LOCUS       NP_059089                272 aa            linear   ROD 07-FEB-2025
DEFINITION  ATP-dependent Clp protease proteolytic subunit, mitochondrial
            precursor [Mus musculus].
ACCESSION   NP_059089
VERSION     NP_059089.1
DBSOURCE    REFSEQ: accession NM_017393.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Xu,L., Tan,C., Barr,J., Talaba,N., Verheyden,J., Chin,J.S.,
            Gaboyan,S., Kasaraneni,N., Elgamal,R.M., Gaulton,K.J., Lin,G.,
            Afshar,K., Golts,E., Meier,A., Crotty Alexander,L.E., Borok,Z.,
            Shen,Y., Chung,W.K., McCulley,D.J. and Sun,X.
  TITLE     Context-dependent roles of mitochondrial LONP1 in orchestrating the
            balance between airway progenitor versus progeny cells
  JOURNAL   Cell Stem Cell 31 (10), 1465-1483 (2024)
   PUBMED   39181129
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Key,J., Gispert,S. and Auburger,G.
  TITLE     Knockout Mouse Studies Show That Mitochondrial CLPP Peptidase and
            CLPX Unfoldase Act in Matrix Condensates near IMM, as Fast Stress
            Response in Protein Assemblies for Transcript Processing,
            Translation, and Heme Production
  JOURNAL   Genes (Basel) 15 (6), 694 (2024)
   PUBMED   38927630
  REMARK    GeneRIF: Knockout Mouse Studies Show That Mitochondrial CLPP
            Peptidase and CLPX Unfoldase Act in Matrix Condensates near IMM, as
            Fast Stress Response in Protein Assemblies for Transcript
            Processing, Translation, and Heme Production.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Key,J., Gispert,S., Kandi,A.R., Heinz,D., Hamann,A., Osiewacz,H.D.,
            Meierhofer,D. and Auburger,G.
  TITLE     CLPP-Null Eukaryotes with Excess Heme Biosynthesis Show Reduced
            L-arginine Levels, Probably via CLPX-Mediated OAT Activation
  JOURNAL   Biomolecules 14 (2), 241 (2024)
   PUBMED   38397478
  REMARK    GeneRIF: CLPP-Null Eukaryotes with Excess Heme Biosynthesis Show
            Reduced L-arginine Levels, Probably via CLPX-Mediated OAT
            Activation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 272)
  AUTHORS   Ergun,Y., Imamoglu,A.G., Cozzolino,M., Demirkiran,C., Basar,M.,
            Garg,A., Yildirim,R.M. and Seli,E.
  TITLE     Mitochondrial Unfolded Protein Response Gene Clpp Is Required for
            Oocyte Function and Female Fertility
  JOURNAL   Int J Mol Sci 25 (3), 1866 (2024)
   PUBMED   38339144
  REMARK    GeneRIF: Mitochondrial Unfolded Protein Response Gene Clpp Is
            Required for Oocyte Function and Female Fertility.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 272)
  AUTHORS   Guillon,B., Bulteau,A.L., Wattenhofer-Donze,M., Schmucker,S.,
            Friguet,B., Puccio,H., Drapier,J.C. and Bouton,C.
  TITLE     Frataxin deficiency causes upregulation of mitochondrial Lon and
            ClpP proteases and severe loss of mitochondrial Fe-S proteins
  JOURNAL   FEBS J 276 (4), 1036-1047 (2009)
   PUBMED   19154341
  REMARK    GeneRIF: The correlative effect of Lon and ClpP upregulation on
            loss of mitochondrial Fe-S proteins during the progression of the
            disease may suggest that Fe-S proteins are potential targets of Lon
            and ClpP proteases in FRDA.
REFERENCE   7  (residues 1 to 272)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   8  (residues 1 to 272)
  AUTHORS   Andresen,B.S., Corydon,T.J., Wilsbech,M., Bross,P., Schroeder,L.D.,
            Hindkjaer,T.F., Bolund,L. and Gregersen,N.
  TITLE     Characterization of mouse Clpp protease cDNA, gene, and protein
  JOURNAL   Mamm Genome 11 (4), 275-280 (2000)
   PUBMED   10754102
REFERENCE   9  (residues 1 to 272)
  AUTHORS   Santagata,S., Bhattacharyya,D., Wang,F.H., Singha,N., Hodtsev,A.
            and Spanopoulou,E.
  TITLE     Molecular cloning and characterization of a mouse homolog of
            bacterial ClpX, a novel mammalian class II member of the Hsp100/Clp
            chaperone family
  JOURNAL   J Biol Chem 274 (23), 16311-16319 (1999)
   PUBMED   10347188
REFERENCE   10 (residues 1 to 272)
  AUTHORS   Ko,M.S., Threat,T.A., Wang,X., Horton,J.H., Cui,Y., Wang,X.,
            Pryor,E., Paris,J., Wells-Smith,J., Kitchen,J.R., Rowe,L.B.,
            Eppig,J., Satoh,T., Brant,L., Fujiwara,H., Yotsumoto,S. and
            Nakashima,H.
  TITLE     Genome-wide mapping of unselected transcripts from extraembryonic
            tissue of 7.5-day mouse embryos reveals enrichment in the t-complex
            and under-representation on the X chromosome
  JOURNAL   Hum Mol Genet 7 (12), 1967-1978 (1998)
   PUBMED   9811942
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY294002.1, AK145765.1 and AC073683.3.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC001998.1, AK145765.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="17"
                     /map="17 29.61 cM"
     Protein         1..272
                     /product="ATP-dependent Clp protease proteolytic subunit,
                     mitochondrial precursor"
                     /EC_number="3.4.21.92"
                     /note="putative ATP-dependent Clp protease proteolytic
                     subunit, mitochondrial; endopeptidase Clp; caseinolytic
                     protease, ATP-dependent, proteolytic subunit homolog;
                     caseinolytic peptidase, ATP-dependent, proteolytic subunit
                     homolog; ClpP caseinolytic peptidase, ATP-dependent,
                     proteolytic subunit"
                     /calculated_mol_wt=24101
     transit_peptide 1..52
                     /note="Mitochondrion. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (O88696.1)"
                     /calculated_mol_wt=5718
     mat_peptide     53..272
                     /product="ATP-dependent Clp protease proteolytic subunit,
                     mitochondrial. /id=PRO_0000005517"
                     /note="propagated from UniProtKB/Swiss-Prot (O88696.1)"
                     /calculated_mol_wt=24101
     Region          53..245
                     /region_name="clpP"
                     /note="ATP-dependent Clp protease proteolytic subunit;
                     Reviewed; PRK00277"
                     /db_xref="CDD:178955"
     Site            order(82,84,93..94,97..98,101,116,123,127,130,133..134,
                     138,146,168,170,176..179,193,196,198,200,223,225)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:132928"
     Site            order(149,174,223)
                     /site_type="active"
                     /note="active site residues [active]"
                     /db_xref="CDD:132928"
     Site            207
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (O88696.1)"
     Region          240..272
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88696.1)"
     CDS             1..272
                     /gene="Clpp"
                     /gene_synonym="D17Wsu160e"
                     /coded_by="NM_017393.2:65..883"
                     /db_xref="CCDS:CCDS28920.1"
                     /db_xref="GeneID:53895"
                     /db_xref="MGI:MGI:1858213"
ORIGIN      
        1 mwprvllgea rvavdgcral lsrlavhfsp pwtavscspl rrslhgtatr afplipivve
       61 qtgrgerayd iysrllreri vcvmgpidds vaslviaqll flqsesnkkp ihmyinspgg
      121 vvtaglaiyd tmqyilnpic twcvgqaasm gslllaagsp gmrhslpnsr imihqpsgga
      181 rgqatdiaiq aeeimklkkq lyniyakhtk qslqviesam erdrymspme aqefgildkv
      241 lvhppqdged epelvqketa taptdppapt st
//
