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Q9XSM0

- PTGDS_SHEEP

UniProt

Q9XSM0 - PTGDS_SHEEP

Protein

Prostaglandin-H2 D-isomerase

Gene

PTGDS

Organism
Ovis aries (Sheep)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      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 By similarity.By similarity

    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 – 651NucleophileBy similarity

    GO - Molecular functioni

    1. prostaglandin-D synthase activity Source: UniProtKB
    2. retinoid binding Source: UniProtKB
    3. small molecule binding Source: InterPro
    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. 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

    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
    OrganismiOvis aries (Sheep)
    Taxonomic identifieri9940 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis
    ProteomesiUP000002356: Unplaced

    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. Golgi apparatus Source: UniProtKB
    3. nuclear membrane Source: UniProtKB-SubCell
    4. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    5. rough endoplasmic reticulum Source: UniProtKB

    Keywords - Cellular componenti

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424By similarityAdd
    BLAST
    Chaini25 – 191167Prostaglandin-H2 D-isomerasePRO_0000017951Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi51 – 511N-linked (GlcNAc...)By similarity
    Glycosylationi78 – 781N-linked (GlcNAc...)By similarity
    Disulfide bondi89 ↔ 186By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Expressioni

    Tissue specificityi

    In the male reproductive system, it is expressed in the testis and epididymis, and is secreted into the seminal fluid.3 Publications

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ9XSM0.
    SMRiQ9XSM0. Positions 30-188.
    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

    HOVERGENiHBG106490.

    Family and domain databases

    Gene3Di2.40.128.20. 1 hit.
    InterProiIPR012674. Calycin.
    IPR011038. Calycin-like.
    IPR002345. Lipocalin.
    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.

    Sequencei

    Sequence statusi: Complete.

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

    Q9XSM0-1 [UniParc]FASTAAdd to Basket

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    MATPNRPWMG LLLLGVLGVL QTPAPTEAAL QPNFEEDKFL GRWFTSGLAS    50
    NSSWFLEKRK VLSMCKSEVA PAADGGLNVT STFLRKDQCE TRTLLLRPAG 100
    PPGCYSYTSP HWSSTHEVSV AETDYETYAL LYTESVRGPG PDSLMATLYS 150
    RTQTPRAEVK EKFTTFARSL GFTEEGIVFL PKTDKCMEVR T 191
    Length:191
    Mass (Da):21,183
    Last modified:November 1, 1999 - v1
    Checksum:iB7555070F8A54244
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ133642 mRNA. Translation: CAB40371.1.
    RefSeqiNP_001009257.1. NM_001009257.1.
    UniGeneiOar.691.

    Genome annotation databases

    GeneIDi443192.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ133642 mRNA. Translation: CAB40371.1 .
    RefSeqi NP_001009257.1. NM_001009257.1.
    UniGenei Oar.691.

    3D structure databases

    ProteinModelPortali Q9XSM0.
    SMRi Q9XSM0. Positions 30-188.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 443192.

    Organism-specific databases

    CTDi 5730.

    Phylogenomic databases

    HOVERGENi HBG106490.

    Family and domain databases

    Gene3Di 2.40.128.20. 1 hit.
    InterProi IPR012674. Calycin.
    IPR011038. Calycin-like.
    IPR002345. Lipocalin.
    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.
    ProtoNeti Search...

    Publicationsi

    1. "Mammalian lipocalin-type prostaglandin D2 synthase in the fluids of the male genital tract: putative biochemical and physiological functions."
      Fouchecourt S., Charpigny G., Reinaud P., Dumont P., Dacheux J.-L.
      Biol. Reprod. 66:458-467(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    2. "Glutathione-independent prostaglandin D2 synthase in ram and stallion epididymal fluids: origin and regulation."
      Fouchecourt S., Dacheux F., Dacheux J.-L.
      Biol. Reprod. 60:558-566(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-45; 63-68 AND 100-107, TISSUE SPECIFICITY.
    3. "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: TISSUE SPECIFICITY.
    4. "Prostaglandin d(2) synthase secreted in the caput epididymidis displays spatial and temporal delay between messenger RNA and protein expression during postnatal development."
      Fouchecourt S., Castella S., Dacheux F., Dacheux J.-L.
      Biol. Reprod. 68:174-179(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiPTGDS_SHEEP
    AccessioniPrimary (citable) accession number: Q9XSM0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 86 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3