CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018710
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lon protease homolog, mitochondrial 
Protein Synonyms/Alias
 Lon protease-like protein; LONP; Mitochondrial ATP-dependent protease Lon; Serine protease 15 
Gene Name
 Lonp1 
Gene Synonyms/Alias
 Lon; Prss15 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
136IVEVKNKKLVELLRRacetylation[1]
243VGDELGAKPQLEMVTacetylation[1]
288ALTAEIVKTIRDIIAacetylation[1]
347LEETNILKRLYKALSacetylation[1]
357YKALSLLKKEFELSKacetylation[1]
358KALSLLKKEFELSKLacetylation[1]
376LGREVEEKIKQTHRKacetylation[1]
401KKELGLEKDDKDAIEacetylation[1]
404LGLEKDDKDAIEEKFacetylation[1]
416EKFRERLKELVVPKHacetylation[1]
422LKELVVPKHVMDVVDacetylation[1]
571IQCLKKTKTENPLVLacetylation[1]
584VLIDEVDKIGRGYQGacetylation[1]
738NLQDFVGKPVFTVERacetylation[1]
886VLPVGGIKEKTIAAKacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
Functional Description
 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 (By similarity). 
Sequence Annotation
 DOMAIN 112 358 Lon.
 NP_BIND 513 520 ATP (By similarity).
 ACT_SITE 845 845 By similarity.
 ACT_SITE 888 888 By similarity.  
Keyword
 ATP-binding; Complete proteome; DNA-binding; Hydrolase; Mitochondrion; Nucleotide-binding; Protease; Reference proteome; Serine protease; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 950 AA 
Protein Sequence
MAASTGYVRL WAAARCWVLR RPLLAVTGGR VPSASGSWLR RGCRVCDTST PWGGRVPMGG 60
GQWRGLWDAG SRGGSDETSE GGVEDGATAS SGEGPVVTAL APMTVPDVFP HLPLIAISRN 120
PVFPRFIKIV EVKNKKLVEL LRRKVRLAQP YVGVFLKRDD NNESDVVESL DEIYHTGTFA 180
QIHEMQDLGD KLRMIVTGHR RIHISRQLEV EPEGLEPEAE NKQKSRRKLK RGKKEVGDEL 240
GAKPQLEMVT EATSDTSKEV LMVEVENVAH EDFQVTEEVK ALTAEIVKTI RDIIALNPLY 300
RESVLQMMQA GQRVVDNPIY LSDMGAALTG AESHELQDVL EETNILKRLY KALSLLKKEF 360
ELSKLQQRLG REVEEKIKQT HRKYLLQEQL KIIKKELGLE KDDKDAIEEK FRERLKELVV 420
PKHVMDVVDE ELSKLALLDN HSSEFNVTRN YLDWLTSIPW GRQSDENLDL ARAQSVLEED 480
HYGMEDVKKR VLEFIAVSQL RGSTQGKILC FHGPPGVGKT SIARSIARAL GREYFRFSVG 540
GMTDVAEIKG HRRTYVGAMP GKIIQCLKKT KTENPLVLID EVDKIGRGYQ GDPSSALLEL 600
LDPEQNANFL DHYLDVPVDL SKVLFICTAN VTDTIPEPLR DRMEMINVSG YVAQEKLAIA 660
ERYLVPQART LCGLDESKAQ LSATVLTLLI KQYCRESGVR NLQKQVEKVL RKAAYKIVSG 720
EAQTVHVTPE NLQDFVGKPV FTVERMYDVT PPGVVMGLAW TAMGGSTLFV ETSLRRPQPS 780
GSKEDKDGSL EVTGQLGDVM KESARIAYTF ARAFLMEQDP ENDFLVTSHI HLHVPEGATP 840
KDGPSAGCTI VTALLSLALG QPVLQNLAMT GEVSLTGKVL PVGGIKEKTI AAKRAGVTCI 900
ILPAENRKDF SDLAPFITEG LEVHFVEHYR DIFRIAFPLR EHQEALAVER 950 
Gene Ontology
 GO:0042645; C:mitochondrial nucleoid; IBA:RefGenome.
 GO:0043531; F:ADP binding; IEA:Compara.
 GO:0005524; F:ATP binding; IBA:RefGenome.
 GO:0004176; F:ATP-dependent peptidase activity; IDA:RGD.
 GO:0051880; F:G-quadruplex DNA binding; IEA:Compara.
 GO:0070362; F:mitochondrial heavy strand promoter anti-sense binding; IEA:Compara.
 GO:0070361; F:mitochondrial light strand promoter anti-sense binding; IBA:RefGenome.
 GO:0043565; F:sequence-specific DNA binding; IEA:HAMAP.
 GO:0004252; F:serine-type endopeptidase activity; IBA:RefGenome.
 GO:0003697; F:single-stranded DNA binding; IBA:RefGenome.
 GO:0003727; F:single-stranded RNA binding; IBA:RefGenome.
 GO:0007568; P:aging; IEP:RGD.
 GO:0043623; P:cellular protein complex assembly; IMP:RGD.
 GO:0034599; P:cellular response to oxidative stress; IBA:RefGenome.
 GO:0051131; P:chaperone-mediated protein complex assembly; IEA:HAMAP.
 GO:0006515; P:misfolded or incompletely synthesized protein catabolic process; IBA:RefGenome.
 GO:0007005; P:mitochondrion organization; IEP:RGD.
 GO:0070407; P:oxidation-dependent protein catabolic process; IBA:RefGenome.
 GO:0051260; P:protein homooligomerization; IBA:RefGenome.
 GO:0090296; P:regulation of mitochondrial DNA replication; IEA:HAMAP.
 GO:0010044; P:response to aluminum ion; IEP:RGD.
 GO:0009725; P:response to hormone stimulus; IEP:RGD.
 GO:0001666; P:response to hypoxia; IEP:RGD. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR003959; ATPase_AAA_core.
 IPR004815; Lon_bac/euk-typ.
 IPR027065; Lon_Prtase.
 IPR027503; lonm_euk.
 IPR027417; P-loop_NTPase.
 IPR008269; Pept_S16_C.
 IPR003111; Pept_S16_N.
 IPR008268; Peptidase_S16_AS.
 IPR015947; PUA-like_domain.
 IPR020568; Ribosomal_S5_D2-typ_fold.
 IPR014721; Ribosomal_S5_D2-typ_fold_subgr. 
Pfam
 PF00004; AAA
 PF02190; LON
 PF05362; Lon_C 
SMART
 SM00382; AAA
 SM00464; LON 
PROSITE
 PS01046; LON_SER 
PRINTS