CLPB_BOVIN
ID CLPB_BOVIN Reviewed; 677 AA.
AC Q5E9N5;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
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DR EMBL; BT020885; AAX08902.1; -; mRNA.
DR EMBL; BC103469; AAI03470.1; -; mRNA.
DR RefSeq; NP_001015625.1; NM_001015625.1.
DR AlphaFoldDB; Q5E9N5; -.
DR SMR; Q5E9N5; -.
DR STRING; 9913.ENSBTAP00000001687; -.
DR PaxDb; Q5E9N5; -.
DR PRIDE; Q5E9N5; -.
DR Ensembl; ENSBTAT00000001687; ENSBTAP00000001687; ENSBTAG00000001280.
DR GeneID; 520639; -.
DR KEGG; bta:520639; -.
DR CTD; 81570; -.
DR VEuPathDB; HostDB:ENSBTAG00000001280; -.
DR VGNC; VGNC:27458; CLPB.
DR eggNOG; KOG1051; Eukaryota.
DR GeneTree; ENSGT00390000012961; -.
DR HOGENOM; CLU_005070_9_3_1; -.
DR InParanoid; Q5E9N5; -.
DR OMA; CKNAIFI; -.
DR OrthoDB; 611758at2759; -.
DR TreeFam; TF328654; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000001280; Expressed in spermatid and 110 other tissues.
DR ExpressionAtlas; Q5E9N5; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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; IEA:Ensembl.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0039529; P:RIG-I signaling pathway; IEA:Ensembl.
DR Gene3D; 1.25.40.20; -; 1.
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; 2.
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 2: Evidence at transcript level;
KW Acetylation; ANK repeat; ATP-binding; Hydrolase; Mitochondrion;
KW Nucleotide-binding; Reference proteome; Repeat; Transit peptide.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 29..677
FT /note="Caseinolytic peptidase B protein homolog"
FT /id="PRO_0000286349"
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 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; 75440 MW; EBFE78C4376E0A80 CRC64;
MLGSLVSKRT APAPRLLLQL LRSPSLRSHE SATGQSVTTG GRGEPQWLRA AVGGRHGTSP
ALLTGGGAAT GGRQRGRTET PCLAAATWGR LPSPEDTLPG QDSWNGVLSR AGLGVWALAT
ALVVHCYSKS PSSKDAALME AARANNVQEV SRLLSEGADV NARHRLGWTA LMVAAINRND
SVVQVLLAAG ADPNLGDDFS SVYKTAKDQG IHSLEVLVTR EDDFNNRLNN RASFKGCTAL
HYAVLADDYR TVKELLDGGA NPLQRNEMGH TPLDYAREGE VMKLLRTSET KYQEKQRKRE
AEERRRFPLE QRLKEHIIGQ ESAIATVGAA IRRKENGWYD EEHPLVFLFL GSSGIGKTEL
AKQTAKYMHK DAKKGFIRLD MSEFQERHEV AKFIGSPPGY IGHEEGGQLT KKLKQCPNAV
VLFDEVDKAH PDVLTIMLQL FDEGRLTDGK GKTIDCKDAI FIMTSNVASD EIAQHALQLR
QEALEMSRNR IAENLGDVQI SDKITISKNF KENVIRPILK AHFRRDEFLG RINEIVYFLP
FCHSELIQLV NKELNFWAKR AKQRHNITLL WDREVADVLV EGYNVHYGAR SIKHEVERRV
VNQLAAAYEQ DLLPGGCTLR ITVEDSDKQL LRSPELSSSQ AERRPPKLRL EIIDKDSKTH
KLDIQAPLHP EKVCHTL
