ID F6XLW4_CALJA Unreviewed; 896 AA.
AC F6XLW4;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Lon protease homolog, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03120};
DE EC=3.4.21.53 {ECO:0000256|HAMAP-Rule:MF_03120};
DE AltName: Full=Lon protease-like protein {ECO:0000256|HAMAP-Rule:MF_03120};
DE Short=LONP {ECO:0000256|HAMAP-Rule:MF_03120};
DE AltName: Full=Mitochondrial ATP-dependent protease Lon {ECO:0000256|HAMAP-Rule:MF_03120};
DE AltName: Full=Serine protease 15 {ECO:0000256|HAMAP-Rule:MF_03120};
GN Name=LONP1 {ECO:0000256|HAMAP-Rule:MF_03120,
GN ECO:0000313|Ensembl:ENSCJAP00000046333.3};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000046333.3, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000046333.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000046333.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: ATP-dependent serine protease that mediates the selective
CC degradation of misfolded, unassembled or oxidatively damaged
CC polypeptides as well as certain short-lived regulatory proteins in the
CC mitochondrial matrix. May also have a chaperone function in the
CC assembly of inner membrane protein complexes. Participates in the
CC regulation of mitochondrial gene expression and in the maintenance of
CC the integrity of the mitochondrial genome. Binds to mitochondrial
CC promoters and RNA in a single-stranded, site-specific, and strand-
CC specific manner. May regulate mitochondrial DNA replication and/or gene
CC expression using site-specific, single-stranded DNA binding to target
CC the degradation of regulatory proteins binding to adjacent sites in
CC mitochondrial promoters. {ECO:0000256|HAMAP-Rule:MF_03120}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03120};
CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity. The
CC ATP-binding and proteolytic domains (AP-domain) form a hexameric
CC chamber, while the N-terminal domain is arranged as a trimer of dimers.
CC DNA and RNA binding is stimulated by substrate and inhibited by ATP
CC binding. Interacts with TWNK and mitochondrial DNA polymerase subunit
CC POLG. {ECO:0000256|HAMAP-Rule:MF_03120}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305, ECO:0000256|HAMAP-Rule:MF_03120}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|HAMAP-
CC Rule:MF_03120, ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-
CC ProRule:PRU01122, ECO:0000256|RuleBase:RU000591}.
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DR AlphaFoldDB; F6XLW4; -.
DR Ensembl; ENSCJAT00000060966.3; ENSCJAP00000046333.3; ENSCJAG00000017041.5.
DR GeneTree; ENSGT00530000063553; -.
DR HOGENOM; CLU_004109_1_0_1; -.
DR Proteomes; UP000008225; Chromosome 22.
DR Bgee; ENSCJAG00000017041; Expressed in testis and 6 other cell types or tissues.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:UniProtKB-UniRule.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0070407; P:oxidation-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:UniProtKB-UniRule.
DR CDD; cd19500; RecA-like_Lon; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.5.5270; -; 1.
DR Gene3D; 1.20.58.1480; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 2.30.130.40; LON domain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_03120; lonm_euk; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR004815; Lon_bac/euk-typ.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR003111; Lon_prtase_N.
DR InterPro; IPR046336; Lon_prtase_N_sf.
DR InterPro; IPR027503; Lonm_euk.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008268; Peptidase_S16_AS.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00763; lon; 1.
DR PANTHER; PTHR43718; LON PROTEASE; 1.
DR PANTHER; PTHR43718:SF2; LON PROTEASE HOMOLOG, MITOCHONDRIAL; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR PIRSF; PIRSF001174; Lon_proteas; 2.
DR PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00464; LON; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS01046; LON_SER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03120}; DNA-binding {ECO:0000256|HAMAP-Rule:MF_03120};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03120, ECO:0000256|PIRNR:PIRNR001174};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000256|HAMAP-
KW Rule:MF_03120};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03120,
KW ECO:0000256|PIRNR:PIRNR001174};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_03120};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW Rule:MF_03120}; Transit peptide {ECO:0000256|HAMAP-Rule:MF_03120}.
FT TRANSIT 1..42
FT /note="Mitochondrion"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120"
FT CHAIN 42..896
FT /note="Lon protease homolog, mitochondrial"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120"
FT /id="PRO_5035346726"
FT DOMAIN 60..304
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 695..885
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 154..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 791
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT ACT_SITE 834
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT BINDING 459..466
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120,
FT ECO:0000256|PIRSR:PIRSR001174-2"
SQ SEQUENCE 896 AA; 100457 MW; 6DF3289D031DA183 CRC64;
MAAGTGYVRL WGAARCWALR RPILAAAGGR VPTAAGAWLL RGPVITALTP MTIPDVFPHL
PLIAITRNPV FPRFIKIIEV KNKKLVELLR RKVRLAQPYV GVFLKRDDNS ESDVVENLDE
IYHTGTFAQI HEMQDLGDKL RMIVMGHRRV HISRQLEVEP EEPEAENKHK PRRKSKRSRK
EAEDELGARH PAELAMEPAT DLPGEVLMVE VENVVHEDFQ VTEEVKALTA EIVKTIRDII
ALNPLYRESV LQMMQAGQRV VDNPIYLSDM GAALTGAESH ELQDVLEETN IPKRLYKALS
LLKKEFELSK LQQRLGREVE EKIKQTHRKY LLQEQLKIIK KELGLEKDDK DAIEEKFRER
LKELVVPKHV MDVVDEELSK LGLLDNHSSE FNVTRNYLDW LTSIPWGKYS DENLDLARAQ
AVLEEDHYGM EDVKKRILEF IAVSQLRGST QGKILCFYGP PGVGKTSIAR SIARALNREY
FRFSVGGMTD VAEIKGHRRT YVGAMPGKII QCLKKTKTEN PLILIDEVDK IGRGYQGDPS
SALLELLDPE QNANFLDHYL DVPVDLSKVL FICTANVTDT IPEPLRDRME VISVSGYVAQ
EKLAIAERYL VPQARALCGL DESKAKLSSD VLTLLIKQYC RESGVRNLQK QVEKVLRKSA
YKIVSGEAES VEVTPENLQD FVGKPMFTVE RMYDVTPPGV VMGLAWTAMG GSTLFVETSL
RRPRDRDAKG EKDGSLEVTG QLGEVMKESA RIAYTFARAF LMQHAPDNEY LVTSHIHLHV
PEGATPKDGP SAGCTIVTAL LSLAMGRPVR QNLAMTGEVS LTGKILPVGG IKEKTIAAKR
AGVTCIVLPA ENKKDFCDLA GFITEGLEVH FVEHYRQIFH IAFPEEEAAE ALAVER
//
