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    cyn-9 Peptidyl-prolyl cis-trans isomerase 9 [ Caenorhabditis elegans ]

    Gene ID: 175471, updated on 9-Dec-2024

    Summary

    Official Symbol
    cyn-9
    Official Full Name
    Peptidyl-prolyl cis-trans isomerase 9
    Primary source
    WormBase:WBGene00000885
    Locus tag
    CELE_T27D1.1
    See related
    AllianceGenome:WB:WBGene00000885
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Caenorhabditis elegans (strain: Bristol N2)
    Lineage
    Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis
    Summary
    Predicted to enable cyclosporin A binding activity and peptidyl-prolyl cis-trans isomerase activity. Predicted to be involved in protein folding. Predicted to be active in cytosol. Is expressed in hypodermis. Orthologous to human NKTR (natural killer cell triggering receptor). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

    See cyn-9 in Genome Data Viewer
    Location:
    chromosome: III
    Exon count:
    6
    Sequence:
    Chromosome: III; NC_003281.10 (3697821..3699640, complement)

    Chromosome III - NC_003281.10Genomic Context describing neighboring genes Neighboring gene ncRNA Neighboring gene Neuropeptide receptor 15 Neighboring gene Protein disulfide-isomerase 1 Neighboring gene Conserved plasma membrane protein

    Interactions

    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Markers

    Gene Ontology Provided by WormBase

    Function Evidence Code Pubs
    enables cyclosporin A binding IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    enables peptidyl-prolyl cis-trans isomerase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    enables peptidyl-prolyl cis-trans isomerase activity IEA
    Inferred from Electronic Annotation
    more info
     
    enables peptidyl-prolyl cis-trans isomerase activity ISS
    Inferred from Sequence or Structural Similarity
    more info
    PubMed 
    enables peptidyl-prolyl cis-trans isomerase activity NAS
    Non-traceable Author Statement
    more info
    PubMed 
    Process Evidence Code Pubs
    involved_in extracellular matrix organization TAS
    Traceable Author Statement
    more info
    PubMed 
    involved_in protein folding IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    involved_in protein folding NAS
    Non-traceable Author Statement
    more info
    PubMed 
    involved_in protein folding TAS
    Traceable Author Statement
    more info
    PubMed 
    involved_in protein peptidyl-prolyl isomerization IEA
    Inferred from Electronic Annotation
    more info
     
    Component Evidence Code Pubs
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
     

    General protein information

    Preferred Names
    Peptidyl-prolyl cis-trans isomerase 9
    NP_497745.1
    • Confirmed by transcript evidence

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

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

    Reference assembly

    Genomic

    1. NC_003281.10 Reference assembly

      Range
      3697821..3699640 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_065344.5NP_497745.1  Peptidyl-prolyl cis-trans isomerase 9 [Caenorhabditis elegans]

      See identical proteins and their annotated locations for NP_497745.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      A2NTF2, Q09339, Q09637
      Conserved Domains (1) summary
      cl00197
      Location:6172
      cyclophilin; cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains eukaryotic, bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase, Rotamase) and in addition bind the ...