Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q29095

- PTGDS_PIG

UniProt

Q29095 - PTGDS_PIG

Protein

Prostaglandin-H2 D-isomerase

Gene

PTGDS

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 sitei63 – 631NucleophileBy 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
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: 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 – 189165Prostaglandin-H2 D-isomerasePRO_0000017948Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei25 – 251Pyrrolidone carboxylic acidBy similarity
    Glycosylationi49 – 491N-linked (GlcNAc...)By similarity
    Glycosylationi76 – 761N-linked (GlcNAc...)By similarity
    Disulfide bondi87 ↔ 184By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

    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.2 Publications

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ29095.
    SMRiQ29095. Positions 27-187.
    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.
    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.

    Q29095-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATPSSLWLG LALLGTLGVL QTPAQASLQP NFQEDKFLGR WFTSGLASNS    50
    SWFLEKKKVL SMCKSLVAPA PDGGFNLTST FLRKDQCVTR TLMLRPAGPP 100
    GCYSYTSPHG GSNLEVSVVE TDYKNYALLH TESGPSPGPA FRMATLYSRS 150
    QAPGAAVREK FTAFAKARGF TEDGIVFLPR NEKCLEEHE 189
    Length:189
    Mass (Da):20,568
    Last modified:November 1, 1996 - v1
    Checksum:iA46560DF77E33E72
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X92979 mRNA. Translation: CAA63556.1.
    RefSeqiNP_999393.1. NM_214228.1.
    UniGeneiSsc.16187.

    Genome annotation databases

    GeneIDi397456.
    KEGGissc:397456.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X92979 mRNA. Translation: CAA63556.1 .
    RefSeqi NP_999393.1. NM_214228.1.
    UniGenei Ssc.16187.

    3D structure databases

    ProteinModelPortali Q29095.
    SMRi Q29095. Positions 27-187.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi Q29095.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 397456.
    KEGGi ssc:397456.

    Organism-specific databases

    CTDi 5730.

    Phylogenomic databases

    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. "Constitutive secretion of beta-trace protein by cultivated porcine choroid plexus epithelial cells: elucidation of its complete amino acid and cDNA sequences."
      Hoffmann A., Gath U., Gross G., Lauber J., Getclaff R., Hillwig S., Galla H.J., Conradt H.S.
      J. Cell. Physiol. 169:235-241(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 27-58; 61-94; 96-123; 125-147; 150-158; 161-166; 169-180 AND 184-189, TISSUE SPECIFICITY.
    2. "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.

    Entry informationi

    Entry nameiPTGDS_PIG
    AccessioniPrimary (citable) accession number: Q29095
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 94 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