CLPX_MOUSE
ID CLPX_MOUSE Reviewed; 634 AA.
AC Q9JHS4; E9QLZ8; Q9WVD1;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial;
DE Flags: Precursor;
GN Name=Clpx;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=11003706; DOI=10.1007/s003350010173;
RA Corydon T.J., Wilsbech M., Jespersgaard C., Andresen B.S., Borglum A.D.,
RA Pedersen S., Bolund L., Gregersen N., Bross P.;
RT "Human and mouse mitochondrial orthologs of bacterial ClpX.";
RL Mamm. Genome 11:899-905(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF LYS-300.
RC STRAIN=BALB/cJ;
RX PubMed=10347188; DOI=10.1074/jbc.274.23.16311;
RA Santagata S., Bhattacharyya D., Wang F.H., Singha N., Hodtsev A.,
RA Spanopoulou E.;
RT "Molecular cloning and characterization of a mouse homolog of bacterial
RT ClpX, a novel mammalian class II member of the Hsp100/Clp chaperone
RT family.";
RL J. Biol. Chem. 274:16311-16319(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=22710082; DOI=10.1016/j.jsb.2012.06.001;
RA Lowth B.R., Kirstein-Miles J., Saiyed T., Broetz-Oesterhelt H.,
RA Morimoto R.I., Truscott K.N., Dougan D.A.;
RT "Substrate recognition and processing by a Walker B mutant of the human
RT mitochondrial AAA+ protein CLPX.";
RL J. Struct. Biol. 179:193-201(2012).
CC -!- FUNCTION: ATP-dependent specificity component of the Clp protease
CC complex. Hydrolyzes ATP. Targets specific substrates for degradation by
CC the Clp complex. Can perform chaperone functions in the absence of
CC CLPP. Enhances the DNA-binding activity of TFAM and is required for
CC maintaining a normal mitochondrial nucleoid structure
CC (PubMed:10347188). ATP-dependent unfoldase that stimulates the
CC incorporation of the pyridoxal phosphate cofactor into 5-
CC aminolevulinate synthase, thereby activating 5-aminolevulinate (ALA)
CC synthesis, the first step in heme biosynthesis. Important for efficient
CC erythropoiesis through up-regulation of heme biosynthesis (By
CC similarity). {ECO:0000250|UniProtKB:O76031,
CC ECO:0000269|PubMed:10347188}.
CC -!- SUBUNIT: Homohexamer that forms a ring structure; this hexamerization
CC requires ATP binding. Component of the Clp complex formed by the
CC assembly of two CLPP heptameric rings with two CLPX hexameric rings,
CC giving rise to a symmetrical structure with two central CLPP rings
CC flanked by a CLPX ring at either end of the complex (PubMed:22710082).
CC Interacts with TFAM (By similarity). {ECO:0000250|UniProtKB:O76031,
CC ECO:0000269|PubMed:22710082}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:22710082}.
CC Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in liver (at protein level).
CC {ECO:0000269|PubMed:22710082}.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000255|PROSITE-
CC ProRule:PRU01250}.
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DR EMBL; AJ276991; CAC01232.1; -; mRNA.
DR EMBL; AF134983; AAD42187.1; -; mRNA.
DR EMBL; AC110235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS23288.1; -.
DR RefSeq; NP_035932.2; NM_011802.3.
DR AlphaFoldDB; Q9JHS4; -.
DR SMR; Q9JHS4; -.
DR BioGRID; 234776; 5.
DR STRING; 10090.ENSMUSP00000015501; -.
DR iPTMnet; Q9JHS4; -.
DR PhosphoSitePlus; Q9JHS4; -.
DR EPD; Q9JHS4; -.
DR jPOST; Q9JHS4; -.
DR MaxQB; Q9JHS4; -.
DR PaxDb; Q9JHS4; -.
DR PeptideAtlas; Q9JHS4; -.
DR PRIDE; Q9JHS4; -.
DR ProteomicsDB; 285494; -.
DR Antibodypedia; 51984; 99 antibodies from 25 providers.
DR DNASU; 270166; -.
DR Ensembl; ENSMUST00000015501; ENSMUSP00000015501; ENSMUSG00000015357.
DR GeneID; 270166; -.
DR KEGG; mmu:270166; -.
DR UCSC; uc009qdb.2; mouse.
DR CTD; 10845; -.
DR MGI; MGI:1346017; Clpx.
DR VEuPathDB; HostDB:ENSMUSG00000015357; -.
DR eggNOG; KOG0745; Eukaryota.
DR GeneTree; ENSGT00390000017625; -.
DR InParanoid; Q9JHS4; -.
DR OMA; YKIWTKG; -.
DR OrthoDB; 1040247at2759; -.
DR PhylomeDB; Q9JHS4; -.
DR TreeFam; TF312884; -.
DR BioGRID-ORCS; 270166; 11 hits in 72 CRISPR screens.
DR ChiTaRS; Clpx; mouse.
DR PRO; PR:Q9JHS4; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9JHS4; protein.
DR Bgee; ENSMUSG00000015357; Expressed in spermatid and 241 other tissues.
DR ExpressionAtlas; Q9JHS4; baseline and differential.
DR Genevisible; Q9JHS4; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0009368; C:endopeptidase Clp complex; ISS:UniProtKB.
DR GO; GO:0009841; C:mitochondrial endopeptidase Clp complex; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IDA:MGI.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:MGI.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; ISO:MGI.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0016504; F:peptidase activator activity; ISO:MGI.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0046034; P:ATP metabolic process; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010603; Znf_CppX_C4.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00382; clpX; 1.
DR PROSITE; PS51902; CLPX_ZB; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Chaperone; Metal-binding; Mitochondrion;
KW Mitochondrion nucleoid; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..56
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 57..634
FT /note="ATP-dependent Clp protease ATP-binding subunit clpX-
FT like, mitochondrial"
FT /id="PRO_0000005519"
FT DOMAIN 94..147
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT REGION 69..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 295..302
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 438
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O76031"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O76031"
FT MUTAGEN 300
FT /note="K->A: Loss of ATP hydrolysis."
FT /evidence="ECO:0000269|PubMed:10347188"
FT CONFLICT 37
FT /note="V -> M (in Ref. 2; AAD42187)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="G -> A (in Ref. 2; AAD42187)"
FT /evidence="ECO:0000305"
FT CONFLICT 457..458
FT /note="Missing (in Ref. 2; AAD42187)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="A -> R (in Ref. 1; CAC01232)"
FT /evidence="ECO:0000305"
FT CONFLICT 631
FT /note="A -> R (in Ref. 2; AAD42187)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 634 AA; 69229 MW; E6AF4326113B7072 CRC64;
MSSCGACTCG AAAARLLTTS LTSAQRGISC GRIHVPVLGR LGTTLDAQAL RRAPLRTFSE
TPAYFASKDG ANKDGSGDGN KKSVTEGSSK KSGSGNSGKG GNQLRCPKCG DLCTHVETFV
SSTRFVKCEK CHHFFVVLSE ADSKKSIIKE PESAAEAVKL AFQQKPPPPP KKIYNYLDKY
VVGQSFAKKV LSVAVYNHYK RIYNNIPANL RQQAEAEKQT SLTPRELEIR RREDEYRFTK
LLQIAGISPH GNALGASMQQ QVNQQMPQEK RGGEVLDSSQ DDIKLEKSNI LLLGPTGSGK
TLLAQTLAKC LDVPFAICDC TTLTQAGYVG EDIESVIAKL LQDANYNVEK AQQGIVFLDE
VDKIGSVPGI HQLRDVGGEG VQQGLLKLLE GTIVNVPEKN SRKLRGETVQ VDTTNVLFVA
SGAFNGLDRI ISRRKNEKYL GFGTPSNLGK GRRAAAAADL ANRSGESNTH QDIEEKDRLL
RHVEARDLIE FGMIPEFVGR LPVVVPLHSL DEKTLVQILT EPRNAVIPQY QALFSMDKCE
LNVTEDALKA IARLALERKT GARGLRSIME KLLLEPMFEV PNSDIVCVEV DKEVVEGKKE
PGYIRAPSKE SSEEEYDSGV EEDGWPRQAD AANS
