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    Ptges3l prostaglandin E synthase 3 like [ Rattus norvegicus (Norway rat) ]

    Gene ID: 103693432, updated on 9-Dec-2024

    Summary

    Official Symbol
    Ptges3lprovided by RGD
    Official Full Name
    prostaglandin E synthase 3 likeprovided by RGD
    Primary source
    RGD:9413039
    See related
    EnsemblRapid:ENSRNOG00000050347 AllianceGenome:RGD:9413039
    Gene type
    protein coding
    RefSeq status
    VALIDATED
    Organism
    Rattus norvegicus
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
    Summary
    Predicted to enable Hsp90 protein binding activity and protein-folding chaperone binding activity. Predicted to be located in cytoplasm. Orthologous to human PTGES3L (prostaglandin E synthase 3 like). [provided by Alliance of Genome Resources, Dec 2024]
    Expression
    Biased expression in Muscle (RPKM 119.2), Heart (RPKM 88.1) and 8 other tissues See more
    Orthologs
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    Try the new Transcript table

    Genomic context

    See Ptges3l in Genome Data Viewer
    Location:
    10q31
    Exon count:
    7
    Annotation release Status Assembly Chr Location
    RS_2024_02 current GRCr8 (GCF_036323735.1) 10 NC_086028.1 (86854268..86861568, complement)
    RS_2023_06 previous assembly mRatBN7.2 (GCF_015227675.2) 10 NC_051345.1 (86354019..86361318, complement)
    106 previous assembly Rnor_6.0 (GCF_000001895.5) 10 NC_005109.4 (89331368..89338644, complement)

    Chromosome 10 - NC_086028.1Genomic Context describing neighboring genes Neighboring gene glucose-6-phosphatase catalytic subunit 1 Neighboring gene alanyl-tRNA synthetase domain containing 1 Neighboring gene RUN domain containing 1 Neighboring gene ribosomal protein L27

    Genomic regions, transcripts, and products

    General gene information

    Gene Ontology Provided by RGD

    Function Evidence Code Pubs
    enables Hsp90 protein binding IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    enables Hsp90 protein binding IEA
    Inferred from Electronic Annotation
    more info
     
    enables protein-folding chaperone binding IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    enables protein-folding chaperone binding IEA
    Inferred from Electronic Annotation
    more info
     
    Process Evidence Code Pubs
    involved_in chaperone-mediated protein complex assembly IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    involved_in protein folding IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    Component Evidence Code Pubs
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
     
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    is_active_in nucleus IBA
    Inferred from Biological aspect of Ancestor
    more info
     

    General protein information

    Preferred Names
    putative protein PTGES3L
    Names
    alanyl-tRNA synthetase domain containing 1-like
    prostaglandin E synthase 3 (cytosolic)-like

    NCBI Reference Sequences (RefSeq)

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    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    mRNA and Protein(s)

    1. NM_001399462.1NP_001386391.1  putative protein PTGES3L

      Status: VALIDATED

      Source sequence(s)
      JAXUCZ010000010
      UniProtKB/TrEMBL
      A0A8I6AJ40, A6HJB6
      Conserved Domains (1) summary
      cd00237
      Location:5110
      p23; p23 binds heat shock protein (Hsp)90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis.

    RefSeqs of Annotated Genomes: GCF_036323735.1-RS_2024_02

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference GRCr8

    Genomic

    1. NC_086028.1 Reference GRCr8

      Range
      86854268..86861568 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_063268252.1XP_063124322.1  putative protein PTGES3L isoform X1

      UniProtKB/TrEMBL
      A6HJB5, M0R7Z4
      Related
      ENSRNOP00000065582.3, ENSRNOT00000073923.4
    2. XM_008768222.4XP_008766444.1  putative protein PTGES3L isoform X3

      See identical proteins and their annotated locations for XP_008766444.1

      Conserved Domains (1) summary
      cl00175
      Location:192
      alpha-crystallin-Hsps_p23-like; alpha-crystallin domain (ACD) found in alpha-crystallin-type small heat shock proteins, and a similar domain found in p23 (a cochaperone for Hsp90) and in other p23-like proteins.
    3. XM_039087748.2XP_038943676.1  putative protein PTGES3L isoform X4

      Conserved Domains (1) summary
      cd00237
      Location:35140
      p23; p23 binds heat shock protein (Hsp)90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis.
    4. XM_008768220.4XP_008766442.1  putative protein PTGES3L isoform X2

      See identical proteins and their annotated locations for XP_008766442.1

      UniProtKB/TrEMBL
      A0A8I5ZS02
      Related
      ENSRNOP00000093004.2, ENSRNOT00000106212.2
      Conserved Domains (1) summary
      cd00237
      Location:35140
      p23; p23 binds heat shock protein (Hsp)90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis.