LONM_RAT
ID LONM_RAT Reviewed; 950 AA.
AC Q924S5;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Lon protease homolog, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03120};
DE EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_03120};
DE AltName: Full=Lon protease-like protein {ECO:0000255|HAMAP-Rule:MF_03120};
DE Short=LONP {ECO:0000255|HAMAP-Rule:MF_03120};
DE AltName: Full=Mitochondrial ATP-dependent protease Lon {ECO:0000255|HAMAP-Rule:MF_03120};
DE AltName: Full=Serine protease 15 {ECO:0000255|HAMAP-Rule:MF_03120};
DE Flags: Precursor;
GN Name=Lonp1; Synonyms=Lon, Prss15;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX PubMed=12082077; DOI=10.1083/jcb.200108103;
RA Hori O., Ichinoda F., Tamatani T., Yamaguchi A., Sato N., Ozawa K.,
RA Kitao Y., Miyazaki M., Harding H.P., Ron D., Tohyama M., Stern D.M.,
RA Ogawa S.;
RT "Transmission of cell stress from endoplasmic reticulum to mitochondria:
RT enhanced expression of Lon protease.";
RL J. Cell Biol. 157:1151-1160(2002).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=7961901; DOI=10.1016/s0021-9258(19)62045-4;
RA Wang N., Maurizi M.R., Emmert-Buck L., Gottesman M.M.;
RT "Synthesis, processing, and localization of human Lon protease.";
RL J. Biol. Chem. 269:29308-29313(1994).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12752449; DOI=10.1046/j.1432-1033.2003.03598.x;
RA Bakala H., Delaval E., Hamelin M., Bismuth J., Borot-Laloi C., Corman B.,
RA Friguet B.;
RT "Changes in rat liver mitochondria with aging. Lon protease-like reactivity
RT and N(epsilon)-carboxymethyllysine accumulation in the matrix.";
RL Eur. J. Biochem. 270:2295-2302(2003).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15560797; DOI=10.1111/j.1432-1033.2004.04422.x;
RA Delaval E., Perichon M., Friguet B.;
RT "Age-related impairment of mitochondrial matrix aconitase and ATP-
RT stimulated protease in rat liver and heart.";
RL Eur. J. Biochem. 271:4559-4564(2004).
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:0000255|HAMAP-Rule:MF_03120,
CC ECO:0000269|PubMed:12752449, ECO:0000269|PubMed:15560797}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_03120}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC Rule:MF_03120, ECO:0000269|PubMed:12752449,
CC ECO:0000269|PubMed:15560797, ECO:0000269|PubMed:7961901}.
CC -!- INDUCTION: By hypoxia or ER stress. {ECO:0000269|PubMed:12082077}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC Rule:MF_03120}.
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DR EMBL; AB064323; BAB62423.1; -; mRNA.
DR RefSeq; NP_596895.1; NM_133404.1.
DR AlphaFoldDB; Q924S5; -.
DR SMR; Q924S5; -.
DR BioGRID; 251027; 2.
DR IntAct; Q924S5; 2.
DR STRING; 10116.ENSRNOP00000066618; -.
DR MEROPS; S16.002; -.
DR iPTMnet; Q924S5; -.
DR PhosphoSitePlus; Q924S5; -.
DR jPOST; Q924S5; -.
DR PaxDb; Q924S5; -.
DR PRIDE; Q924S5; -.
DR Ensembl; ENSRNOT00000074253; ENSRNOP00000066618; ENSRNOG00000046502.
DR GeneID; 170916; -.
DR KEGG; rno:170916; -.
DR CTD; 9361; -.
DR RGD; 621598; Lonp1.
DR eggNOG; KOG2004; Eukaryota.
DR GeneTree; ENSGT00530000063553; -.
DR HOGENOM; CLU_004109_1_1_1; -.
DR InParanoid; Q924S5; -.
DR OMA; YVGPPIY; -.
DR OrthoDB; 528132at2759; -.
DR PhylomeDB; Q924S5; -.
DR PRO; PR:Q924S5; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000046502; Expressed in adult mammalian kidney and 19 other tissues.
DR Genevisible; Q924S5; RN.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:RGD.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0043531; F:ADP binding; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; ISO:RGD.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:RGD.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IDA:RGD.
DR GO; GO:0070182; F:DNA polymerase binding; ISO:RGD.
DR GO; GO:0051880; F:G-quadruplex DNA binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0001018; F:mitochondrial promoter sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003697; F:single-stranded DNA binding; ISO:RGD.
DR GO; GO:0003727; F:single-stranded RNA binding; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:RGD.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IBA:GO_Central.
DR GO; GO:0007005; P:mitochondrion organization; IEP:RGD.
DR GO; GO:0070407; P:oxidation-dependent protein catabolic process; ISO:RGD.
DR GO; GO:0030163; P:protein catabolic process; IDA:RGD.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
DR GO; GO:0065003; P:protein-containing complex assembly; IMP:RGD.
DR GO; GO:0006508; P:proteolysis; ISO:RGD.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; ISO:RGD.
DR GO; GO:0010044; P:response to aluminum ion; IEP:RGD.
DR GO; GO:0009725; P:response to hormone; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR Gene3D; 2.30.130.40; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR43718; PTHR43718; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR PIRSF; PIRSF001174; Lon_proteas; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00464; LON; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00763; lon; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS01046; LON_SER; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; DNA-binding; Hydrolase; Mitochondrion; Nucleotide-binding;
KW Protease; Reference proteome; Serine protease; Transit peptide.
FT TRANSIT 1..65
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT CHAIN 66..950
FT /note="Lon protease homolog, mitochondrial"
FT /id="PRO_0000254962"
FT DOMAIN 112..358
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 749..939
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 67..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 845
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT ACT_SITE 888
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT BINDING 513..520
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
SQ SEQUENCE 950 AA; 105793 MW; D505C3D851B6F0E7 CRC64;
MAASTGYVRL WAAARCWVLR RPLLAVTGGR VPSASGSWLR RGCRVCDTST PWGGRVPMGG
GQWRGLWDAG SRGGSDETSE GGVEDGATAS SGEGPVVTAL APMTVPDVFP HLPLIAISRN
PVFPRFIKIV EVKNKKLVEL LRRKVRLAQP YVGVFLKRDD NNESDVVESL DEIYHTGTFA
QIHEMQDLGD KLRMIVTGHR RIHISRQLEV EPEGLEPEAE NKQKSRRKLK RGKKEVGDEL
GAKPQLEMVT EATSDTSKEV LMVEVENVAH EDFQVTEEVK ALTAEIVKTI RDIIALNPLY
RESVLQMMQA GQRVVDNPIY LSDMGAALTG AESHELQDVL EETNILKRLY KALSLLKKEF
ELSKLQQRLG REVEEKIKQT HRKYLLQEQL KIIKKELGLE KDDKDAIEEK FRERLKELVV
PKHVMDVVDE ELSKLALLDN HSSEFNVTRN YLDWLTSIPW GRQSDENLDL ARAQSVLEED
HYGMEDVKKR VLEFIAVSQL RGSTQGKILC FHGPPGVGKT SIARSIARAL GREYFRFSVG
GMTDVAEIKG HRRTYVGAMP GKIIQCLKKT KTENPLVLID EVDKIGRGYQ GDPSSALLEL
LDPEQNANFL DHYLDVPVDL SKVLFICTAN VTDTIPEPLR DRMEMINVSG YVAQEKLAIA
ERYLVPQART LCGLDESKAQ LSATVLTLLI KQYCRESGVR NLQKQVEKVL RKAAYKIVSG
EAQTVHVTPE NLQDFVGKPV FTVERMYDVT PPGVVMGLAW TAMGGSTLFV ETSLRRPQPS
GSKEDKDGSL EVTGQLGDVM KESARIAYTF ARAFLMEQDP ENDFLVTSHI HLHVPEGATP
KDGPSAGCTI VTALLSLALG QPVLQNLAMT GEVSLTGKVL PVGGIKEKTI AAKRAGVTCI
ILPAENRKDF SDLAPFITEG LEVHFVEHYR DIFRIAFPLR EHQEALAVER
