CLPB_MOUSE
ID CLPB_MOUSE Reviewed; 677 AA.
AC Q60649;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Caseinolytic peptidase B protein homolog;
DE EC=3.6.1.- {ECO:0000250|UniProtKB:Q9H078};
DE AltName: Full=Suppressor of potassium transport defect 3;
DE Flags: Precursor;
GN Name=Clpb; Synonyms=Skd3;
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=7835694; DOI=10.1016/0378-1119(94)00697-q;
RA Perier F., Radeke C.M., Raab-Graham K.F., Vandenberg C.A.;
RT "Expression of a putative ATPase suppresses the growth defect of a yeast
RT potassium transport mutant: identification of a mammalian member of the
RT Clp/HSP104 family.";
RL Gene 152:157-163(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 574-590, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, and Pancreas;
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).
CC -!- FUNCTION: May function as a regulatory ATPase and be related to
CC secretion/protein trafficking process. Involved in mitochondrial-
CC mediated antiviral innate immunity, activates RIG-I-mediated signal
CC transduction and production of IFNB1 and pro-inflammatory cytokine IL6.
CC {ECO:0000250|UniProtKB:Q9H078}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9H078};
CC -!- SUBUNIT: Interacts with PHB and PHB2. Interacts with MAVS; the
CC interaction is enhanced by Sendai virus infection.
CC {ECO:0000250|UniProtKB:Q9H078}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000250|UniProtKB:Q9H078}.
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in testis.
CC Also expressed in heart, skeletal muscle and kidney.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
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DR EMBL; U09874; AAA62869.1; -; mRNA.
DR EMBL; BC048175; AAH48175.1; -; mRNA.
DR CCDS; CCDS21513.1; -.
DR PIR; I49045; I49045.
DR RefSeq; NP_033217.1; NM_009191.3.
DR AlphaFoldDB; Q60649; -.
DR SMR; Q60649; -.
DR BioGRID; 203267; 7.
DR IntAct; Q60649; 1.
DR MINT; Q60649; -.
DR STRING; 10090.ENSMUSP00000001884; -.
DR PhosphoSitePlus; Q60649; -.
DR SwissPalm; Q60649; -.
DR REPRODUCTION-2DPAGE; Q60649; -.
DR EPD; Q60649; -.
DR jPOST; Q60649; -.
DR MaxQB; Q60649; -.
DR PaxDb; Q60649; -.
DR PRIDE; Q60649; -.
DR ProteomicsDB; 283861; -.
DR Antibodypedia; 30838; 198 antibodies from 27 providers.
DR DNASU; 20480; -.
DR Ensembl; ENSMUST00000001884; ENSMUSP00000001884; ENSMUSG00000001829.
DR GeneID; 20480; -.
DR KEGG; mmu:20480; -.
DR UCSC; uc009ipb.1; mouse.
DR CTD; 81570; -.
DR MGI; MGI:1100517; Clpb.
DR VEuPathDB; HostDB:ENSMUSG00000001829; -.
DR eggNOG; KOG1051; Eukaryota.
DR GeneTree; ENSGT00390000012961; -.
DR HOGENOM; CLU_005070_9_3_1; -.
DR InParanoid; Q60649; -.
DR OMA; CKNAIFI; -.
DR TreeFam; TF328654; -.
DR BioGRID-ORCS; 20480; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Clpb; mouse.
DR PRO; PR:Q60649; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q60649; protein.
DR Bgee; ENSMUSG00000001829; Expressed in spermatid and 243 other tissues.
DR ExpressionAtlas; Q60649; baseline and differential.
DR Genevisible; Q60649; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140374; P:antiviral innate immune response; ISO:MGI.
DR GO; GO:0034605; P:cellular response to heat; ISO:MGI.
DR GO; GO:0039529; P:RIG-I signaling pathway; ISO:MGI.
DR Gene3D; 1.25.40.20; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00248; ANK; 3.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
PE 1: Evidence at protein level;
KW Acetylation; ANK repeat; ATP-binding; Direct protein sequencing; Hydrolase;
KW Mitochondrion; Nucleotide-binding; Reference proteome; Repeat;
KW Transit peptide.
FT TRANSIT 1..50
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 51..677
FT /note="Caseinolytic peptidase B protein homolog"
FT /id="PRO_0000191240"
FT REPEAT 133..162
FT /note="ANK 1"
FT REPEAT 166..195
FT /note="ANK 2"
FT REPEAT 235..265
FT /note="ANK 3"
FT REPEAT 268..297
FT /note="ANK 4"
FT REGION 85..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 351..358
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 559
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H078"
SQ SEQUENCE 677 AA; 76004 MW; F2E5921E44ECCEB2 CRC64;
MMLSAVLRRT TPAPRLFLGL IKSPSLQSRG GAYGRGVVTG DRGEPQRLRA AAWVRPGASS
TFVPGRGAAT WGRRGERTEI PYLTAASSER GPSPEETLPG QDSWNGVPNK TGLGMWALAM
ALVVQCYSKN PSNKDAALME AARANNVQEV RRLLSEGADV NARHKLGWTA LMVASISHNE
SVVQVLLAAG ADPNLGDEFS SVYKTANEQG VHSLEVLVTR EDDFNNRLNH RASFKGCTAL
HYAVLADDYS IVKELLDRGA NPLQRNEMGH TPLDYAREGE VMKLLKTSET KYMEKQRKRE
AEERRRFPLE QRLKEHIIGQ ESAIATVGAA IRRKENGWYD EEHPLVFLFL GSSGIGKTEL
AKQTAKYMHK DAKKGFIRLD MSEFQERHEV AKFIGSPPGY IGHEEGGQLT KKLKQCPNAV
VLFDEVDKAH PDVLTIMLQL FDEGRLTDGK GKTIDCKDAI FIMTSNVASD EIAQHALQLR
QEALEMSRNR IAENLGDVQM SDKITISKNF KENVIRPILK AHFRRDEFLG RINEIVYFLP
FCHSELIQLV NKELNFWAKR AKQRHNITLL WDREVADVLV DGYNVHYGAR SIKHEVERRV
VNQLAAAYEQ DLLPGGCTLR ITVEDSDKHL LKSPELPSPQ AEKRPPTLRL EIIDKDSKTR
KLDIQAPLHP EKVCYTI
