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Lon protease homolog, mitochondrial (EC 3.4.21.53) (Lon protease-like protein) (LONP) (Mitochondrial ATP-dependent protease Lon) (Serine protease 15)

 LONM_MOUSE              Reviewed;         949 AA.
Q8CGK3; Q3TSK9; Q3TVL2; Q3TXE4; Q3TZW3; Q9DBP9;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
31-OCT-2006, sequence version 2.
18-JUL-2018, entry version 139.
RecName: Full=Lon protease homolog, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03120};
EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_03120};
AltName: Full=Lon protease-like protein {ECO:0000255|HAMAP-Rule:MF_03120};
Short=LONP {ECO:0000255|HAMAP-Rule:MF_03120};
AltName: Full=Mitochondrial ATP-dependent protease Lon {ECO:0000255|HAMAP-Rule:MF_03120};
AltName: Full=Serine protease 15 {ECO:0000255|HAMAP-Rule:MF_03120};
Flags: Precursor;
Name=Lonp1; Synonyms=Prss15;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DNA-BINDING, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
STRAIN=BALB/cJ; TISSUE=Kidney;
PubMed=12657466; DOI=10.1016/S0378-1119(03)00403-7;
Lu B., Liu T., Crosby J.A., Thomas-Wohlever J., Lee I., Suzuki C.K.;
"The ATP-dependent Lon protease of Mus musculus is a DNA-binding
protein that is functionally conserved between yeast and mammals.";
Gene 306:45-55(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Lung, Ovary, and Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
PROTEIN SEQUENCE OF 434-448; 490-500 AND 930-938, AND IDENTIFICATION
BY MASS SPECTROMETRY.
TISSUE=Hippocampus;
Lubec G., Klug S.;
Submitted (MAR-2007) to UniProtKB.
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: ATP-dependent serine protease that mediates the
selective degradation of misfolded, unassembled or oxidatively
damaged polypeptides as well as certain short-lived regulatory
proteins in the mitochondrial matrix. May also have a chaperone
function in the assembly of inner membrane protein complexes.
Participates in the regulation of mitochondrial gene expression
and in the maintenance of the integrity of the mitochondrial
genome. Binds to mitochondrial promoters and RNA in a single-
stranded, site-specific, and strand-specific manner. May regulate
mitochondrial DNA replication and/or gene expression using site-
specific, single-stranded DNA binding to target the degradation of
regulatory proteins binding to adjacent sites in mitochondrial
promoters. {ECO:0000255|HAMAP-Rule:MF_03120,
ECO:0000269|PubMed:12657466}.
-!- CATALYTIC ACTIVITY: Hydrolysis of proteins in presence of ATP.
{ECO:0000255|HAMAP-Rule:MF_03120}.
-!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
The ATP-binding and proteolytic domains (AP-domain) form a
hexameric chamber, while the N-terminal domain is arranged as a
trimer of dimers. DNA and RNA binding is stimulated by substrate
and inhibited by ATP binding. Interacts with TWNK and
mitochondrial DNA polymerase subunit POLG. {ECO:0000255|HAMAP-
Rule:MF_03120}.
-!- INTERACTION:
P81122:Irs2; NbExp=2; IntAct=EBI-911958, EBI-1369862;
-!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
Rule:MF_03120, ECO:0000269|PubMed:12657466}.
-!- TISSUE SPECIFICITY: Detected in liver > heart > kidney > testis.
{ECO:0000269|PubMed:12657466}.
-!- SIMILARITY: Belongs to the peptidase S16 family.
{ECO:0000255|HAMAP-Rule:MF_03120}.
-----------------------------------------------------------------------
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EMBL; AY190302; AAN85210.1; -; mRNA.
EMBL; AK004820; BAB23591.1; -; mRNA.
EMBL; AK157474; BAE34094.1; -; mRNA.
EMBL; AK159302; BAE34972.1; -; mRNA.
EMBL; AK160071; BAE35606.1; -; mRNA.
EMBL; AK161983; BAE36666.1; -; mRNA.
CCDS; CCDS28910.1; -.
RefSeq; NP_083058.2; NM_028782.2.
UniGene; Mm.329136; -.
ProteinModelPortal; Q8CGK3; -.
SMR; Q8CGK3; -.
BioGrid; 216521; 2.
IntAct; Q8CGK3; 5.
MINT; Q8CGK3; -.
STRING; 10090.ENSMUSP00000041814; -.
ChEMBL; CHEMBL3259486; -.
MEROPS; S16.002; -.
iPTMnet; Q8CGK3; -.
PhosphoSitePlus; Q8CGK3; -.
SwissPalm; Q8CGK3; -.
REPRODUCTION-2DPAGE; Q8CGK3; -.
REPRODUCTION-2DPAGE; Q9DBP9; -.
EPD; Q8CGK3; -.
MaxQB; Q8CGK3; -.
PaxDb; Q8CGK3; -.
PeptideAtlas; Q8CGK3; -.
PRIDE; Q8CGK3; -.
DNASU; 74142; -.
Ensembl; ENSMUST00000047226; ENSMUSP00000041814; ENSMUSG00000041168.
GeneID; 74142; -.
KEGG; mmu:74142; -.
UCSC; uc008dcp.2; mouse.
CTD; 9361; -.
MGI; MGI:1921392; Lonp1.
eggNOG; KOG2004; Eukaryota.
eggNOG; COG0466; LUCA.
GeneTree; ENSGT00530000063553; -.
HOGENOM; HOG000261409; -.
HOVERGEN; HBG000798; -.
InParanoid; Q8CGK3; -.
KO; K08675; -.
OMA; RSAENFG; -.
OrthoDB; EOG091G01TN; -.
PhylomeDB; Q8CGK3; -.
TreeFam; TF105001; -.
ChiTaRS; Lonp1; mouse.
PRO; PR:Q8CGK3; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000041168; -.
CleanEx; MM_LONP1; -.
Genevisible; Q8CGK3; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
GO; GO:0042645; C:mitochondrial nucleoid; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0043531; F:ADP binding; ISO:MGI.
GO; GO:0005524; F:ATP binding; ISO:MGI.
GO; GO:0004176; F:ATP-dependent peptidase activity; IDA:MGI.
GO; GO:0016887; F:ATPase activity; IDA:MGI.
GO; GO:0070182; F:DNA polymerase binding; ISO:MGI.
GO; GO:0051880; F:G-quadruplex DNA binding; ISO:MGI.
GO; GO:0001018; F:mitochondrial promoter sequence-specific DNA binding; IDA:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0003697; F:single-stranded DNA binding; IDA:MGI.
GO; GO:0003727; F:single-stranded RNA binding; ISO:MGI.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0034622; P:cellular protein-containing complex assembly; ISO:MGI.
GO; GO:0034599; P:cellular response to oxidative stress; ISO:MGI.
GO; GO:0007005; P:mitochondrion organization; ISO:MGI.
GO; GO:0070407; P:oxidation-dependent protein catabolic process; ISO:MGI.
GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
GO; GO:0006508; P:proteolysis; IDA:MGI.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; ISO:MGI.
GO; GO:0010044; P:response to aluminum ion; IEA:Ensembl.
GO; GO:0009725; P:response to hormone; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
Gene3D; 3.30.230.10; -; 1.
HAMAP; MF_03120; lonm_euk; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR004815; Lon_bac/euk-typ.
InterPro; IPR008269; Lon_proteolytic.
InterPro; IPR027065; Lon_Prtase.
InterPro; IPR003111; Lon_substr-bd.
InterPro; IPR027503; Lonm_euk.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR008268; Peptidase_S16_AS.
InterPro; IPR015947; PUA-like_sf.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
PANTHER; PTHR43718; PTHR43718; 1.
Pfam; PF00004; AAA; 1.
Pfam; PF05362; Lon_C; 1.
Pfam; PF02190; LON_substr_bdg; 1.
PIRSF; PIRSF001174; Lon_proteas; 1.
SMART; SM00382; AAA; 1.
SMART; SM00464; LON; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF54211; SSF54211; 1.
SUPFAM; SSF88697; SSF88697; 1.
TIGRFAMs; TIGR00763; lon; 1.
PROSITE; PS51787; LON_N; 1.
PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PROSITE; PS01046; LON_SER; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Direct protein sequencing;
DNA-binding; Hydrolase; Mitochondrion; Nucleotide-binding; Protease;
Reference proteome; Serine protease; Transit peptide.
TRANSIT 1 65 Mitochondrion. {ECO:0000255|HAMAP-
Rule:MF_03120}.
CHAIN 66 949 Lon protease homolog, mitochondrial.
/FTId=PRO_0000254961.
DOMAIN 112 357 Lon N-terminal. {ECO:0000255|PROSITE-
ProRule:PRU01123}.
DOMAIN 748 938 Lon proteolytic. {ECO:0000255|PROSITE-
ProRule:PRU01122}.
NP_BIND 512 519 ATP. {ECO:0000255|HAMAP-Rule:MF_03120}.
ACT_SITE 844 844 {ECO:0000255|HAMAP-Rule:MF_03120}.
ACT_SITE 887 887 {ECO:0000255|HAMAP-Rule:MF_03120}.
CONFLICT 90 90 S -> G (in Ref. 2; BAB23591).
{ECO:0000305}.
CONFLICT 99 99 A -> T (in Ref. 2; BAE34094).
{ECO:0000305}.
CONFLICT 202 202 I -> T (in Ref. 2; BAB23591).
{ECO:0000305}.
CONFLICT 214 214 G -> R (in Ref. 1; AAN85210).
{ECO:0000305}.
CONFLICT 240 240 G -> S (in Ref. 2; BAE34094).
{ECO:0000305}.
CONFLICT 248 248 V -> L (in Ref. 2; BAE34094).
{ECO:0000305}.
CONFLICT 271 271 D -> Y (in Ref. 2; BAB23591).
{ECO:0000305}.
CONFLICT 368 368 L -> P (in Ref. 2; BAB23591).
{ECO:0000305}.
CONFLICT 424 424 M -> I (in Ref. 2; BAE36666).
{ECO:0000305}.
CONFLICT 449 449 N -> K (in Ref. 2; BAE34972).
{ECO:0000305}.
CONFLICT 636 636 E -> K (in Ref. 2; BAE34094).
{ECO:0000305}.
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


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