CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-032259
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lon protease homolog 2, peroxisomal 
Protein Synonyms/Alias
 Lon protease-like protein 2; Peroxisomal Lon protease 
Gene Name
 LONP2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
304NDHYAMEKLKKRVLEacetylation[1]
323RQLKNNLKGPILCFVubiquitination[2]
762IIPRRNEKDLEGIPGacetylation[1]
Reference
 [1] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961] 
Functional Description
 ATP-dependent serine protease that mediates the selective degradation of misfolded and unassembled polypeptides in the peroxisomal matrix. Necessary for type 2 peroxisome targeting signal (PTS2)-containing protein processing and facilitates peroxisome matrix protein import. May indirectly regulate peroxisomal fatty acid beta-oxidation through degradation of the self-processed forms of TYSND1 (By similarity). 
Sequence Annotation
 DOMAIN 13 183 Lon (By similarity).
 NP_BIND 331 338 ATP (By similarity).
 MOTIF 806 808 Microbody targeting signal (By
 ACT_SITE 699 699 By similarity.
 ACT_SITE 742 742 By similarity.  
Keyword
 ATP-binding; Complete proteome; Hydrolase; Nucleotide-binding; Peroxisome; Protease; Reference proteome; Serine protease. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 808 AA 
Protein Sequence
MSSVSPIQIP SRLPLLLTHE GVLLPGSTMR TSVDSARNLQ LVRSRLLKGT SLQSTILGVI 60
PNTPDPASDA QDLPPLHRIG TAALAVQVVG SNWPKPHYTL LITGLCRFQI VQVLKEKPYP 120
IAEVEQLDRL EEFPNTCKMR EELGELSEQF YKYAVQILDA VSLEERFKMT IPLLVRQIEG 180
LKLLQKTRKP KQDDDKRVIA IRPIRRITHI SGTLEDEDED EDNDDIVMLE KKIRTSSMPE 240
QAHKVCVKEI KRLKKMPQSM PEYALTRNYL ELMVELPWNK STTDRLDIRA ARILLDNDHY 300
AMEKLKKRVL EYLAVRQLKN NLKGPILCFV GPPGVGKTSV GRSVAKTLGR EFHRIALGGV 360
CDQSDIRGHR RTYVGSMPGR IINGLKTVGV NNPVFLLDEV DKLGKSLQGD PAAALLEVLD 420
PEQNHNFTDH YLNVAFDLSQ VLFIATANTT ATIPAALLDR MEIIQVPGYT QEEKIEIAHR 480
HLIPKQLEQH GLTPQQIQIP QVTTLDIITR YTREAGVRSL DRKLGAICRA VAVKVAEGQH 540
KEAKLDRSDV TEREGCREHI LEDEKPESIS DTTDLALPPE MPILIDFHAL KDILGPPMYE 600
MEVSQRLSQP GVAIGLAWTP LGGEIMFVEA SRMDGEGQLT LTGQLGDVMK ESAHLAISWL 660
RSNAKKYQLT NAFGSFDLLD NTDIHLHFPA GAVTKDGPSA GVTIVTCLAS LFSGRLVRSD 720
VAMTGEITLR GLVLPVGGIK DKVLAAHRAG LKQVIIPRRN EKDLEGIPGN VRQDLSFVTA 780
SCLDEVLNAA FDGGFTVKTR PGLLNSKL 808 
Gene Ontology
 GO:0005782; C:peroxisomal matrix; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:HAMAP.
 GO:0004176; F:ATP-dependent peptidase activity; IEA:HAMAP.
 GO:0004252; F:serine-type endopeptidase activity; IEA:HAMAP.
 GO:0006200; P:ATP catabolic process; IEA:GOC.
 GO:0006515; P:misfolded or incompletely synthesized protein catabolic process; IEA:HAMAP.
 GO:0016558; P:protein import into peroxisome matrix; IEA:HAMAP.
 GO:0016485; P:protein processing; IEA:HAMAP. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR003959; ATPase_AAA_core.
 IPR004815; Lon_bac/euk-typ.
 IPR027065; Lon_Prtase.
 IPR027501; lonp2_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 
PROSITE
 PS01046; LON_SER 
PRINTS