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    Ppig peptidylprolyl isomerase G [ Rattus norvegicus (Norway rat) ]

    Gene ID: 83624, updated on 27-Nov-2024

    Summary

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    Official Symbol
    Ppigprovided by RGD
    Official Full Name
    peptidylprolyl isomerase Gprovided by RGD
    Primary source
    RGD:620315
    See related
    EnsemblRapid:ENSRNOG00000007673 AllianceGenome:RGD:620315
    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
    Enables peptidyl-prolyl cis-trans isomerase activity. Predicted to be involved in protein folding. Located in nuclear matrix. Orthologous to human PPIG (peptidylprolyl isomerase G). [provided by Alliance of Genome Resources, Nov 2024]
    Expression
    Biased expression in Brain (RPKM 93.5), Thymus (RPKM 87.5) and 9 other tissues See more
    Orthologs
    human mouse all
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    Genomic context

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    See Ppig in Genome Data Viewer
    Location:
    3q21
    Exon count:
    16
    Annotation release Status Assembly Chr Location
    RS_2024_02 current GRCr8 (GCF_036323735.1) 3 NC_086021.1 (74891846..74923010)
    RS_2023_06 previous assembly mRatBN7.2 (GCF_015227675.2) 3 NC_051338.1 (54484023..54512929)
    106 previous assembly Rnor_6.0 (GCF_000001895.5) 3 NC_005102.4 (55959756..55990040)

    Chromosome 3 - NC_086021.1Genomic Context describing neighboring genes Neighboring gene kelch-like family member 41 Neighboring gene FAST kinase domains 1 Neighboring gene cilia and flagella associated protein 210 Neighboring gene phosphatase, orphan 2

    Genomic regions, transcripts, and products

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    Go to nucleotide: Graphics FASTA GenBank

    Expression

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    • Project title: A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages
    • Description: 320 RNA samples isolated from 11 organs (adrenal gland, brain, heart, kidney, liver, lung, muscle, spleen, thymus, and testes or uterus) from both sexes of Fischer 344 rats across four developmental stages (2-, 6-, 21-, and 104-weeks-old)
    • BioProject: PRJNA238328
    • Publication: PMID 24510058
    • Analysis date: Mon Jun 6 17:44:12 2016

    Bibliography

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    Related articles in PubMed

    1. Matrin CYP, an SR-rich cyclophilin that associates with the nuclear matrix and splicing factors. Mortillaro MJ, et al. J Biol Chem, 1998 Apr 3. PMID 9525923
    2. Spliceosomal immunophilins. Mesa A, et al. FEBS Lett, 2008 Jul 9. PMID 18544344, Free PMC Article
    3. Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases. Davis TL, et al. PLoS Biol, 2010 Jul 27. PMID 20676357, Free PMC Article
    4. Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites. Hoffert JD, et al. Proc Natl Acad Sci U S A, 2006 May 2. PMID 16641100, Free PMC Article
    5. The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Baltz AG, et al. Mol Cell, 2012 Jun 8. PMID 22681889

    See all (9) citations in PubMed

    GeneRIFs: Gene References Into Functions

    General gene information

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    Markers

    Homology

    Gene Ontology Provided by RGD

    Function Evidence Code Pubs
    enables RNA polymerase II CTD heptapeptide repeat P3 isomerase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables RNA polymerase II CTD heptapeptide repeat P6 isomerase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    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 IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables peptidyl-prolyl cis-trans isomerase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables peptidyl-prolyl cis-trans isomerase activity ISO
    Inferred from Sequence Orthology
    more info
    		  
    Process Evidence Code Pubs
    involved_in biological_process ND
    No biological Data available
    more info
    		  
    involved_in protein folding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in protein folding IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in regulation of transcription by RNA polymerase II IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytosol IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cytosol ISO
    Inferred from Sequence Orthology
    more info
    		  
    located_in nuclear matrix IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in nuclear speck IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in nuclear speck ISO
    Inferred from Sequence Orthology
    more info
    		  
    is_active_in nucleus IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  

    General protein information

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    Preferred Names
    peptidyl-prolyl cis-trans isomerase G
    Names
    PPIase G
    cyclophilin G
    matrin cyclophilin (matrin-cyp)
    matrin-cyp
    peptidyl-prolyl isomerase G
    rotamase G
    NP_113981.2
    XP_006234386.1
    XP_006234387.1
    XP_006234388.1
    XP_006234389.1
    XP_006234390.1
    XP_006234392.1
    XP_006234393.1
    XP_006234395.1
    XP_006234396.1
    XP_006234397.1
    XP_017447552.1
    XP_017447553.1
    XP_038961873.1
    XP_063140727.1
    XP_063140728.1
    XP_063140730.1

    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_001431479.1 → NP_001418408.1  peptidyl-prolyl cis-trans isomerase G

      Status: VALIDATED

      Source sequence(s)
      JAXUCZ010000003
      UniProtKB/TrEMBL
      A6HM13, G3V6Y9

    2. NM_001431480.1 → NP_001418409.1  peptidyl-prolyl cis-trans isomerase G

      Status: VALIDATED

      Source sequence(s)
      JAXUCZ010000003
      UniProtKB/TrEMBL
      A6HM13, G3V6Y9

    3. NM_001431481.1 → NP_001418410.1  peptidyl-prolyl cis-trans isomerase G

      Status: VALIDATED

      Source sequence(s)
      JAXUCZ010000003
      UniProtKB/TrEMBL
      A6HM13, G3V6Y9

    4. NM_001431482.1 → NP_001418411.1  peptidyl-prolyl cis-trans isomerase G

      Status: VALIDATED

      Source sequence(s)
      JAXUCZ010000003
      UniProtKB/TrEMBL
      A6HM13, G3V6Y9

    5. NM_001431483.1 → NP_001418412.1  peptidyl-prolyl cis-trans isomerase G

      Status: VALIDATED

      Source sequence(s)
      JAXUCZ010000003
      UniProtKB/TrEMBL
      A6HM13, G3V6Y9

    6. NM_001431484.1 → NP_001418413.1  peptidyl-prolyl cis-trans isomerase G

      Status: VALIDATED

      Source sequence(s)
      JAXUCZ010000003
      UniProtKB/TrEMBL
      A6HM13, G3V6Y9

    7. NM_001431485.1 → NP_001418414.1  peptidyl-prolyl cis-trans isomerase G

      Status: VALIDATED

      Source sequence(s)
      JAXUCZ010000003
      UniProtKB/TrEMBL
      A6HM13, G3V6Y9

    8. NM_001431486.1 → NP_001418415.1  peptidyl-prolyl cis-trans isomerase G

      Status: VALIDATED

      Source sequence(s)
      JAXUCZ010000003
      UniProtKB/TrEMBL
      A6HM13, G3V6Y9

    9. NM_001431487.1 → NP_001418416.1  peptidyl-prolyl cis-trans isomerase G

      Status: VALIDATED

      Source sequence(s)
      JAXUCZ010000003
      UniProtKB/TrEMBL
      A6HM13, G3V6Y9

    10. NM_001431488.1 → NP_001418417.1  peptidyl-prolyl cis-trans isomerase G

      Status: VALIDATED

      Source sequence(s)
      JAXUCZ010000003
      UniProtKB/TrEMBL
      A6HM13, G3V6Y9

    11. NM_031793.3 → NP_113981.2  peptidyl-prolyl cis-trans isomerase G

      Status: VALIDATED

      Source sequence(s)
      JAXUCZ010000003
      UniProtKB/Swiss-Prot
      O55035, Q5U346
      UniProtKB/TrEMBL
      A6HM13, G3V6Y9
      Related
      ENSRNOP00000010216.5, ENSRNOT00000010216.8
      Conserved Domains (1) summary
      cl00197
      Location:8 → 175
      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 immunosuppressive drug ...

    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_086021.1 Reference GRCr8

      Range
      74891846..74923010
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_006234335.5 → XP_006234397.1  peptidyl-prolyl cis-trans isomerase G isoform X1

      Conserved Domains (1) summary
      cl00197
      Location:8 → 175
      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 immunosuppressive drug ...

    2. XM_063284658.1 → XP_063140728.1  peptidyl-prolyl cis-trans isomerase G isoform X1

      UniProtKB/TrEMBL
      A6HM13, G3V6Y9

    3. XM_006234328.5 → XP_006234390.1  peptidyl-prolyl cis-trans isomerase G isoform X1

      Conserved Domains (1) summary
      cl00197
      Location:8 → 175
      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 immunosuppressive drug ...

    4. XM_006234331.5 → XP_006234393.1  peptidyl-prolyl cis-trans isomerase G isoform X1

      Conserved Domains (1) summary
      cl00197
      Location:8 → 175
      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 immunosuppressive drug ...

    5. XM_017592064.3 → XP_017447553.1  peptidyl-prolyl cis-trans isomerase G isoform X1

      UniProtKB/Swiss-Prot
      O55035, Q5U346
      UniProtKB/TrEMBL
      A6HM13, G3V6Y9
      Conserved Domains (1) summary
      cl00197
      Location:8 → 175
      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 immunosuppressive drug ...

    6. XM_006234326.5 → XP_006234388.1  peptidyl-prolyl cis-trans isomerase G isoform X1

      Conserved Domains (1) summary
      cl00197
      Location:8 → 175
      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 immunosuppressive drug ...

    7. XM_006234324.5 → XP_006234386.1  peptidyl-prolyl cis-trans isomerase G isoform X1

      Conserved Domains (1) summary
      cl00197
      Location:8 → 175
      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 immunosuppressive drug ...

    8. XM_017592063.3 → XP_017447552.1  peptidyl-prolyl cis-trans isomerase G isoform X1

      UniProtKB/Swiss-Prot
      O55035, Q5U346
      UniProtKB/TrEMBL
      A6HM13, G3V6Y9
      Conserved Domains (1) summary
      cl00197
      Location:8 → 175
      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 immunosuppressive drug ...

    9. XM_006234327.5 → XP_006234389.1  peptidyl-prolyl cis-trans isomerase G isoform X1

      Conserved Domains (1) summary
      cl00197
      Location:8 → 175
      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 immunosuppressive drug ...

    10. XM_006234333.5 → XP_006234395.1  peptidyl-prolyl cis-trans isomerase G isoform X1

      See identical proteins and their annotated locations for XP_006234395.1

      UniProtKB/Swiss-Prot
      O55035, Q5U346
      UniProtKB/TrEMBL
      A6HM13, G3V6Y9
      Conserved Domains (1) summary
      cl00197
      Location:8 → 175
      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 immunosuppressive drug ...

    11. XM_039105945.2 → XP_038961873.1  peptidyl-prolyl cis-trans isomerase G isoform X1

      Conserved Domains (1) summary
      cl00197
      Location:8 → 175
      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 immunosuppressive drug ...

    12. XM_006234325.4 → XP_006234387.1  peptidyl-prolyl cis-trans isomerase G isoform X1

      Conserved Domains (1) summary
      cl00197
      Location:8 → 175
      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 immunosuppressive drug ...

    13. XM_063284657.1 → XP_063140727.1  peptidyl-prolyl cis-trans isomerase G isoform X1

      UniProtKB/TrEMBL
      A6HM13, G3V6Y9

    14. XM_006234330.4 → XP_006234392.1  peptidyl-prolyl cis-trans isomerase G isoform X1

      Conserved Domains (1) summary
      cl00197
      Location:8 → 175
      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 immunosuppressive drug ...

    15. XM_006234334.4 → XP_006234396.1  peptidyl-prolyl cis-trans isomerase G isoform X1

      Conserved Domains (1) summary
      cl00197
      Location:8 → 175
      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 immunosuppressive drug ...

    16. XM_063284660.1 → XP_063140730.1  peptidyl-prolyl cis-trans isomerase G isoform X2

    Nucleotide Protein Strain
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    O55035.2 GenPept UniProtKB/Swiss-Prot:O55035

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