LONM1_ARATH
ID LONM1_ARATH Reviewed; 940 AA.
AC P93655; O04954; Q8RWX1;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Lon protease homolog 1, mitochondrial;
DE EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_03120};
DE Flags: Precursor;
GN Name=LON1; OrderedLocusNames=At5g26860; ORFNames=F2P16.23;
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 [MRNA].
RC STRAIN=cv. Columbia;
RA Sarria R., Lyznik A., MacKenzie S.;
RT "Mitochondrial LON protease homolog from Arabidopsis thaliana (Columbia).";
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=17478548; DOI=10.1093/pcp/pcm052;
RA Ostersetzer O., Kato Y., Adam Z., Sakamoto W.;
RT "Multiple intracellular locations of Lon protease in Arabidopsis: evidence
RT for the localization of AtLon4 to chloroplasts.";
RL Plant Cell Physiol. 48:881-885(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19076295; DOI=10.1111/j.1469-8137.2008.02701.x;
RA Rigas S., Daras G., Laxa M., Marathias N., Fasseas C., Sweetlove L.J.,
RA Hatzopoulos P.;
RT "Role of Lon1 protease in post-germinative growth and maintenance of
RT mitochondrial function in Arabidopsis thaliana.";
RL New Phytol. 181:588-600(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
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 ECO:0000269|PubMed:19076295}.
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:14671022,
CC ECO:0000269|PubMed:17478548, ECO:0000269|PubMed:19076295}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC Rule:MF_03120}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB48000.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAB61060.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U88087; AAB48000.1; ALT_FRAME; mRNA.
DR EMBL; AF007270; AAB61060.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY091049; AAM13870.1; -; mRNA.
DR EMBL; AY117355; AAM51430.1; -; mRNA.
DR PIR; T01765; T01765.
DR AlphaFoldDB; P93655; -.
DR SMR; P93655; -.
DR BioGRID; 18019; 6.
DR IntAct; P93655; 4.
DR STRING; 3702.AT5G26860.1; -.
DR MEROPS; S16.011; -.
DR iPTMnet; P93655; -.
DR SwissPalm; P93655; -.
DR PaxDb; P93655; -.
DR PRIDE; P93655; -.
DR ProteomicsDB; 238630; -.
DR EnsemblPlants; AT5G26860.1; AT5G26860.1; AT5G26860.
DR Gramene; AT5G26860.1; AT5G26860.1; AT5G26860.
DR Araport; AT5G26860; -.
DR TAIR; locus:2148458; AT5G26860.
DR eggNOG; KOG2004; Eukaryota.
DR HOGENOM; CLU_004109_1_0_1; -.
DR InParanoid; P93655; -.
DR PhylomeDB; P93655; -.
DR PRO; PR:P93655; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P93655; baseline and differential.
DR Genevisible; P93655; AT.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; HDA:TAIR.
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: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 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 1: Evidence at protein level;
KW ATP-binding; DNA-binding; Hydrolase; Mitochondrion; Nucleotide-binding;
KW Phosphoprotein; Protease; Reference proteome; Serine protease;
KW Transit peptide.
FT TRANSIT 1..61
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT CHAIN 62..940
FT /note="Lon protease homolog 1, mitochondrial"
FT /id="PRO_0000026739"
FT DOMAIN 100..307
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 751..935
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 70..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 841
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT ACT_SITE 884
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT BINDING 464..471
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT CONFLICT 288
FT /note="V -> F (in Ref. 1; AAB48000)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="K -> Q (in Ref. 1; AAB48000)"
FT /evidence="ECO:0000305"
FT CONFLICT 679
FT /note="A -> S (in Ref. 1; AAB48000)"
FT /evidence="ECO:0000305"
FT CONFLICT 935..936
FT /note="YD -> FA (in Ref. 1; AAB48000)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 940 AA; 103930 MW; 606E0A8BC9AE5E28 CRC64;
MLKLFTSSAS RVHHLTPVSR VVGSSPVESP LFKALSQITG WNRRSTSLGH RAFFCSEPTN
GEAAAEAETK AVESDSEVSD SKSSSAIVPT NPRPEDCLTV LALPVPHRPL FPGFYMPIYV
KDPKVLAALQ ESRRRQAPYA GAFLLKDDPS ADSSSSTDAE KNINELKGKE LLNRLHEVGT
LAQISSIQGD QVILVGHRRL RIKEMVSEEP LTVKVDHLKD NPFDMDDDVV KATSFEVIST
LRDVLKTSSL WRDHVQTYTQ HIGDFTYPRL ADFGAAICGA NRHQAQEVLE ELDVHKRLRL
TLELMKKEME ISKIQETIAK AIEEKISGEQ RRYLLNEQLK AIKKELGVET DDKSALSAKF
KERIEPNKEK IPAHVLQVIE EELTKLQLLE ASSSEFNVTR NYLDWLTILP WGNYSNENFD
VARAQTILDE DHYGLSDVKE RILEFIAVGR LRGTSQGKII CLSGPPGVGK TSIGRSIARA
LNRKFFRFSV GGLADVAEIK GHRRTYVGAM PGKMVQCLKS VGTANPLVLI DEIDKLGRGH
AGDPASALLE LLDPEQNANF LDHYLDVTID LSKVLFVCTA NVIDMIPNPL LDRMEVISIA
GYITDEKVHI ARDYLEKTAR GDCGVKPEQV EVSDAALLSL IENYCREAGV RNLQKQIEKI
YRKIALKLVR EGAVPEEPAV ASDPEEAEIV ADVGESIENH TVEENTVSSA EEPKEEAQTE
KIAIETVMID ESNLADYVGK PVFHAEKLYE QTPVGVVMGL AWTSMGGSTL YIETTVVEEG
EGKGGLNITG QLGDVMKESA QIAHTVARKI MLEKEPENQF FANSKLHLHV PAGATPKDGP
SAGCTMITSL LSLATKKPVR KDLAMTGEVT LTGRILPIGG VKEKTIAARR SQIKTIIFPE
ANRRDFDELA ENVKEGLNVH FVDDYGKIFE LAFGYDKQED
