LONP2_CAEEL
ID LONP2_CAEEL Reviewed; 773 AA.
AC Q9XW87;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Lon protease homolog 2, peroxisomal {ECO:0000255|HAMAP-Rule:MF_03121};
DE EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_03121};
GN Name=lonp-2 {ECO:0000312|WormBase:Y75B8A.4};
GN ORFNames=Y75B8A.4 {ECO:0000312|WormBase:Y75B8A.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: ATP-dependent serine protease that mediates the selective
CC degradation of misfolded and unassembled polypeptides in the
CC peroxisomal matrix. Necessary for type 2 peroxisome targeting signal
CC (PTS2)-containing protein processing and facilitates peroxisome matrix
CC protein import. {ECO:0000255|HAMAP-Rule:MF_03121}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03121};
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000255|HAMAP-
CC Rule:MF_03121}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC Rule:MF_03121}.
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DR EMBL; AL033514; CAA22082.1; -; Genomic_DNA.
DR PIR; T27382; T27382.
DR RefSeq; NP_499577.1; NM_067176.3.
DR AlphaFoldDB; Q9XW87; -.
DR SMR; Q9XW87; -.
DR STRING; 6239.Y75B8A.4; -.
DR MEROPS; S16.A06; -.
DR EPD; Q9XW87; -.
DR PaxDb; Q9XW87; -.
DR PeptideAtlas; Q9XW87; -.
DR EnsemblMetazoa; Y75B8A.4.1; Y75B8A.4.1; WBGene00013541.
DR GeneID; 176643; -.
DR KEGG; cel:CELE_Y75B8A.4; -.
DR UCSC; Y75B8A.4.1; c. elegans.
DR CTD; 176643; -.
DR WormBase; Y75B8A.4; CE23016; WBGene00013541; lonp-2.
DR eggNOG; KOG2004; Eukaryota.
DR GeneTree; ENSGT00530000063553; -.
DR HOGENOM; CLU_004109_4_3_1; -.
DR InParanoid; Q9XW87; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 528132at2759; -.
DR PhylomeDB; Q9XW87; -.
DR Reactome; R-CEL-9033241; Peroxisomal protein import.
DR PRO; PR:Q9XW87; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00013541; Expressed in larva and 4 other tissues.
DR GO; GO:0005782; C:peroxisomal matrix; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016558; P:protein import into peroxisome matrix; IEA:UniProtKB-UniRule.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:UniProtKB-UniRule.
DR GO; GO:0006625; P:protein targeting to peroxisome; IBA:GO_Central.
DR Gene3D; 2.30.130.40; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_03121; lonp2_euk; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR004815; Lon_bac/euk-typ.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR003111; Lon_prtase_N.
DR InterPro; IPR046336; Lon_prtase_N_sf.
DR InterPro; IPR027501; Lonp2_euk.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR10046; PTHR10046; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR PIRSF; PIRSF001174; Lon_proteas; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00464; LON; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR00763; lon; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PE 3: Inferred from homology;
KW ATP-binding; Hydrolase; Nucleotide-binding; Peroxisome; Protease;
KW Reference proteome; Serine protease.
FT CHAIN 1..773
FT /note="Lon protease homolog 2, peroxisomal"
FT /id="PRO_0000395785"
FT DOMAIN 9..196
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 587..766
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT MOTIF 771..773
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT ACT_SITE 672
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT ACT_SITE 715
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT BINDING 336..343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
SQ SEQUENCE 773 AA; 85613 MW; 4D2E64FC04A113EA CRC64;
MKIEENMELP VILVTSGVLL PGASLKIPIR SKLNIQTIEK YLTRSSNDNY VVIAYKVSTD
KVYEVATIAY VEKLFGWTFN STVHYSLDVI GLHRANIDKL SLPTCIVSKV VDLNEAISNQ
NAIEKLVTGA KIIASNSLTD KFSREIYSLI DEKEYGKLAD LCVSQMKFLG FMQLLEFLGA
NGTDARVEMC IKWMNEKKDA NTLKLKVPNS LEASFPVDGK KRKIPNVKNQ VEQLEEKLNA
IEFSDEVSDR VYSELHRLKS MNAQQSEYNI LMNWLELVSS LPWNTSTIDD IELHKARTIL
TESHEAMDDV KERVLEHLAV CKMNNSVKGM ILCFTGPPGI GKTSIAKAIA ESMGRKFQRV
SLGGIRDESD IRGHRRTYVA AMPGRIIEAL KTCKTNNPVF LLDEVDKLYS GNQGSPSAAL
LELLDPEQNS TFHDHYLNIP FDVSKIMFIA TANDIDRLEP ALRDRLEIIE MSGYSLKEKV
KICENHLLTR QLTKHCISHD YVKLERQAIV AMIEEYTMEA GVRQLERNVG AICRNVALRL
AEALNSDPGA DVLPVMELPI QISASNIHKI LKNKHMKRVK IVEKMRPLPA GVCFGLSVTT
IGGRVMPIEA SKSKGTGKIV TTGHLGKVLK ESILVAKGWL SANSERLGLG TLEDQDIHVH
LPAGAVNKDG PSAGTGLACA LVSLATNIPL RSDAAVTGEI SLTGHVLPIG GVKEKVLAAQ
REGLRRVVLP KSNEEEYLKM DEDIRLEMDV VLAETIEDVI GAMMDKSPVL AKL
