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O97921

- PTGDS_HORSE

UniProt

O97921 - PTGDS_HORSE

Protein

Prostaglandin-H2 D-isomerase

Gene

PTGDS

Organism
Equus caballus (Horse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 May 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
    OrganismiEquus caballus (Horse)
    Taxonomic identifieri9796 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus
    ProteomesiUP000002281: 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. extracellular space Source: UniProtKB
    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424By similarityAdd
    BLAST
    Chaini25 – 194170Prostaglandin-H2 D-isomerasePRO_0000017944Add
    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 ↔ 189By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

    Expressioni

    Tissue specificityi

    In the male reproductive system, it is expressed in the testis and epididymis, and is secreted into the seminal fluid.1 Publication

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    STRINGi9796.ENSECAP00000007190.

    Structurei

    3D structure databases

    ProteinModelPortaliO97921.
    SMRiO97921. Positions 24-192.
    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.
    HOVERGENiHBG106490.
    KOiK01830.

    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.

    O97921-1 [UniParc]FASTAAdd to Basket

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    MAASHTLWMG LVLLGVLGVL QTRAQAQPSL QPNFQQDKFL GRWFTSGLAS    50
    NSSWFREKKK VLSMCTSVVA PTADGGFNLT STFLRKDQCE TRTLLLQPAG 100
    PPGCYSYTSP HWGMVHEVSV VETDYEEYAL LYTHAESTKG LGGQDFRMAT 150
    LYSRVQSPRP EVKEKFSTFA KAQGFTEDAI VFLPQTDKCM EEHN 194
    Length:194
    Mass (Da):21,669
    Last modified:May 1, 1999 - v1
    Checksum:iC6E271A540877994
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti115 – 1217VHEVSVV → PHEMSMM AA sequence (PubMed:10026099)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ133469 mRNA. Translation: CAB38173.1.
    RefSeqiNP_001075337.1. NM_001081868.1.
    UniGeneiEca.12658.

    Genome annotation databases

    GeneIDi100067921.
    KEGGiecb:100067921.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ133469 mRNA. Translation: CAB38173.1 .
    RefSeqi NP_001075337.1. NM_001081868.1.
    UniGenei Eca.12658.

    3D structure databases

    ProteinModelPortali O97921.
    SMRi O97921. Positions 24-192.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9796.ENSECAP00000007190.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100067921.
    KEGGi ecb:100067921.

    Organism-specific databases

    CTDi 5730.

    Phylogenomic databases

    eggNOGi NOG45731.
    HOVERGENi HBG106490.
    KOi K01830.

    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].
    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 108-122, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiPTGDS_HORSE
    AccessioniPrimary (citable) accession number: O97921
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 97 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