ID LONM3_ARATH Reviewed; 924 AA.
AC Q9M9L8;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 24-JAN-2024, entry version 144.
DE RecName: Full=Lon protease homolog 3, mitochondrial;
DE EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_03120};
DE Flags: Precursor;
GN Name=LON3; OrderedLocusNames=At3g05780; ORFNames=F10A16.7;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
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. {ECO:0000255|HAMAP-Rule:MF_03120}.
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 -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC Rule:MF_03120}.
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DR EMBL; AC012393; AAF26080.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74296.1; -; Genomic_DNA.
DR RefSeq; NP_566258.1; NM_111452.1.
DR AlphaFoldDB; Q9M9L8; -.
DR SMR; Q9M9L8; -.
DR STRING; 3702.Q9M9L8; -.
DR MEROPS; S16.A03; -.
DR PaxDb; 3702-AT3G05780-1; -.
DR EnsemblPlants; AT3G05780.1; AT3G05780.1; AT3G05780.
DR GeneID; 819747; -.
DR Gramene; AT3G05780.1; AT3G05780.1; AT3G05780.
DR KEGG; ath:AT3G05780; -.
DR Araport; AT3G05780; -.
DR TAIR; AT3G05780; LON3.
DR eggNOG; KOG2004; Eukaryota.
DR HOGENOM; CLU_004109_1_0_1; -.
DR InParanoid; Q9M9L8; -.
DR OMA; MFEKEPE; -.
DR OrthoDB; 1103874at2759; -.
DR PhylomeDB; Q9M9L8; -.
DR PRO; PR:Q9M9L8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M9L8; baseline and differential.
DR Genevisible; Q9M9L8; AT.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
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:SF14; LON PROTEASE HOMOLOG 3, MITOCHONDRIAL-RELATED; 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 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; DNA-binding; Hydrolase; Mitochondrion; Nucleotide-binding;
KW Protease; Reference proteome; Serine protease; Transit peptide.
FT TRANSIT 1..63
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT CHAIN 64..924
FT /note="Lon protease homolog 3, mitochondrial"
FT /id="PRO_0000045424"
FT DOMAIN 112..325
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 738..922
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 828
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT ACT_SITE 871
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT BINDING 447..454
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
SQ SEQUENCE 924 AA; 103476 MW; DF6BCA96ECF99C65 CRC64;
MMPKRFNTSG FDTTLRLPSY YGFLHLTQSL TLNSRVFYGA RHVTPPAIRI GSNPVQSLLL
FRAPTQLTGW NRSSRDLLGR RVSFSDRSDG VDLLSSSPIL STNPNLDDSL TVIALPLPHK
PLIPGFYMPI HVKDPKVLAA LQESTRQQSP YVGAFLLKDC ASTDSSSRSE TEDNVVEKFK
VKGKPKKKRR KELLNRIHQV GTLAQISSIQ GEQVILVGRR RLIIEEMVSE DPLTVRVDHL
KDKPYDKDNA VIKASYVEVI STLREVLKTN SLWRDQDIGD FSYQHLADFG AGISGANKHK
NQGVLTELDV HKRLELTLEL VKKQVEINKI KETDDGSSLS AKIRVRIDTK RDKIPKHVIK
VMEEEFTKLE MLEENYSDFD LTYNYLHWLT VLPWGNFSYE NFDVLRAKKI LDEDHYGLSD
VKERILEFIA VGRLRGTSQG KIICLSGPPG VGKTSIGRSI ARALDRKFFR FSVGGLSDVA
EIKGHCQTYV GAMPGKMVQC LKSVGTANPL ILFDEIDKLG RCHTGDPASA LLEVMDPEQN
AKFLDHFLNV TIDLSKVLFV CTANVIEMIP GPLLDRMEVI DLSGYVTDEK MHIARDYLVK
KTCRDCGIKP EHVDLSDAAL LSLIENYCRE AGVRNLQKQI EKIYRKVALE LVRQGAVSFD
VTDTKDTKSL AKTDSEVKRM KVADIMKILE SATGDSTESK TKQSGLVAKT FEKVMIDESN
LADYVGKPVF QEEKIYEQTP VGVVMGLAWT SMGGSTLYIE TTFVEEGLGK GGLHITGQLG
DVMKESAQIA HTVARRIMFE KEPENLFFAN SKLHLHVPEG ATPKDGPSAG CTMITSFLSL
AMKKLVRKDL AMTGEVTLTG RILPIGGVKE KTIAARRSQI KTIIFPEANR RDFEELAENM
KEGLDVHFVD EYEKIFDLAF NYDH
//
