycopeptides for glycan structure and attachment site identification." Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G. Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-51 AND ASN-78, STRUCTURE OF CARBOHYDRATES, MASS SPECTROMETRY. Tissue: Cerebrospinal fluid.
[32]	"Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD." Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G. Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-78, STRUCTURE OF CARBOHYDRATES, MASS SPECTROMETRY.
[33]	"LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins." Halim A., Ruetschi U., Larson G., Nilsson J. J. Proteome Res. 12:573-584(2013) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT SER-29, MASS SPECTROMETRY.
[34]	"Structure-function analysis of human l-prostaglandin D synthase bound with fatty acid molecules." Zhou Y., Shaw N., Li Y., Zhao Y., Zhang R., Liu Z.J. FASEB J. 24:4668-4677(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 29-190 OF MUTANT ALA-65 IN COMPLEXES WITH FATTY ACIDS, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF LYS-59; MET-64; CYS-65; LEU-79; PHE-83; LEU-131 AND TYR-149, DOMAIN.
[35]	"Crystal structure of the human lipocalin-type prostaglandin D synthase crystallised with the substrate analog 9,11-dideoxy-9alpha,11alpha- epoxymethanoprostaglandin f2alpha." Structural genomics consortium (SGC) Submitted (JAN-2010) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 23-190 IN COMPLEX WITH SUBSTRATE ANALOG.
+	Additional computationally mapped references.

Web resources

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00013179.

PIR

A44455.
PH1567.

RefSeq

NP_000945.3. NM_000954.5.

UniGene

Hs.446429.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2WWP	X-ray	2.00	A/B	23-190	[»]
3O19	X-ray	1.66	A	29-190	[»]
3O22	X-ray	1.40	A	29-190	[»]
3O2Y	X-ray	1.70	A/B	29-190	[»]

ProteinModelPortal

P41222.

ModBase

Search...

Protein-protein interaction databases

IntAct

P41222. 8 interactions.

MINT

MINT-2862256.

STRING

9606.ENSP00000360687.

PTM databases

PhosphoSite

P41222.

Polymorphism databases

DMDM

730305.

2D gel databases

UCD-2DPAGE

P41222.

Proteomic databases

PaxDb

P41222.

PRIDE

P41222.

Protocols and materials databases

DNASU

5730.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000371625; ENSP00000360687; ENSG00000107317.
ENST00000471521; ENSP00000435033; ENSG00000107317.

GeneID

5730.

KEGG

hsa:5730.

UCSC

uc004cke.3. human.

Organism-specific databases

CTD

5730.

GeneCards

GC09P139871.

HGNC

HGNC:9592. PTGDS.

HPA

CAB009916.
HPA004938.

MIM

176803. gene.

neXtProt

NX_P41222.

PharmGKB

PA33945.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG45731.

HOVERGEN

HBG106490.

KO

K01830.

OrthoDB

EOG4DV5NJ.

PhylomeDB

P41222.

Enzyme and pathway databases

BRENDA

5.3.99.2. 2681.

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

P41222.

Bgee

P41222.

CleanEx

HS_PTGDS.

Genevestigator

P41222.

GermOnline

ENSG00000107317. Homo sapiens.

Family and domain databases

Gene3D

2.40.128.20. 1 hit.

InterPro

IPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002972. PstgldnD_synth.
[Graphical view]

Pfam

PF00061. Lipocalin. 1 hit.
[Graphical view]

PRINTS

PR00179. LIPOCALIN.
PR01254. PGNDSYNTHASE.

SUPFAM

SSF50814. Calycin. 1 hit.

PROSITE

PS00213. LIPOCALIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P41222.

ChiTaRS

PTGDS. human.

EvolutionaryTrace

P41222.

GenomeRNAi

5730.

NextBio

22290.

SOURCE

Search...

Entry information

Entry name

PTGDS_HUMAN

Accession

Primary (citable) accession number: P41222
Secondary accession number(s): B2R727 , Q5SQ10, Q7M4P3, Q9UC22, Q9UCC9, Q9UCD9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 135 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.