LONM_CAEEL
ID LONM_CAEEL Reviewed; 971 AA.
AC O44952;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 152.
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 Flags: Precursor;
GN Name=lonp-1 {ECO:0000312|WormBase:C34B2.6};
GN ORFNames=C34B2.6 {ECO:0000312|WormBase:C34B2.6};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22700657; DOI=10.1126/science.1223560;
RA Nargund A.M., Pellegrino M.W., Fiorese C.J., Baker B.M., Haynes C.M.;
RT "Mitochondrial import efficiency of ATFS-1 regulates mitochondrial UPR
RT activation.";
RL Science 337:587-590(2012).
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 DNA
CC in a site-specific manner. Involved in the degradation of transcription
CC factor atfs-1 in the mitochondrion (PubMed:22700657).
CC {ECO:0000255|HAMAP-Rule:MF_03120, ECO:0000269|PubMed:22700657}.
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 or homoheptamer. Organized in a ring with a
CC central cavity. {ECO:0000255|HAMAP-Rule:MF_03120}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC Rule:MF_03120}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes transcription
CC factor atfs-1 accumulation in mitochondria.
CC {ECO:0000269|PubMed:22700657}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC Rule:MF_03120}.
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DR EMBL; FO080220; CCD62124.1; -; Genomic_DNA.
DR PIR; T32883; T32883.
DR RefSeq; NP_492796.1; NM_060395.5.
DR AlphaFoldDB; O44952; -.
DR SMR; O44952; -.
DR BioGRID; 38377; 24.
DR IntAct; O44952; 1.
DR STRING; 6239.C34B2.6; -.
DR EPD; O44952; -.
DR PaxDb; O44952; -.
DR PeptideAtlas; O44952; -.
DR EnsemblMetazoa; C34B2.6.1; C34B2.6.1; WBGene00016391.
DR GeneID; 172966; -.
DR KEGG; cel:CELE_C34B2.6; -.
DR UCSC; C34B2.6; c. elegans.
DR CTD; 172966; -.
DR WormBase; C34B2.6; CE16894; WBGene00016391; lonp-1.
DR eggNOG; KOG2004; Eukaryota.
DR GeneTree; ENSGT00530000063553; -.
DR HOGENOM; CLU_004109_1_0_1; -.
DR InParanoid; O44952; -.
DR OMA; YVGPPIY; -.
DR OrthoDB; 528132at2759; -.
DR PhylomeDB; O44952; -.
DR PRO; PR:O44952; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00016391; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
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; IBA:GO_Central.
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:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:UniProtKB-UniRule.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IBA:GO_Central.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR GO; GO:0070407; P:oxidation-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0030163; P:protein catabolic process; IMP:UniProtKB.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
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 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 3: Inferred from homology;
KW ATP-binding; DNA-binding; Hydrolase; Mitochondrion; Nucleotide-binding;
KW Protease; Reference proteome; Serine protease; Transit peptide.
FT TRANSIT 1..55
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT CHAIN 56..971
FT /note="Lon protease homolog, mitochondrial"
FT /id="PRO_0000026735"
FT DOMAIN 89..357
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 784..971
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 190..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..227
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 878
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT ACT_SITE 921
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT BINDING 512..519
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
SQ SEQUENCE 971 AA; 108206 MW; 7B10DD7D18E6E3C2 CRC64;
MYRAGAVLLR GATRTRLLAA ASAHQSFATF SQRNQSILMM KSMELAGNSG ERRFYSTHDD
PIAVDDSLEL YKDLGGMSPI QVPADMPNVP MLAINRYPLF PGFIKKVDIV KDDNLKALIR
RQLSLKQPYA GVFVKRDDEN KEETITSLSE VYPTGSFVQI IEVRDQGSVL ELVLSAHRRI
RALEPIDEIT PKNETPLNGR RARGKRAASA TSPLTPPPSP PPLAPSVASV APEISATEEK
EEKTTPPSAT GEKQKKGIIM VRTENVVAEP VPKNNETKAT MMAIVQTIRD VVQFNQLFGQ
QINLLLHPSQ NVIDNPVYLC DLVATLVQSA ETKDLQEMMD EIDVSKRLKI ALLLIQKEKA
VAKLKYDINK DVEKKVQDHH RKYLLNEQLK VIKKELGIEK DEKTTIIEKI DERIKTLAVP
EYALKVINEE KTKLQFLDPH SSEFSVTRNY LEWLTSVPWG LTSPENRRLS VAKKALDEGH
YGMKDVKERI MEFIAVNLLR KSIGGKILCF HGPPGVGKTS IAKSIATALN REYFRFSVGG
MTDVAEIKGH RRTYVGAMPG KMIQCMKKVK TENPLVLIDE VDKIGGAGFH GDPASALLEL
LDPEQNANFN DHFLDVPVDL SRVLFICTAN EISKIPGPLR DRMEMIDVSG YLAEEKVEIA
HQHLIPQLRK DTSLATEQLK IEDSALEELI KHYCRESGVR NLQQHIERIF RKAALQIAEQ
QNEDEEPAEK ATTAITENSE AEPITSTSSA DCLKSSAEQI VVCTENLQKF VGRPKFTSDR
MYEVTPPGVI MGLAWTAMGG SALYIETVLK RPVDLTNDKD GSIETTGNLG DVMKESVRTA
LTVAKGILAR EQPDNKFFDK AHIHIHVPEG ATPKDGPSAG VTLVSSLLSL ALDRPVVQDM
AMTGEISLTG KVLPVGGIRE KVIAARRVGA KRVFLPNENR RDFDDLPEFM KSELDIRFVS
HYDELYEHLF Q
