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O09114

- PTGDS_MOUSE

UniProt

O09114 - PTGDS_MOUSE

Protein

Prostaglandin-H2 D-isomerase

Gene

Ptgds

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      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.8 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.2 Publications

    Kineticsi

    1. KM=0.8 µM for prostaglandin H21 Publication

    Vmax=5.9 µmol/min/mg enzyme1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei65 – 651Nucleophile

    GO - Molecular functioni

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

    GO - Biological processi

    1. prostaglandin biosynthetic process Source: UniProtKB
    2. regulation of circadian sleep/wake cycle, sleep Source: UniProtKB
    3. response to glucocorticoid Source: Ensembl
    4. 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

    BRENDAi5.3.99.2. 3474.
    ReactomeiREACT_188623. 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):
    Glutathione-independent PGD synthase
    Lipocalin-type prostaglandin-D synthase
    Prostaglandin-D2 synthase
    Short name:
    L-PGDS
    Short name:
    PGD2 synthase
    Short name:
    PGDS2
    Gene namesi
    Name:Ptgds
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:99261. Ptgds.

    Subcellular locationi

    Rough endoplasmic reticulum By similarity. Nucleus membrane By similarity. Golgi apparatus By similarity. Cytoplasmperinuclear region By similarity. Secreted By similarity
    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 By similarity.By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB
    2. extracellular space Source: Ensembl
    3. Golgi apparatus Source: UniProtKB
    4. nuclear membrane Source: UniProtKB-SubCell
    5. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    6. 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
    Mutagenesisi45 – 451S → A: Reduces enzyme activity by about half. Reduces enzyme activity tenfold; when associated with A-67 and A-81. 1 Publication
    Mutagenesisi65 – 651C → A: Loss of enzyme activity. No effect on ligand binding. 1 Publication
    Mutagenesisi67 – 671T → A: Reduces enzyme activity by about half. Reduces enzyme activity tenfold; when associated with A-45 and A-81. 1 Publication
    Mutagenesisi81 – 811S → A: Slightly reduced enzyme activity. half. Reduces enzyme activity tenfold; when associated with A-45 and A-67. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424By similarityAdd
    BLAST
    Chaini25 – 189165Prostaglandin-H2 D-isomerasePRO_0000017947Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei25 – 251Pyrrolidone carboxylic acidBy similarity
    Glycosylationi51 – 511N-linked (GlcNAc...)By similarity
    Glycosylationi78 – 781N-linked (GlcNAc...)By similarity
    Disulfide bondi89 ↔ 1861 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

    Proteomic databases

    MaxQBiO09114.
    PaxDbiO09114.
    PRIDEiO09114.

    PTM databases

    PhosphoSiteiO09114.

    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. In the male reproductive system, it is expressed in the testis, efferent ducts and epididymis, and is secreted into the seminal fluid. In the eye, it is expressed in the pigmented epithelium of the retina and the nonpigmented epithelium of the ciliary body, and secreted into the aqueous humor. Low 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 the ear, heart and lung.4 Publications

    Developmental stagei

    Initially detected at 14.5 dpc in the mesenchymal cells of the brain. Later in development, observed in the choroid plexus and within single cells in the brain.

    Inductioni

    By IL-1 beta and thyroid hormone. Probably induced by dexamethasone, dihydrotestosterone, progesterone, retinoic acid and retinal. Repressed by the Notch-Hes signaling pathway.1 Publication

    Gene expression databases

    BgeeiO09114.
    CleanExiMM_PTGDS.
    GenevestigatoriO09114.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    Secondary structure

    1
    189
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi27 – 293
    Helixi36 – 394
    Beta strandi41 – 5010
    Helixi55 – 584
    Turni59 – 613
    Beta strandi66 – 716
    Beta strandi75 – 8511
    Beta strandi89 – 9810
    Beta strandi104 – 1074
    Beta strandi110 – 1134
    Beta strandi116 – 1249
    Turni125 – 1273
    Beta strandi128 – 1347
    Turni137 – 1404
    Beta strandi144 – 15411
    Helixi157 – 16913
    Helixi174 – 1763
    Beta strandi177 – 1793
    Beta strandi184 – 1874

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CZTX-ray2.00A25-189[»]
    2CZUX-ray2.10A/B25-189[»]
    2E4JNMR-A25-189[»]
    2KTDNMR-A25-189[»]
    2RQ0NMR-A25-189[»]
    ProteinModelPortaliO09114.
    SMRiO09114. Positions 35-189.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO09114.

    Family & Domainsi

    Domaini

    Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.3 Publications

    Sequence similaritiesi

    Belongs to the calycin superfamily. Lipocalin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG45731.
    GeneTreeiENSGT00620000088005.
    HOGENOMiHOG000231660.
    HOVERGENiHBG106490.
    InParanoidiO09114.
    KOiK01830.
    OMAiPGQDFRM.
    OrthoDBiEOG78PVBH.
    PhylomeDBiO09114.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O09114-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAALRMLWMG LVLLGLLGFP QTPAQGHDTV QPNFQQDKFL GRWYSAGLAS    50
    NSSWFREKKA VLYMCKTVVA PSTEGGLNLT STFLRKNQCE TKIMVLQPAG 100
    APGHYTYSSP HSGSIHSVSV VEANYDEYAL LFSRGTKGPG QDFRMATLYS 150
    RTQTLKDELK EKFTTFSKAQ GLTEEDIVFL PQPDKCIQE 189
    Length:189
    Mass (Da):21,066
    Last modified:July 1, 1997 - v1
    Checksum:iC2C0B3E3B5928643
    GO
    Isoform 2 (identifier: O09114-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-63: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:126
    Mass (Da):13,941
    Checksum:i7F9FEDCFBEFF99A6
    GO

    Sequence cautioni

    The sequence BAA21769.1 differs from that shown. Reason: Frameshift at position 47.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6363Missing in isoform 2. 1 PublicationVSP_041029Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X89222 mRNA. Translation: CAA61506.1.
    Y10138 Genomic DNA. Translation: CAA71226.1.
    AB006361 mRNA. Translation: BAA21769.1. Frameshift.
    D83329 Genomic DNA. Translation: BAA74461.1.
    AK131859 mRNA. Translation: BAE20833.1.
    CH466542 Genomic DNA. Translation: EDL08250.1.
    CH466542 Genomic DNA. Translation: EDL08251.1.
    BC038083 mRNA. Translation: AAH38083.1.
    BC043015 mRNA. Translation: AAH43015.1.
    CCDSiCCDS38074.1. [O09114-1]
    PIRiS57748.
    RefSeqiNP_032989.2. NM_008963.2. [O09114-1]
    XP_006497849.1. XM_006497786.1. [O09114-1]
    XP_006497850.1. XM_006497787.1. [O09114-1]
    UniGeneiMm.1008.

    Genome annotation databases

    EnsembliENSMUST00000015234; ENSMUSP00000015234; ENSMUSG00000015090. [O09114-1]
    ENSMUST00000114251; ENSMUSP00000109889; ENSMUSG00000015090. [O09114-1]
    ENSMUST00000114259; ENSMUSP00000109897; ENSMUSG00000015090. [O09114-1]
    GeneIDi19215.
    KEGGimmu:19215.
    UCSCiuc008isf.1. mouse. [O09114-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X89222 mRNA. Translation: CAA61506.1 .
    Y10138 Genomic DNA. Translation: CAA71226.1 .
    AB006361 mRNA. Translation: BAA21769.1 . Frameshift.
    D83329 Genomic DNA. Translation: BAA74461.1 .
    AK131859 mRNA. Translation: BAE20833.1 .
    CH466542 Genomic DNA. Translation: EDL08250.1 .
    CH466542 Genomic DNA. Translation: EDL08251.1 .
    BC038083 mRNA. Translation: AAH38083.1 .
    BC043015 mRNA. Translation: AAH43015.1 .
    CCDSi CCDS38074.1. [O09114-1 ]
    PIRi S57748.
    RefSeqi NP_032989.2. NM_008963.2. [O09114-1 ]
    XP_006497849.1. XM_006497786.1. [O09114-1 ]
    XP_006497850.1. XM_006497787.1. [O09114-1 ]
    UniGenei Mm.1008.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CZT X-ray 2.00 A 25-189 [» ]
    2CZU X-ray 2.10 A/B 25-189 [» ]
    2E4J NMR - A 25-189 [» ]
    2KTD NMR - A 25-189 [» ]
    2RQ0 NMR - A 25-189 [» ]
    ProteinModelPortali O09114.
    SMRi O09114. Positions 35-189.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi O09114.
    ChEMBLi CHEMBL4334.

    PTM databases

    PhosphoSitei O09114.

    Proteomic databases

    MaxQBi O09114.
    PaxDbi O09114.
    PRIDEi O09114.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000015234 ; ENSMUSP00000015234 ; ENSMUSG00000015090 . [O09114-1 ]
    ENSMUST00000114251 ; ENSMUSP00000109889 ; ENSMUSG00000015090 . [O09114-1 ]
    ENSMUST00000114259 ; ENSMUSP00000109897 ; ENSMUSG00000015090 . [O09114-1 ]
    GeneIDi 19215.
    KEGGi mmu:19215.
    UCSCi uc008isf.1. mouse. [O09114-1 ]

    Organism-specific databases

    CTDi 5730.
    MGIi MGI:99261. Ptgds.

    Phylogenomic databases

    eggNOGi NOG45731.
    GeneTreei ENSGT00620000088005.
    HOGENOMi HOG000231660.
    HOVERGENi HBG106490.
    InParanoidi O09114.
    KOi K01830.
    OMAi PGQDFRM.
    OrthoDBi EOG78PVBH.
    PhylomeDBi O09114.
    TreeFami TF336103.

    Enzyme and pathway databases

    BRENDAi 5.3.99.2. 3474.
    Reactomei REACT_188623. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).

    Miscellaneous databases

    ChiTaRSi PTGDS. mouse.
    EvolutionaryTracei O09114.
    NextBioi 295972.
    PROi O09114.
    SOURCEi Search...

    Gene expression databases

    Bgeei O09114.
    CleanExi MM_PTGDS.
    Genevestigatori O09114.

    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. "Developmental expression of murine Beta-trace in embryos and adult animals suggests a function in maturation and maintenance of blood-tissue barriers."
      Hoffmann A., Baechner D., Betat N., Lauber J., Gross G.
      Dev. Dyn. 207:332-343(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
      Strain: NMRI.
      Tissue: Brain.
    2. Hoffmann A., Steinert P., Lauber J., Gross G.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    3. "Isolation of putative prostaglandin D synthetase from mouse choroid plexus."
      Kita H., Kawamoto S., Okubo K., Matsubara K.
      Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: C57BL/6.
      Tissue: Brain.
    4. "Lack of tactile pain (allodynia) in lipocalin-type prostaglandin D synthase-deficient mice."
      Eguchi N., Minami T., Shirafuji N., Kanaoka Y., Tanaka T., Nagata A., Yoshida N., Urade Y., Ito S., Hayaishi O.
      Proc. Natl. Acad. Sci. U.S.A. 96:726-730(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
      Strain: 129/Sv.
      Tissue: Liver.
    5. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Small intestine.
    6. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 2).
      Tissue: Eye.
    8. "Prostaglandin D synthase gene is involved in the regulation of non-rapid eye movement sleep."
      Pinzar E., Kanaoka Y., Inui T., Eguchi N., Urade Y., Hayaishi O.
      Proc. Natl. Acad. Sci. U.S.A. 97:4903-4907(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Pronounced eosinophilic lung inflammation and Th2 cytokine release in human lipocalin-type prostaglandin D synthase transgenic mice."
      Fujitani Y., Kanaoka Y., Aritake K., Uodome N., Okazaki-Hatake K., Urade Y.
      J. Immunol. 168:443-449(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    10. "Perineuronal oligodendrocytes protect against neuronal apoptosis through the production of lipocalin-type prostaglandin D synthase in a genetic demyelinating model."
      Taniike M., Mohri I., Eguchi N., Beuckmann C.T., Suzuki K., Urade Y.
      J. Neurosci. 22:4885-4896(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Stage and region-specific localization of lipocalin-type prostaglandin D synthase in the adult murine testis and epididymis."
      Gerena R.L., Eguchi N., Urade Y., Killian G.J.
      J. Androl. 21:848-854(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    12. "Dexamethasone induces lipocalin-type prostaglandin D synthase gene expression in mouse neuronal cells."
      Garcia-Fernandez L.F., Iniguez M.A., Eguchi N., Fresno M., Urade Y., Munoz A.
      J. Neurochem. 75:460-470(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY DEXAMETHASONE.
    13. "Structural basis of multi-functional lipocalin-type prostaglandin D synthase."
      RIKEN structural genomics initiative (RSGI)
      Submitted (OCT-2006) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 24-189.
    14. "NMR solution structure of lipocalin-type prostaglandin D synthase: evidence for partial overlapping of catalytic pocket and retinoic acid-binding pocket within the central cavity."
      Shimamoto S., Yoshida T., Inui T., Gohda K., Kobayashi Y., Fujimori K., Tsurumura T., Aritake K., Urade Y., Ohkubo T.
      J. Biol. Chem. 282:31373-31379(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 25-189, FUNCTION, CATALYTIC ACTIVITY, DOMAIN.
    15. "Structural basis of the catalytic mechanism operating in open-closed conformers of lipocalin type prostaglandin D synthase."
      Kumasaka T., Aritake K., Ago H., Irikura D., Tsurumura T., Yamamoto M., Miyano M., Urade Y., Hayaishi O.
      J. Biol. Chem. 284:22344-22352(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 25-189 OF MUTANT ALA-65 IN COMPLEX WITH RETINOIC ACID, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF SER-45; CYS-65; THR-67 AND SER-81, BIOPHYSICOCHEMICAL PROPERTIES, DISULFIDE BOND, DOMAIN.
    16. "Structural analysis of lipocalin-type prostaglandin D synthase complexed with biliverdin by small-angle X-ray scattering and multi-dimensional NMR."
      Miyamoto Y., Nishimura S., Inoue K., Shimamoto S., Yoshida T., Fukuhara A., Yamada M., Urade Y., Yagi N., Ohkubo T., Inui T.
      J. Struct. Biol. 169:209-218(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 25-189 IN COMPLEX WITH BILIVERDIN, FUNCTION, DOMAIN.

    Entry informationi

    Entry nameiPTGDS_MOUSE
    AccessioniPrimary (citable) accession number: O09114
    Secondary accession number(s): O09157
    , O35091, Q3V2G5, Q62169
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 133 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3