LONM_MOUSE
ID LONM_MOUSE Reviewed; 949 AA.
AC Q8CGK3; Q3TSK9; Q3TVL2; Q3TXE4; Q3TZW3; Q9DBP9;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 164.
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 AltName: Full=Lon protease-like protein {ECO:0000255|HAMAP-Rule:MF_03120};
DE Short=LONP {ECO:0000255|HAMAP-Rule:MF_03120};
DE AltName: Full=Mitochondrial ATP-dependent protease Lon {ECO:0000255|HAMAP-Rule:MF_03120};
DE AltName: Full=Serine protease 15 {ECO:0000255|HAMAP-Rule:MF_03120};
DE Flags: Precursor;
GN Name=Lonp1; Synonyms=Prss15;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Kidney;
RX PubMed=12657466; DOI=10.1016/s0378-1119(03)00403-7;
RA Lu B., Liu T., Crosby J.A., Thomas-Wohlever J., Lee I., Suzuki C.K.;
RT "The ATP-dependent Lon protease of Mus musculus is a DNA-binding protein
RT that is functionally conserved between yeast and mammals.";
RL Gene 306:45-55(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Lung, Ovary, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PROTEIN SEQUENCE OF 434-448; 490-500 AND 930-938, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(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
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:0000255|HAMAP-Rule:MF_03120,
CC ECO:0000269|PubMed:12657466}.
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. 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:0000255|HAMAP-Rule:MF_03120}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC Rule:MF_03120, ECO:0000269|PubMed:12657466}.
CC -!- TISSUE SPECIFICITY: Detected in liver > heart > kidney > testis.
CC {ECO:0000269|PubMed:12657466}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC Rule:MF_03120}.
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DR EMBL; AY190302; AAN85210.1; -; mRNA.
DR EMBL; AK004820; BAB23591.1; -; mRNA.
DR EMBL; AK157474; BAE34094.1; -; mRNA.
DR EMBL; AK159302; BAE34972.1; -; mRNA.
DR EMBL; AK160071; BAE35606.1; -; mRNA.
DR EMBL; AK161983; BAE36666.1; -; mRNA.
DR CCDS; CCDS28910.1; -.
DR RefSeq; NP_083058.2; NM_028782.2.
DR AlphaFoldDB; Q8CGK3; -.
DR SMR; Q8CGK3; -.
DR BioGRID; 216521; 24.
DR IntAct; Q8CGK3; 3.
DR MINT; Q8CGK3; -.
DR STRING; 10090.ENSMUSP00000041814; -.
DR ChEMBL; CHEMBL3259486; -.
DR MEROPS; S16.002; -.
DR iPTMnet; Q8CGK3; -.
DR PhosphoSitePlus; Q8CGK3; -.
DR SwissPalm; Q8CGK3; -.
DR REPRODUCTION-2DPAGE; Q8CGK3; -.
DR REPRODUCTION-2DPAGE; Q9DBP9; -.
DR EPD; Q8CGK3; -.
DR jPOST; Q8CGK3; -.
DR MaxQB; Q8CGK3; -.
DR PaxDb; Q8CGK3; -.
DR PeptideAtlas; Q8CGK3; -.
DR PRIDE; Q8CGK3; -.
DR ProteomicsDB; 286228; -.
DR Antibodypedia; 811; 305 antibodies from 29 providers.
DR DNASU; 74142; -.
DR Ensembl; ENSMUST00000047226; ENSMUSP00000041814; ENSMUSG00000041168.
DR GeneID; 74142; -.
DR KEGG; mmu:74142; -.
DR UCSC; uc008dcp.2; mouse.
DR CTD; 9361; -.
DR MGI; MGI:1921392; Lonp1.
DR VEuPathDB; HostDB:ENSMUSG00000041168; -.
DR eggNOG; KOG2004; Eukaryota.
DR GeneTree; ENSGT00530000063553; -.
DR HOGENOM; CLU_004109_1_1_1; -.
DR InParanoid; Q8CGK3; -.
DR OMA; YVGPPIY; -.
DR OrthoDB; 528132at2759; -.
DR PhylomeDB; Q8CGK3; -.
DR TreeFam; TF105001; -.
DR BRENDA; 3.4.21.53; 3474.
DR BioGRID-ORCS; 74142; 25 hits in 77 CRISPR screens.
DR ChiTaRS; Lonp1; mouse.
DR PRO; PR:Q8CGK3; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8CGK3; protein.
DR Bgee; ENSMUSG00000041168; Expressed in adrenal medulla and 268 other tissues.
DR ExpressionAtlas; Q8CGK3; baseline and differential.
DR Genevisible; Q8CGK3; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0043531; F:ADP binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:MGI.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IDA:MGI.
DR GO; GO:0070182; F:DNA polymerase binding; ISO:MGI.
DR GO; GO:0051880; F:G-quadruplex DNA binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0001018; F:mitochondrial promoter sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:MGI.
DR GO; GO:0003727; F:single-stranded RNA binding; ISO:MGI.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:MGI.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IBA:GO_Central.
DR GO; GO:0007005; P:mitochondrion organization; ISO:MGI.
DR GO; GO:0070407; P:oxidation-dependent protein catabolic process; ISO:MGI.
DR GO; GO:0030163; P:protein catabolic process; ISO:MGI.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; IDA:MGI.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; ISO:MGI.
DR GO; GO:0010044; P:response to aluminum ion; IEA:Ensembl.
DR GO; GO:0009725; P:response to hormone; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
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; Direct protein sequencing; DNA-binding; Hydrolase;
KW Mitochondrion; Nucleotide-binding; Protease; Reference proteome;
KW Serine protease; Transit peptide.
FT TRANSIT 1..65
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT CHAIN 66..949
FT /note="Lon protease homolog, mitochondrial"
FT /id="PRO_0000254961"
FT DOMAIN 112..357
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 748..938
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 68..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 844
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT ACT_SITE 887
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"
FT CONFLICT 90
FT /note="S -> G (in Ref. 2; BAB23591)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="A -> T (in Ref. 2; BAE34094)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="I -> T (in Ref. 2; BAB23591)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="G -> R (in Ref. 1; AAN85210)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="G -> S (in Ref. 2; BAE34094)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="V -> L (in Ref. 2; BAE34094)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="D -> Y (in Ref. 2; BAB23591)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="L -> P (in Ref. 2; BAB23591)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="M -> I (in Ref. 2; BAE36666)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="N -> K (in Ref. 2; BAE34972)"
FT /evidence="ECO:0000305"
FT CONFLICT 636
FT /note="E -> K (in Ref. 2; BAE34094)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 949 AA; 105843 MW; 4622E900C8D90369 CRC64;
MAASTGYVRL WAAARCWVLR RPLLAVTGGR VPSASGSWLR RGCRACDMSA PWGGRVLPGG
VQWRGLWDSG NRGGSDETSE GGAEDGATAS TGEGPVVTAL APMTVPDVFP HLPLIAITRN
PVFPRFIKIV EVKNKKLVEL LRRKVRLAQP YVGVFLKRDD NNESDVVESL DEIYHTGTFA
QIHEMQDLGD KLRMIVTGHR RIHISRQLEV EPEGLEPEAE KQKSRRKLKR GKKEVEDELG
PKPQLEMVTE AATDTSKEVL MVEVENVAHE DFQVTEEVKA LTAEIVKTIR DIIALNPLYR
ESVLQMMQAG QRVVDNPIYL SDMGAALTGA ESHELQDVLE ETNILKRLYK ALSLLKKEFE
LSKLQQRLGR EVEEKIKQTH RKYLLQEQLK IIKKELGLEK DDKDAIEEKF RERLRELVVP
KHVMDVVDEE LSKLALLDNH SSEFNVTRNY LDWLTSIPWG RQSDENLDLA RAQAVLEEDH
YGMEDVKKRV LEFIAVSQLR GSTQGKILCF HGPPGVGKTS IARSIARALG REYFRFSVGG
MTDVAEIKGH RRTYVGAMPG KIIQCLKKTK TENPLVLIDE VDKIGRGYQG DPSSALLELL
DPEQNANFLD HYLDVPVDLS KVLFICTANV IDTIPEPLRD RMEMINVSGY VAQEKLAIAE
RYLVPQARTL CGLDESKAQL SAAVLTLLIK QYCRESGVRN LQKQVEKVLR KAAYKIVSGE
AQTVQVTPEN LQDFVGKPVF TVERMYEVTP PGVVMGLAWT AMGGSTLFVE TSLRRPQPSG
SKEDKDGSLE VTGQLGDVMK ESARIAYTYA RAFLMEQDPE NDFLVTSHIH LHVPEGATPK
DGPSAGCTIV TALLSLALGQ PVLQNLAMTG EVSLTGKVLP VGGIKEKTIA AKRAGVTCII
LPAENRKDYS DLAPFITEGL EVHFVEHYRD IFPIAFPRRE HREALAVER
