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P41222 (PTGDS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length190 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.35

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.35

Subunit structure

Monomer. Ref.35

Subcellular location

Rough endoplasmic reticulum. Nucleus membrane. Golgi apparatus. Cytoplasmperinuclear 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.35

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.31 Ref.33 Ref.34

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 processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
Prostaglandin biosynthesis
Prostaglandin metabolism
Transport
   Cellular componentCytoplasm
Endoplasmic reticulum
Golgi apparatus
Membrane
Nucleus
Secreted
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionIsomerase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processarachidonic acid metabolic process

Traceable author statement. Source: Reactome

cyclooxygenase pathway

Traceable author statement. Source: Reactome

prostaglandin biosynthetic process

Inferred from direct assay Ref.35. Source: UniProtKB

regulation of circadian sleep/wake cycle, sleep

Inferred from sequence or structural similarity. Source: UniProtKB

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

transport

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

extracellular region

Inferred from direct assay Ref.13. 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_functionfatty acid binding

Inferred from direct assay Ref.35. Source: UniProtKB

prostaglandin-D synthase activity

Inferred from direct assay Ref.35. Source: UniProtKB

retinoid binding

Inferred from sequence or structural similarity. Source: UniProtKB

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 – 2222 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18
Chain23 – 190168Prostaglandin-H2 D-isomerase
PRO_0000017945

Sites

Active site651Nucleophile

Amino acid modifications

Glycosylation291O-linked (GalNAc...) Ref.34
Glycosylation511N-linked (GlcNAc...) (complex) Ref.12 Ref.30 Ref.32
Glycosylation781N-linked (GlcNAc...) (complex) Ref.12 Ref.29 Ref.31 Ref.32 Ref.33
Disulfide bond89 ↔ 186 By similarity

Natural variations

Natural variant561R → Q.
Corresponds to variant rs11552179 [ dbSNP | Ensembl ].
VAR_004273

Experimental info

Mutagenesis591K → A: Increases enzyme activity about two-fold. Ref.35
Mutagenesis641M → A: Reduces enzyme activity almost ten-fold. Ref.35
Mutagenesis651C → A: Loss of enzyme activity. Ref.35
Mutagenesis791L → A: Reduces enzyme activity over ten-fold. Ref.35
Mutagenesis831F → A: Reduces enzyme activity about five-fold. Ref.35
Mutagenesis1311L → A: Reduces enzyme activity almost ten-fold. Ref.35
Mutagenesis1491Y → A: Increases enzyme activity about two-fold. Ref.35
Sequence conflict251E → P AA sequence Ref.18
Sequence conflict331N → L AA sequence Ref.17

Secondary structure

............................... 190
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P41222 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: DF35FE48AD0D5EF3

FASTA19021,029
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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.
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.
Tissue: Liver.
[31]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-78.
[32]"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.
Tissue: Cerebrospinal fluid.
[33]"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, IDENTIFICATION BY MASS SPECTROMETRY.
[34]"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, IDENTIFICATION BY MASS SPECTROMETRY.
[35]"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.
[36]"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

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.
CCDSCCDS7019.1.
PIRA44455.
PH1567.
RefSeqNP_000945.3. NM_000954.5.
UniGeneHs.446429.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP41222.
SMRP41222. Positions 28-182.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111702. 13 interactions.
IntActP41222. 10 interactions.
MINTMINT-2862256.
STRING9606.ENSP00000360687.

Chemistry

BindingDBP41222.

PTM databases

PhosphoSiteP41222.

Polymorphism databases

DMDM730305.

2D gel databases

UCD-2DPAGEP41222.

Proteomic databases

PaxDbP41222.
PRIDEP41222.

Protocols and materials databases

DNASU5730.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371625; ENSP00000360687; ENSG00000107317.
ENST00000471521; ENSP00000435033; ENSG00000107317.
GeneID5730.
KEGGhsa:5730.
UCSCuc004cke.3. human.

Organism-specific databases

CTD5730.
GeneCardsGC09P139871.
HGNCHGNC:9592. PTGDS.
HPACAB009916.
HPA004938.
MIM176803. gene.
neXtProtNX_P41222.
PharmGKBPA33945.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG45731.
HOVERGENHBG106490.
KOK01830.
PhylomeDBP41222.
TreeFamTF336103.

Enzyme and pathway databases

BioCycMetaCyc:HS02989-MONOMER.
BRENDA5.3.99.2. 2681.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP41222.
BgeeP41222.
CleanExHS_PTGDS.
GenevestigatorP41222.

Family and domain databases

Gene3D2.40.128.20. 1 hit.
InterProIPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022272. Lipocalin_CS.
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.
PROSITEPS00213. LIPOCALIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPTGDS. human.
EvolutionaryTraceP41222.
GeneWikiProstaglandin_D2_synthase.
GenomeRNAi5730.
NextBio22290.
PROP41222.
SOURCESearch...

Entry information

Entry namePTGDS_HUMAN
AccessionPrimary (citable) accession number: P41222
Secondary accession number(s): B2R727 expand/collapse secondary AC list , Q5SQ10, Q7M4P3, Q9UC22, Q9UCC9, Q9UCD9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 9, 2014
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM