ID G5C0Q5_HETGA Unreviewed; 895 AA.
AC G5C0Q5;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 67.
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 ORFNames=GW7_20492 {ECO:0000313|EMBL:EHB15116.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB15116.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB15116.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
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 EMBL; JH172722; EHB15116.1; -; Genomic_DNA.
DR AlphaFoldDB; G5C0Q5; -.
DR STRING; 10181.G5C0Q5; -.
DR MEROPS; S16.002; -.
DR eggNOG; KOG2004; Eukaryota.
DR InParanoid; G5C0Q5; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
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; 3.
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:UP000006813};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW Rule:MF_03120}; Transit peptide {ECO:0000256|HAMAP-Rule:MF_03120}.
FT CHAIN 1..895
FT /note="Lon protease homolog, mitochondrial"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120"
FT /id="PRO_5023243215"
FT TRANSIT 1
FT /note="Mitochondrion"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120"
FT DOMAIN 10..254
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 693..883
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 110..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 789
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT ACT_SITE 832
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT BINDING 457..464
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 895 AA; 100572 MW; 948EA1EB7750BCBF CRC64;
MTIPDVFPHL PLIAITRNPV FPRFIKIVEV KNKKLVELLR RKVRLAQPYV GVFLKRDDNN
ESDVVESLDE IYHTGTFAQI HEMQDLGDKL RMIVTGHRRI HINRQLEVEP EEAELENRQK
PRRKAKRGKK EAEDELSPST PREVGQEPAT EAAGEVLMVE VENVVHEDFQ VTEEVKALTA
EIVKTIRDII ALNPLYRESV LQMMQAGQRV VDNPIYLSDM GAALTGAESH ELQDVLEEAN
IPKRLYKALS LLKKEFELSK LQQRLGREVE EKIKQTHRKY LLQEQLKIIK KELGLEKDDK
DAIEEKFRER LRELVVPKHV MDVVDEELSK LGLLDNHSSE FKHCPPALGT PVSPMPTAAP
DWSPQSSLWL LQIRAGSALD VLEGLSQHIL VTRNYLDWLT SVPWGRHSDE NLDLSRAQAV
LEEDHYGMED VKRRILEFIA VSQLRRSTQG KILCFYGPPG VGKTSIARSI ARALNREYFR
FSVGGMTDVA EIKGHRRTYV GAMPGKIIQC LKKTKTENPL VLIDEVDKIG RGYQGDPSSA
LLELLDPEQN ANFLDHYLDV PVDLSKVLFI CTANVTDTIP EPLRDRMEMI NVSGYVAQEK
LAIAERYLVP QARALCGLDE SRARLSAPVL TLLIKQYCRE SGVRNLQKQV EKVLRKAAYK
IVSGEAETVE VTPENLQDFV GKPVFTVERM YDATPPGVVM GLAWTALGGS TLFVETSLRR
PRDRDSKENK DGSLEVTGQL GDVMKESARI AYTFARAFLL QRDPSNDYLV TSHIHLHVPE
GATPKDGPSA GCTIVTALLS LALDQPVQQD LAMTGEVSLT GKILPVGGIK EKTIAAKRAG
VTCIVLPAEN KKDFYDLAAF ITEGLEVHFV EHYSQVFDIA FPVPQRHAEA LAVER
//
