CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016270
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
 LONP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
367RQLKNNLKGPILCFVubiquitination[1]
Reference
 [1] 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 (By similarity). May indirectly regulate peroxisomal fatty acid beta-oxidation through degradation of the self-processed forms of TYSND1. 
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
 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 GVLLPGSTMR TSVDSARNLQ LVRSRLLKGT SLQSTILGVI 60
PNTPDPASDA QDLPPLHRIG TAALAVQVVG SNWPKPHYTL LITGLCRFQI VQVLKEKPYP 120
IAEVEQLDRL EEFPNTCKMR EELGELSEQF YKYAVQLVEM LDMSVPAVAK LRRLLDSLPR 180
EALPDILTSI IRTSNKEKLQ ILDAVSLEER FKMTIPLLVR QIEGLKLLQK TRKPKQDDDK 240
RVIAIRPIRR ITHISGTLED EDEDEDNDDI VMLEKKIRTS SMPEQAHKVC VKEIKRLKKM 300
PQSMPEYALT RNYLELMVEL PWNKSTTDRL DIRAARILLD NDHYAMEKLK KRVLEYLAVR 360
QLKNNLKGPI LCFVGPPGVG KTSVGRSVAK TLGREFHRIA LGGVCDQSDI RGHRRTYVGS 420
MPGRIINGLK TVGVNNPVFL LDEVDKLGKS LQGDPAAALL EVLDPEQNHN FTDHYLNVAF 480
DLSQVLFIAT ANTTATIPAA LLDRMEIIQV PGYTQEEKIE IAHRHLIPKQ LEQHGLTPQQ 540
IQIPQVTTLD IITRYTREAG VRSLDRKLGA ICRAVAVKVA EGQHKEAKLD RSDVTEREGC 600
REHILEDEKP ESISDTTDLA LPPEMPILID FHALKDILGP PMYEMEVSQR LSQPGVAIGL 660
AWTPLGGEIM FVEASRMDGE GQLTLTGQLG DVMKESAHLA ISWLRSNAKK YQLTNAFGSF 720
DLLDNTDIHL HFPAGAVTKD GPSAGVTIVT CLASLFSGRL VRSDVAMTGE ITLRGLVLPV 780
GGIKDKVLAA HRAGLKQVII PRRNEKDLEG IPGNVRQDLS FVTASCLDEV LNAAFDGGFT 840
VKTRPGLLNS KL 852 
Gene Ontology
 GO:0009295; C:nucleoid; IBA:RefGenome.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0005782; C:peroxisomal matrix; IBA:RefGenome.
 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:0006625; P:protein targeting to peroxisome; NAS:UniProtKB.
 GO:0031998; P:regulation of fatty acid beta-oxidation; IMP:UniProtKB.
 GO:0014070; P:response to organic cyclic compound; IEA:Compara.
 GO:0006465; P:signal peptide processing; IMP:UniProtKB. 
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