CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020957
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lon protease homolog 2, peroxisomal 
Protein Synonyms/Alias
 Lon protease-like protein 2; Lon protease 2; Peroxisomal Lon protease 
Gene Name
 Lonp2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
348NDHYAMEKLKRRVLEacetylation[1]
Reference
 [1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123
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 13 219 Lon.
 NP_BIND 375 382 ATP (Potential).
 MOTIF 850 852 Microbody targeting signal (Potential).
 ACT_SITE 743 743 By similarity.
 ACT_SITE 786 786 By similarity.  
Keyword
 Alternative splicing; ATP-binding; Complete proteome; Hydrolase; Nucleotide-binding; Peroxisome; Protease; Reference proteome; Serine protease. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 852 AA 
Protein Sequence
MSSVSPIQIP SRLPLLLTHE SVLLPGSTMR TSVDTARNLQ LVRSRLLKGT SLQSTILGVI 60
PNTPDPASDT QDLPPLHRIG TAALAVQVVG SNWPKPHYTL LITGLCRFQI VQVLKEKPYP 120
VAEVEQLDRL EEFPNICKSR EELGELSEQF YRYAVQLVEM LDMSVPAVAK LRRLLDNLPR 180
EALPDILTSI IRTSNKEKLQ ILDAVSLEDR FKMTIPLLVR QIEGLKLLQK TRKPKQDDDK 240
RVIAIRPIRR IPHIPGTLED EEEEEDNDDI VMLEKKIRTS SMPEQAHKVC VKEIKRLKKM 300
PQSMPEYALT RNYLELMVEL PWNKSTTDRL DIRAARILLD NDHYAMEKLK RRVLEYLAVR 360
QLKNNLKGPI LCFVGPPGVG KTSVGRSVAK TLGREFHRIA LGGVCDQSDI RGHRRTYVGS 420
MPGRIINGLK TVGVNNPVFL LDEVDKLGKS LQGDPAAALL EVLDPEQNHN FTDHYLNVAF 480
DLSQVLFIAT ANTTATIPPA LLDRMEIIQV PGYTQEEKIE IAHRHLIPKQ LEQHGLTPQQ 540
IQIPQHTTLA IITRYTREAG VRSLDRKFGA ICRAVAVKVA EGQHKEAKLD RSDVADGEGC 600
KEHVLEDAKP ESISDTADLA LPPEMPILID SHALKDILGP PLYELEVMIL ISMFTLVLA 659 
Gene Ontology
 GO:0009295; C:nucleoid; IBA:RefGenome.
 GO:0005634; C:nucleus; IDA:MGI.
 GO:0005782; C:peroxisomal matrix; ISS:HGNC.
 GO:0005524; F:ATP binding; IBA:RefGenome.
 GO:0004176; F:ATP-dependent peptidase activity; IBA:RefGenome.
 GO:0043565; F:sequence-specific DNA binding; IBA:RefGenome.
 GO:0004252; F:serine-type endopeptidase activity; IBA:RefGenome.
 GO:0006515; P:misfolded or incompletely synthesized protein catabolic process; IBA:RefGenome.
 GO:0016558; P:protein import into peroxisome matrix; IEA:HAMAP.
 GO:0016485; P:protein processing; IBA:RefGenome.
 GO:0031998; P:regulation of fatty acid beta-oxidation; IEA:Compara.
 GO:0014070; P:response to organic cyclic compound; IEA:Compara.
 GO:0006465; P:signal peptide processing; IEA:Compara. 
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