LONM_DROME
ID LONM_DROME Reviewed; 1024 AA.
AC Q7KUT2; Q9VW20;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=Lon; ORFNames=CG8798;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-898.
RX PubMed=20930118; DOI=10.1073/pnas.1008924107;
RA Matsushima Y., Goto Y., Kaguni L.S.;
RT "Mitochondrial Lon protease regulates mitochondrial DNA copy number and
RT transcription by selective degradation of mitochondrial transcription
RT factor A (TFAM).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:18410-18415(2010).
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. Regulates mitochondrial DNA (mtDNA) copy
CC number and transcription by stabilizing the mitochondrial TFAM:mtDNA
CC ratio via selective degradation of TFAM. {ECO:0000255|HAMAP-
CC Rule:MF_03120, ECO:0000269|PubMed:20930118}.
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, ECO:0000269|PubMed:20930118}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=C;
CC IsoId=Q7KUT2-1; Sequence=Displayed;
CC Name=A;
CC IsoId=Q7KUT2-2; Sequence=VSP_039539;
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC Rule:MF_03120}.
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DR EMBL; AE014296; AAF49134.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN11654.2; -; Genomic_DNA.
DR EMBL; BT099738; ACV53872.1; -; mRNA.
DR RefSeq; NP_649133.1; NM_140876.3. [Q7KUT2-2]
DR RefSeq; NP_730435.2; NM_168806.3. [Q7KUT2-1]
DR AlphaFoldDB; Q7KUT2; -.
DR SMR; Q7KUT2; -.
DR BioGRID; 65408; 6.
DR IntAct; Q7KUT2; 9.
DR STRING; 7227.FBpp0271918; -.
DR MEROPS; S16.002; -.
DR PaxDb; Q7KUT2; -.
DR PRIDE; Q7KUT2; -.
DR DNASU; 40138; -.
DR EnsemblMetazoa; FBtr0074967; FBpp0074735; FBgn0036892. [Q7KUT2-2]
DR EnsemblMetazoa; FBtr0273410; FBpp0271918; FBgn0036892. [Q7KUT2-1]
DR GeneID; 40138; -.
DR KEGG; dme:Dmel_CG8798; -.
DR UCSC; CG8798-RA; d. melanogaster.
DR CTD; 40138; -.
DR FlyBase; FBgn0036892; Lon.
DR VEuPathDB; VectorBase:FBgn0036892; -.
DR eggNOG; KOG2004; Eukaryota.
DR GeneTree; ENSGT00530000063553; -.
DR InParanoid; Q7KUT2; -.
DR OMA; YVGPPIY; -.
DR PhylomeDB; Q7KUT2; -.
DR SignaLink; Q7KUT2; -.
DR BioGRID-ORCS; 40138; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Lon; fly.
DR GenomeRNAi; 40138; -.
DR PRO; PR:Q7KUT2; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036892; Expressed in mouthpart and 37 other tissues.
DR ExpressionAtlas; Q7KUT2; baseline and differential.
DR Genevisible; Q7KUT2; DM.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR GO; GO:0005777; C:peroxisome; ISS:FlyBase.
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:0017171; F:serine hydrolase activity; HDA:FlyBase.
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; IMP:FlyBase.
DR GO; GO:0070407; P:oxidation-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:FlyBase.
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; 2.
DR TIGRFAMs; TIGR00763; lon; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS01046; LON_SER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; DNA-binding; Hydrolase; Mitochondrion;
KW Nucleotide-binding; Protease; Reference proteome; Serine protease;
KW Transit peptide.
FT TRANSIT 1..56
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT CHAIN 57..1024
FT /note="Lon protease homolog, mitochondrial"
FT /id="PRO_0000395762"
FT DOMAIN 94..409
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 800..992
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 219..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 898
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT ACT_SITE 941
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT BINDING 564..571
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT VAR_SEQ 199..216
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000305"
FT /id="VSP_039539"
FT MUTAGEN 898
FT /note="S->A: Severe retardation of TFAM degradation
FT following mtDNA depletion."
FT /evidence="ECO:0000269|PubMed:20930118"
SQ SEQUENCE 1024 AA; 115033 MW; 2472ED9810956576 CRC64;
MLARAIRVRP MMRGIASSSV WNRNRPIQSS LMQYCRDRSL RLQRLHGANL MVQRFYSRKR
DDSNGDIIMG PDLMSDQDTH LPATVAVPDV WPHVPLLAMR KNPLFPRFMK IVEVSNPIIM
DLLRRKVKLN QPYVGVFLKK TDGEEELITN LNDVYNLGTF AQIQELQDLG DKLRMVVVAH
RRIRITGQVV EDVPPPKPVK MTTLHYPLFN IKLQIPAEDQ STDQADAAPI KSRSDPARKP
RGRIPRSRTG KSRESAAAEE LIQNQTLEPP LKSGKVESSS LPKPPTEEKI VEPETGAKEN
VNQSAPSAQP VLIVEVENVK QPIYKQTEEV KALTQEIIKT LRDIITMNPL YRESLQQMLH
QNQRVVDNPI YLCDLGASLS AGEPAELQKI LEETDIPERL QLALTLLKKE LELSRLQQKI
GREVEEKVKQ QHRKYILQEQ LKVIKKELGI EKDDKDAIGE KYREKLKDKV VPEAIMTVID
EELTKLNFLE SHSSEFNVTR NYLDWLTSLP WGVISTENLC LEKATETLND DHYGMEDIKK
RILEFIAVSS LKGSTQGKIL CFHGPPGVGK TSIAKSIARA LNREYFRFSV GGMTDVAEIK
GHRRTYVGAM PGKLIQCLKK TKIENPLVLI DEVDKIGKGY QGDPSSALLE LLDPEQNANF
LDHYLDVPVD LSRVLFICTA NVIDTIPEPL RDRMELIEMS GYVAEEKIAI ARQYLMPQAM
KDCGLTDKHI NISEDALNML IRSYCRESGV RNLQKHIEKV IRKVAFRVVK KEGEHFPVNA
DNLTTFLGKQ IFSSDRMYAT TPVGVVMGLA WTAMGGSSLY IETSRRHIRQ GAKTDPNTVA
GSLHITGNLG DVMKESAQIA LTVARNFLYS LEPNNLFLEQ EHIHLHVPEG ATPKDGPSAG
ITIITALVSL ATGKPVRQDI AMTGEVSLKG KVLPVGGIKE KTIAARRSGV NCLILPVDNK
KDFEELPTYI TDGLEVHFAT TYEDVYKIAF TDVTETTTNN VEEQEPLQKL SSAAAAKSET
WPYS