LOCUS       NP_035932                634 aa            linear   ROD 16-FEB-2025
DEFINITION  ATP-dependent clpX-like chaperone, mitochondrial isoform 1 [Mus
            musculus].
ACCESSION   NP_035932
VERSION     NP_035932.2
DBSOURCE    REFSEQ: accession NM_011802.3
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 634)
  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   2  (residues 1 to 634)
  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   3  (residues 1 to 634)
  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   4  (residues 1 to 634)
  AUTHORS   Guo,C., Xiao,Y., Gu,J., Zhao,P., Hu,Z., Zheng,J., Hua,R., Hai,Z.,
            Su,J., Zhang,J.V., Yeung,W.S.B. and Wang,T.
  TITLE     ClpP/ClpX deficiency impairs mitochondrial functions and mTORC1
            signaling during spermatogenesis
  JOURNAL   Commun Biol 6 (1), 1012 (2023)
   PUBMED   37798322
  REMARK    GeneRIF: ClpP/ClpX deficiency impairs mitochondrial functions and
            mTORC1 signaling during spermatogenesis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 634)
  AUTHORS   Key,J., Torres-Odio,S., Bach,N.C., Gispert,S., Koepf,G.,
            Reichlmeir,M., West,A.P., Prokisch,H., Freisinger,P., Newman,W.G.,
            Shalev,S., Sieber,S.A., Wittig,I. and Auburger,G.
  TITLE     Inactivity of Peptidase ClpP Causes Primary Accumulation of
            Mitochondrial Disaggregase ClpX with Its Interacting Nucleoid
            Proteins, and of mtDNA
  JOURNAL   Cells 10 (12), 3354 (2021)
   PUBMED   34943861
  REMARK    GeneRIF: Inactivity of Peptidase ClpP Causes Primary Accumulation
            of Mitochondrial Disaggregase ClpX with Its Interacting Nucleoid
            Proteins, and of mtDNA.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 634)
  AUTHORS   Da Cruz,S., Xenarios,I., Langridge,J., Vilbois,F., Parone,P.A. and
            Martinou,J.C.
  TITLE     Proteomic analysis of the mouse liver mitochondrial inner membrane
  JOURNAL   J Biol Chem 278 (42), 41566-41571 (2003)
   PUBMED   12865426
REFERENCE   7  (residues 1 to 634)
  AUTHORS   Carninci,P., Waki,K., Shiraki,T., Konno,H., Shibata,K., Itoh,M.,
            Aizawa,K., Arakawa,T., Ishii,Y., Sasaki,D., Bono,H., Kondo,S.,
            Sugahara,Y., Saito,R., Osato,N., Fukuda,S., Sato,K., Watahiki,A.,
            Hirozane-Kishikawa,T., Nakamura,M., Shibata,Y., Yasunishi,A.,
            Kikuchi,N., Yoshiki,A., Kusakabe,M., Gustincich,S., Beisel,K.,
            Pavan,W., Aidinis,V., Nakagawara,A., Held,W.A., Iwata,H., Kono,T.,
            Nakauchi,H., Lyons,P., Wells,C., Hume,D.A., Fagiolini,M.,
            Hensch,T.K., Brinkmeier,M., Camper,S., Hirota,J., Mombaerts,P.,
            Muramatsu,M., Okazaki,Y., Kawai,J. and Hayashizaki,Y.
  TITLE     Targeting a complex transcriptome: the construction of the mouse
            full-length cDNA encyclopedia
  JOURNAL   Genome Res 13 (6B), 1273-1289 (2003)
   PUBMED   12819125
REFERENCE   8  (residues 1 to 634)
  AUTHORS   Tomoyasu,T., Ohkishi,T., Ukyo,Y., Tokumitsu,A., Takaya,A.,
            Suzuki,M., Sekiya,K., Matsui,H., Kutsukake,K. and Yamamoto,T.
  TITLE     The ClpXP ATP-dependent protease regulates flagellum synthesis in
            Salmonella enterica serovar typhimurium
  JOURNAL   J Bacteriol 184 (3), 645-653 (2002)
   PUBMED   11790733
REFERENCE   9  (residues 1 to 634)
  AUTHORS   Corydon,T.J., Wilsbech,M., Jespersgaard,C., Andresen,B.S.,
            Borglum,A.D., Pedersen,S., Bolund,L., Gregersen,N. and Bross,P.
  TITLE     Human and mouse mitochondrial orthologs of bacterial ClpX
  JOURNAL   Mamm Genome 11 (10), 899-905 (2000)
   PUBMED   11003706
REFERENCE   10 (residues 1 to 634)
  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
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC110235.13, AK080339.1, AK087848.1 and AV237409.1.
            
            On Aug 26, 2006 this sequence version replaced NP_035932.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            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 :: AK087848.1, AF134983.1 [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 conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..634
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 35.22 cM"
     Protein         1..634
                     /product="ATP-dependent clpX-like chaperone, mitochondrial
                     isoform 1"
                     /EC_number="3.6.4.10"
                     /note="caseinolytic protease X; ATP-dependent CLP protease
                     ATP-binding subunit ClpX-like, mitochondrial; caseinolytic
                     peptidase X; ATP-dependent clpX-like chaperone,
                     mitochondrial"
                     /calculated_mol_wt=63535
     transit_peptide 1..56
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q9JHS4.2)"
                     /calculated_mol_wt=5712
     mat_peptide     57..634
                     /product="ATP-dependent clpX-like chaperone,
                     mitochondrial. /id=PRO_0000005519"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JHS4.2)"
                     /calculated_mol_wt=63535
     Region          69..102
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JHS4.2)"
     Region          105..133
                     /region_name="Zn-ribbon"
                     /note="C-terminal zinc ribbon domain of RNA polymerase
                     intrinsic transcript cleavage subunit; cl02609"
                     /db_xref="CDD:445850"
     Site            order(106,109,128,131)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:259791"
     Region          173..606
                     /region_name="ClpX"
                     /note="ATP-dependent protease Clp, ATPase subunit ClpX
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1219"
                     /db_xref="CDD:440832"
     Region          204..>308
                     /region_name="DnaC"
                     /note="DNA replication protein DnaC [Replication,
                     recombination and repair]; COG1484"
                     /db_xref="CDD:441093"
     Site            438
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O76031; propagated from
                     UniProtKB/Swiss-Prot (Q9JHS4.2)"
     Region          599..634
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JHS4.2)"
     Site            618
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O76031; propagated from
                     UniProtKB/Swiss-Prot (Q9JHS4.2)"
     CDS             1..634
                     /gene="Clpx"
                     /gene_synonym="E330029I21"
                     /coded_by="NM_011802.3:228..2132"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS23288.1"
                     /db_xref="GeneID:270166"
                     /db_xref="MGI:MGI:1346017"
ORIGIN      
        1 msscgactcg aaaarlltts ltsaqrgisc grihvpvlgr lgttldaqal rraplrtfse
       61 tpayfaskdg ankdgsgdgn kksvtegssk ksgsgnsgkg gnqlrcpkcg dlcthvetfv
      121 sstrfvkcek chhffvvlse adskksiike pesaaeavkl afqqkppppp kkiynyldky
      181 vvgqsfakkv lsvavynhyk riynnipanl rqqaeaekqt sltpreleir rredeyrftk
      241 llqiagisph gnalgasmqq qvnqqmpqek rggevldssq ddikleksni lllgptgsgk
      301 tllaqtlakc ldvpfaicdc ttltqagyvg ediesviakl lqdanynvek aqqgivflde
      361 vdkigsvpgi hqlrdvggeg vqqgllklle gtivnvpekn srklrgetvq vdttnvlfva
      421 sgafngldri isrrknekyl gfgtpsnlgk grraaaaadl anrsgesnth qdieekdrll
      481 rhveardlie fgmipefvgr lpvvvplhsl dektlvqilt eprnavipqy qalfsmdkce
      541 lnvtedalka iarlalerkt garglrsime klllepmfev pnsdivcvev dkevvegkke
      601 pgyirapske sseeeydsgv eedgwprqad aans
//
