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P41222

- PTGDS_HUMAN

UniProt

P41222 - PTGDS_HUMAN

Protein

Prostaglandin-H2 D-isomerase

Gene

PTGDS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    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)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei65 – 651Nucleophile

    GO - Molecular functioni

    1. fatty acid binding Source: UniProtKB
    2. prostaglandin-D synthase activity Source: UniProtKB
    3. retinoid binding Source: UniProtKB
    4. transporter activity Source: UniProtKB

    GO - Biological processi

    1. arachidonic acid metabolic process Source: Reactome
    2. cyclooxygenase pathway Source: Reactome
    3. prostaglandin biosynthetic process Source: UniProtKB
    4. regulation of circadian sleep/wake cycle, sleep Source: UniProtKB
    5. response to glucocorticoid Source: Ensembl
    6. small molecule metabolic process Source: Reactome
    7. transport Source: UniProtKB

    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.
    BRENDAi5.3.99.2. 2681.
    ReactomeiREACT_150149. 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):
    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
    ProteomesiUP000005640: 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

    1. endoplasmic reticulum membrane Source: Reactome
    2. extracellular region Source: UniProtKB
    3. extracellular space Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProt
    5. Golgi apparatus Source: UniProtKB
    6. nuclear membrane Source: UniProtKB-SubCell
    7. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    8. rough endoplasmic reticulum Source: UniProtKB

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi59 – 591K → A: Increases enzyme activity about two-fold. 1 Publication
    Mutagenesisi64 – 641M → A: Reduces enzyme activity almost ten-fold. 1 Publication
    Mutagenesisi65 – 651C → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi79 – 791L → A: Reduces enzyme activity over ten-fold. 1 Publication
    Mutagenesisi83 – 831F → A: Reduces enzyme activity about five-fold. 1 Publication
    Mutagenesisi131 – 1311L → A: Reduces enzyme activity almost ten-fold. 1 Publication
    Mutagenesisi149 – 1491Y → A: Increases enzyme activity about two-fold. 1 Publication

    Organism-specific databases

    PharmGKBiPA33945.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 22227 PublicationsAdd
    BLAST
    Chaini23 – 190168Prostaglandin-H2 D-isomerasePRO_0000017945Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi29 – 291O-linked (GalNAc...)2 Publications
    Glycosylationi51 – 511N-linked (GlcNAc...) (complex)4 Publications
    Glycosylationi78 – 781N-linked (GlcNAc...) (complex)6 Publications
    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.
    PRIDEiP41222.

    2D gel databases

    UCD-2DPAGEP41222.

    PTM databases

    PhosphoSiteiP41222.

    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

    ArrayExpressiP41222.
    BgeeiP41222.
    CleanExiHS_PTGDS.
    GenevestigatoriP41222.

    Organism-specific databases

    HPAiCAB009916.
    HPA004938.

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Protein-protein interaction databases

    BioGridi111702. 13 interactions.
    IntActiP41222. 10 interactions.
    MINTiMINT-2862256.
    STRINGi9606.ENSP00000360687.

    Structurei

    Secondary structure

    1
    190
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi36 – 394
    Beta strandi41 – 5111
    Helixi53 – 608
    Beta strandi62 – 7110
    Beta strandi75 – 8511
    Beta strandi88 – 9811
    Beta strandi104 – 1085
    Turni110 – 1134
    Beta strandi115 – 1239
    Beta strandi125 – 13814
    Helixi139 – 1424
    Beta strandi144 – 15411
    Helixi157 – 16913
    Helixi174 – 1763
    Beta strandi177 – 1793
    Beta strandi184 – 1863

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP41222.
    SMRiP41222. Positions 28-182.
    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

    eggNOGiNOG45731.
    HOVERGENiHBG106490.
    KOiK01830.
    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

    MATHHTLWMG LALLGVLGDL QAAPEAQVSV QPNFQQDKFL GRWFSAGLAS    50
    NSSWLREKKA ALSMCKSVVA PATDGGLNLT STFLRKNQCE TRTMLLQPAG 100
    SLGSYSYRSP HWGSTYSVSV VETDYDQYAL LYSQGSKGPG EDFRMATLYS 150
    RTQTPRAELK EKFTAFCKAQ GFTEDTIVFL PQTDKCMTEQ 190
    Length:190
    Mass (Da):21,029
    Last modified:February 1, 1995 - v1
    Checksum:iDF35FE48AD0D5EF3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251E → P AA sequence (PubMed:8336140)Curated
    Sequence conflicti33 – 331N → L AA sequence (PubMed:9844724)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti56 – 561R → Q.
    Corresponds to variant rs11552179 [ dbSNP | Ensembl ].
    VAR_004273

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.3. human.

    Polymorphism databases

    DMDMi730305.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS7019.1.
    PIRi A44455.
    PH1567.
    RefSeqi NP_000945.3. NM_000954.5.
    UniGenei Hs.446429.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    4IMN X-ray 2.09 A 23-190 [» ]
    4IMO X-ray 1.88 A 23-190 [» ]
    ProteinModelPortali P41222.
    SMRi P41222. Positions 28-182.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111702. 13 interactions.
    IntActi P41222. 10 interactions.
    MINTi MINT-2862256.
    STRINGi 9606.ENSP00000360687.

    Chemistry

    BindingDBi P41222.

    PTM databases

    PhosphoSitei P41222.

    Polymorphism databases

    DMDMi 730305.

    2D gel databases

    UCD-2DPAGE P41222.

    Proteomic databases

    PaxDbi P41222.
    PRIDEi P41222.

    Protocols and materials databases

    DNASUi 5730.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371625 ; ENSP00000360687 ; ENSG00000107317 .
    ENST00000471521 ; ENSP00000435033 ; ENSG00000107317 .
    GeneIDi 5730.
    KEGGi hsa:5730.
    UCSCi uc004cke.3. human.

    Organism-specific databases

    CTDi 5730.
    GeneCardsi GC09P139871.
    HGNCi HGNC:9592. PTGDS.
    HPAi CAB009916.
    HPA004938.
    MIMi 176803. gene.
    neXtProti NX_P41222.
    PharmGKBi PA33945.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG45731.
    HOVERGENi HBG106490.
    KOi K01830.
    PhylomeDBi P41222.
    TreeFami TF336103.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS02989-MONOMER.
    BRENDAi 5.3.99.2. 2681.
    Reactomei REACT_150149. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).

    Miscellaneous databases

    ChiTaRSi PTGDS. human.
    EvolutionaryTracei P41222.
    GeneWikii Prostaglandin_D2_synthase.
    GenomeRNAii 5730.
    NextBioi 22290.
    PROi P41222.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P41222.
    Bgeei P41222.
    CleanExi HS_PTGDS.
    Genevestigatori P41222.

    Family and domain databases

    Gene3Di 2.40.128.20. 1 hit.
    InterProi IPR012674. Calycin.
    IPR011038. Calycin-like.
    IPR002345. Lipocalin.
    IPR022272. Lipocalin_CS.
    IPR000566. Lipocln_cytosolic_FA-bd_dom.
    IPR002972. PstgldnD_synth.
    [Graphical view ]
    Pfami PF00061. Lipocalin. 1 hit.
    [Graphical view ]
    PRINTSi PR00179. LIPOCALIN.
    PR01254. PGNDSYNTHASE.
    SUPFAMi SSF50814. SSF50814. 1 hit.
    PROSITEi PS00213. LIPOCALIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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. 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.

    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: October 1, 2014
    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
    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

    External Data

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