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P22057

- PTGDS_RAT

UniProt

P22057 - PTGDS_RAT

Protein

Prostaglandin-H2 D-isomerase

Gene

Ptgds

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      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.4 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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei65 – 651Nucleophile1 Publication

    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: RGD
    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

    ReactomeiREACT_194948. 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:
    PGD2 synthase
    Short name:
    PGDS
    Short name:
    PGDS2
    Gene namesi
    Name:Ptgds
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 3

    Organism-specific databases

    RGDi3433. Ptgds.

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB
    2. extracellular space Source: RGD
    3. Golgi apparatus Source: UniProtKB
    4. nuclear envelope Source: UniProtKB
    5. nuclear membrane Source: UniProtKB-SubCell
    6. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    7. 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
    Mutagenesisi65 – 651C → A or S: Loss of enzymatic activity. 1 Publication
    Mutagenesisi89 – 891C → A or S: Disrupts disulfide bond. 1 Publication
    Mutagenesisi186 – 1861C → A or S: Disrupts disulfide bond. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Add
    BLAST
    Chaini25 – 189165Prostaglandin-H2 D-isomerasePRO_0000017950Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei25 – 251Pyrrolidone carboxylic acid1 Publication
    Glycosylationi51 – 511N-linked (GlcNAc...)1 Publication
    Glycosylationi78 – 781N-linked (GlcNAc...)1 Publication
    Disulfide bondi89 ↔ 1861 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

    Proteomic databases

    PaxDbiP22057.
    PRIDEiP22057.

    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 eye, it is expressed in the pigmented epithelium of the retina and the nonpigmented epithelium of the iris and ciliary body, and accumulates within the interphotoreceptor matrix, photoreceptors, and aqueous and vitreous humors. In the male reproductive system, it is expressed in the testis and epididymis, and is secreted into the seminal fluid. It has also been detected in the cochlea.9 Publications

    Developmental stagei

    In the brain it is localized in many neurons at 1-2 weeks after birth, whereas in mature animals it is localized to tissues of the blood-brain barrier.1 Publication

    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.4 Publications

    Gene expression databases

    GenevestigatoriP22057.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    BioGridi247558. 2 interactions.
    STRINGi10116.ENSRNOP00000020926.

    Structurei

    3D structure databases

    ProteinModelPortaliP22057.
    SMRiP22057. Positions 24-189.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.By similarity

    Sequence similaritiesi

    Belongs to the calycin superfamily. Lipocalin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG45731.
    GeneTreeiENSGT00620000088005.
    HOGENOMiHOG000231660.
    HOVERGENiHBG106490.
    KOiK01830.
    OMAiPGQDFRM.
    OrthoDBiEOG78PVBH.
    PhylomeDBiP22057.
    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.

    P22057-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAALPMLWTG LVLLGLLGFP QTPAQGHDTV QPNFQQDKFL GRWYSAGLAS    50
    NSSWFREKKE LLFMCQTVVA PSTEGGLNLT STFLRKNQCE TKVMVLQPAG 100
    VPGQYTYNSP HWGSFHSLSV VETDYDEYAF LFSKGTKGPG QDFRMATLYS 150
    RAQLLKEELK EKFITFSKDQ GLTEEDIVFL PQPDKCIQE 189
    Length:189
    Mass (Da):21,301
    Last modified:February 1, 1996 - v2
    Checksum:i866E4CFE0F814FDC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti138 – 1381G → A in S66190. (PubMed:8216319)Curated
    Sequence conflicti144 – 1441R → G in S66190. (PubMed:8216319)Curated

    Mass spectrometryi

    Molecular mass is 18808 Da from positions 25 - 189. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04488 mRNA. Translation: AAA41839.1.
    M94134 Genomic DNA. Translation: AAA41840.1.
    S66190 mRNA. No translation available.
    PIRiA32202.
    S65717.
    RefSeqiNP_037147.1. NM_013015.2.
    UniGeneiRn.11400.

    Genome annotation databases

    EnsembliENSRNOT00000020926; ENSRNOP00000020926; ENSRNOG00000015550.
    GeneIDi25526.
    KEGGirno:25526.
    UCSCiRGD:3433. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04488 mRNA. Translation: AAA41839.1 .
    M94134 Genomic DNA. Translation: AAA41840.1 .
    S66190 mRNA. No translation available.
    PIRi A32202.
    S65717.
    RefSeqi NP_037147.1. NM_013015.2.
    UniGenei Rn.11400.

    3D structure databases

    ProteinModelPortali P22057.
    SMRi P22057. Positions 24-189.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 247558. 2 interactions.
    STRINGi 10116.ENSRNOP00000020926.

    Proteomic databases

    PaxDbi P22057.
    PRIDEi P22057.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000020926 ; ENSRNOP00000020926 ; ENSRNOG00000015550 .
    GeneIDi 25526.
    KEGGi rno:25526.
    UCSCi RGD:3433. rat.

    Organism-specific databases

    CTDi 5730.
    RGDi 3433. Ptgds.

    Phylogenomic databases

    eggNOGi NOG45731.
    GeneTreei ENSGT00620000088005.
    HOGENOMi HOG000231660.
    HOVERGENi HBG106490.
    KOi K01830.
    OMAi PGQDFRM.
    OrthoDBi EOG78PVBH.
    PhylomeDBi P22057.
    TreeFami TF336103.

    Enzyme and pathway databases

    Reactomei REACT_194948. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).

    Miscellaneous databases

    NextBioi 607007.
    PROi P22057.

    Gene expression databases

    Genevestigatori P22057.

    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. "Primary structure of rat brain prostaglandin D synthetase deduced from cDNA sequence."
      Urade Y., Nagata A., Suzuki Y., Fujii Y., Hayaishi O.
      J. Biol. Chem. 264:1041-1045(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 39-53; 60-85; 93-108 AND 138-185, TISSUE SPECIFICITY, GLYCOSYLATION.
      Tissue: Brain.
    2. "Structural organization of the gene for prostaglandin D synthase in the rat brain."
      Igarashi M., Nagata A., Toh H., Urade Y., Hayaihi O.
      Proc. Natl. Acad. Sci. U.S.A. 89:5376-5380(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Wistar.
    3. "Proteins of rat serum, urine, and cerebrospinal fluid: VI. Further protein identifications and interstrain comparison."
      Wait R., Gianazza E., Eberini I., Sironi L., Dunn M.J., Gemeiner M., Miller I.
      Electrophoresis 22:3043-3052(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 26-42, PYROGLUTAMATE FORMATION AT GLN-25, TISSUE SPECIFICITY, MASS SPECTROMETRY.
      Strain: Wistar Kyoto.
      Tissue: Cerebrospinal fluid.
    4. "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 27-41, TISSUE SPECIFICITY.
      Tissue: Cerebrospinal fluid.
    5. "Structural and functional significance of cysteine residues of glutathione-independent prostaglandin D synthase. Identification of Cys65 as an essential thiol."
      Urade Y., Tanaka T., Eguchi N., Kikuchi M., Kimura H., Toh H., Hayaishi O.
      J. Biol. Chem. 270:1422-1428(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 26-32, ACTIVE SITE, COFACTOR, DISULFIDE BOND, MUTAGENESIS OF CYS-65; CYS-89 AND CYS-186.
      Tissue: Brain.
    6. "Brain-specific prostaglandin D2 synthetase mRNA is dependent on thyroid hormone during rat brain development."
      Garcia-Fernandez L.F., Iniguez M.A., Rodriguez-Pena A., Munoz A., Bernal J.
      Biochem. Biophys. Res. Commun. 196:396-401(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 124-189.
    7. Lubec G., Kang S.U., Lubec S.
      Submitted (SEP-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 169-185, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Brain.
    8. "Lipocalin-type prostaglandin D synthase (beta-trace) is a newly recognized type of retinoid transporter."
      Tanaka T., Urade Y., Kimura H., Eguchi N., Nishikawa A., Hayaishi O.
      J. Biol. Chem. 272:15789-15795(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION BY RETINOIDS.
    9. "Binding of biliverdin, bilirubin, and thyroid hormones to lipocalin-type prostaglandin D synthase."
      Beuckmann C.T., Aoyagi M., Okazaki I., Hiroike T., Toh H., Hayaishi O., Urade Y.
      Biochemistry 38:8006-8013(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION.
    10. "Cellular localization of lipocalin-type prostaglandin D synthase (beta-trace) in the central nervous system of the adult rat."
      Beuckmann C.T., Lazarus M., Gerashchenko D., Mizoguchi A., Nomura S., Mohri I., Uesugi A., Kaneko T., Mizuno N., Hayaishi O., Urade Y.
      J. Comp. Neurol. 428:62-78(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    11. "Sertoli cell prostaglandin D2 synthetase is a multifunctional molecule: its expression and regulation."
      Samy E.T., Li J.C.H., Grima J., Lee W.M., Silvestrini B., Cheng C.Y.
      Endocrinology 141:710-721(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION BY PROGESTERONE, RETINOIDS AND THYROID HORMONE.
    12. "Lipocalin-type prostaglandin D synthase (beta-trace) is located in pigment epithelial cells of rat retina and accumulates within interphotoreceptor matrix."
      Beuckmann C.T., Gordon W.C., Kanaoka Y., Eguchi N., Marcheselli V.L., Gerashchenko D.Y., Urade Y., Hayaishi O., Bazan N.G.
      J. Neurosci. 16:6119-6124(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    13. "Dominant expression of mRNA for prostaglandin D synthase in leptomeninges, choroid plexus, and oligodendrocytes of the adult rat brain."
      Urade Y., Kitahama K., Ohishi H., Kaneko T., Mizuno N., Hayaishi O.
      Proc. Natl. Acad. Sci. U.S.A. 90:9070-9074(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    14. "Localization of lipocalin-type prostaglandin D synthase (beta-trace) in iris, ciliary body, and eye fluids."
      Gerashchenko D.Y., Beuckmann C.T., Marcheselli V.L., Gordon W.C., Kanaoka Y., Eguchi N., Urade Y., Hayaishi O., Bazan N.G.
      Invest. Ophthalmol. Vis. Sci. 39:198-203(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    15. "Rat prostaglandin D2 synthetase: its tissue distribution, changes during maturation, and regulation in the testis and epididymis."
      Sorrentino C., Silvestrini B., Braghiroli L., Chung S.S.W., Giacomelli S., Leone M.-G., Xie Y.-B., Sui Y.-P., Mo M.-Y., Cheng C.Y.
      Biol. Reprod. 59:843-853(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION BY DIHYDROTESTOSTERONE.
    16. "Identification of a thyroid hormone response element in the promoter region of the rat lipocalin-type prostaglandin D synthase (beta-trace) gene."
      Garcia-Fernandez L.F., Urade Y., Hayaishi O., Bernal J., Munoz A.
      Brain Res. Mol. Brain Res. 55:321-330(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY THYROID HORMONE AND RETINOIDS.
    17. "Regulation of lipocalin-type prostaglandin D synthase gene expression by Hes-1 through E-box and interleukin-1 beta via two NF-kappaB elements in rat leptomeningeal cells."
      Fujimori K., Fujitani Y., Kadoyama K., Kumanogoh H., Ishikawa K., Urade Y.
      J. Biol. Chem. 278:6018-6026(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY IL-1 BETA, REPRESSION BY NOTCH-HES.
    18. "The first lipocalin with enzymatic activity."
      Peitsch M.C., Boguski M.S.
      Trends Biochem. Sci. 16:363-363(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: SIMILARITY TO THE LIPOCALIN FAMILY.

    Entry informationi

    Entry nameiPTGDS_RAT
    AccessioniPrimary (citable) accession number: P22057
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 130 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3