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    Clpp caseinolytic mitochondrial matrix peptidase proteolytic subunit [ Rattus norvegicus (Norway rat) ]

    Gene ID: 301117, updated on 28-Oct-2024

    Summary

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    Official Symbol
    Clppprovided by RGD
    Official Full Name
    caseinolytic mitochondrial matrix peptidase proteolytic subunitprovided by RGD
    Primary source
    RGD:1588583
    See related
    EnsemblRapid:ENSRNOG00000047052 AllianceGenome:RGD:1588583
    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 identical protein binding activity. Predicted to be involved in membrane protein proteolysis and protein quality control for misfolded or incompletely synthesized proteins. Predicted to be located in mitochondrial matrix. Predicted to be part of endopeptidase Clp complex. Human ortholog(s) of this gene implicated in Perrault syndrome. Orthologous to human CLPP (caseinolytic mitochondrial matrix peptidase proteolytic subunit). [provided by Alliance of Genome Resources, Oct 2024]
    Expression
    Biased expression in Heart (RPKM 56.5), Adrenal (RPKM 53.4) and 9 other tissues See more
    Orthologs
    human mouse all
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    Genomic context

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    See Clpp in Genome Data Viewer
    Location:
    9q11
    Exon count:
    6
    Annotation release Status Assembly Chr Location
    RS_2024_02 current GRCr8 (GCF_036323735.1) 9 NC_086027.1 (1917305..1924706)
    RS_2023_06 previous assembly mRatBN7.2 (GCF_015227675.2) 9 NC_051344.1 (1831680..1837700)
    106 previous assembly Rnor_6.0 (GCF_000001895.5) 9 NC_005108.4 (10048715..10056068, complement)

    Chromosome 9 - NC_086027.1Genomic Context describing neighboring genes Neighboring gene BCL2 interacting protein 3, pseudogene 5 Neighboring gene alkaline ceramidase 1 Neighboring gene alkB homolog 7 Neighboring gene persephin Neighboring gene general transcription factor IIF subunit 1

    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 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. Human mitochondrial ClpP is a stable heptamer that assembles into a tetradecamer in the presence of ClpX. Kang SG, et al. J Biol Chem, 2005 Oct 21. PMID 16115876
    2. Functional proteolytic complexes of the human mitochondrial ATP-dependent protease, hClpXP. Kang SG, et al. J Biol Chem, 2002 Jun 7. PMID 11923310
    3. Mitochondrial localization and oligomeric structure of HClpP, the human homologue of E. coli ClpP. de Sagarra MR, et al. J Mol Biol, 1999 Oct 1. PMID 10525407
    4. Characterization of mouse Clpp protease cDNA, gene, and protein. Andresen BS, et al. Mamm Genome, 2000 Apr. PMID 10754102
    5. Mitochondrial processing peptidase regulates PINK1 processing, import and Parkin recruitment. Greene AW, et al. EMBO Rep, 2012 Apr. PMID 22354088, Free PMC Article

    See all (9) citations in PubMed

    GeneRIFs: Gene References Into Functions

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Markers

    Homology

    Gene Ontology Provided by RGD

    Function Evidence Code Pubs
    enables ATP-dependent peptidase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables ATPase binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables endopeptidase activity ISO
    Inferred from Sequence Orthology
    more info
    		  
    enables identical protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables serine-type endopeptidase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables serine-type endopeptidase activity ISO
    Inferred from Sequence Orthology
    more info
    		  
    Process Evidence Code Pubs
    involved_in membrane protein proteolysis ISO
    Inferred from Sequence Orthology
    more info
    		  
    involved_in protein quality control for misfolded or incompletely synthesized proteins IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in proteolysis ISO
    Inferred from Sequence Orthology
    more info
    		  
    involved_in proteolysis involved in protein catabolic process ISO
    Inferred from Sequence Orthology
    more info
    		  
    Component Evidence Code Pubs
    part_of endopeptidase Clp complex IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    part_of endopeptidase Clp complex ISO
    Inferred from Sequence Orthology
    more info
    		  
    located_in mitochondrial matrix ISO
    Inferred from Sequence Orthology
    more info
    		  
    located_in mitochondrion ISO
    Inferred from Sequence Orthology
    more info
    		  

    General protein information

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    Preferred Names
    ATP-dependent Clp protease proteolytic subunit, mitochondrial
    Names
    ClpP caseinolytic peptidase, ATP-dependent, proteolytic subunit homolog
    caseinolytic peptidase, ATP-dependent, proteolytic subunit homolog
    putative ATP-dependent Clp protease proteolytic subunit, mitochondrial
    NP_001386216.1
    XP_038940263.1
    XP_038940264.1

    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_001399287.1 → NP_001386216.1  ATP-dependent Clp protease proteolytic subunit, mitochondrial precursor

      Status: VALIDATED

      Source sequence(s)
      JAXUCZ010000009
      Related
      ENSRNOP00000066481.2, ENSRNOT00000072001.4
      Conserved Domains (1) summary
      PRK00277
      Location:53 → 245
      clpP; ATP-dependent Clp protease proteolytic subunit; Reviewed

    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_086027.1 Reference GRCr8

      Range
      1917305..1924706
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_039084335.2 → XP_038940263.1  ATP-dependent Clp protease proteolytic subunit, mitochondrial isoform X1

      Conserved Domains (1) summary
      cl23717
      Location:114 → 182
      crotonase-like; Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse set of enzymes including enoyl-CoA hydratase, napthoate synthase, methylmalonyl-CoA decarboxylase, 3-hydoxybutyryl-CoA dehydratase, and dienoyl-CoA isomerase. ...

    2. XM_039084336.2 → XP_038940264.1  ATP-dependent Clp protease proteolytic subunit, mitochondrial isoform X2

      Conserved Domains (1) summary
      cl23717
      Location:98 → 163
      crotonase-like; Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse set of enzymes including enoyl-CoA hydratase, napthoate synthase, methylmalonyl-CoA decarboxylase, 3-hydoxybutyryl-CoA dehydratase, and dienoyl-CoA isomerase. ...
    Nucleotide Protein Strain
    Heading Accession and Version

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