LONP2_XENLA
ID LONP2_XENLA Reviewed; 856 AA.
AC Q2TAF8;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=lonp2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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; BC110947; AAI10948.1; -; mRNA.
DR RefSeq; NP_001089948.1; NM_001096479.1.
DR AlphaFoldDB; Q2TAF8; -.
DR SMR; Q2TAF8; -.
DR MaxQB; Q2TAF8; -.
DR DNASU; 735018; -.
DR GeneID; 735018; -.
DR KEGG; xla:735018; -.
DR CTD; 735018; -.
DR Xenbase; XB-GENE-948729; lonp2.L.
DR OMA; GAWQVVD; -.
DR OrthoDB; 528132at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 735018; Expressed in intestine and 19 other tissues.
DR GO; GO:0005782; C:peroxisomal matrix; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:UniProtKB-UniRule.
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; IPR008268; Peptidase_S16_AS.
DR InterPro; IPR015947; PUA-like_sf.
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 SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00763; lon; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS01046; LON_SER; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Hydrolase; Nucleotide-binding; Peroxisome; Protease;
KW Reference proteome; Serine protease.
FT CHAIN 1..856
FT /note="Lon protease homolog 2, peroxisomal"
FT /id="PRO_0000287645"
FT DOMAIN 13..220
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 655..841
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 586..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 854..856
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT COMPBIAS 586..610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 747
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT ACT_SITE 790
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT BINDING 379..386
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
SQ SEQUENCE 856 AA; 94572 MW; B9A9BE31CAFF2936 CRC64;
MASSGSIQIP RRLPLLLTHE GVLLPGSTMR TSVDTPGNME LVQNRLLRGT SLKSTIIGVV
PNTSDPSSDR EELPSLHRIG TAALAVQVVG SNWPKPHYTL LVTGLCRFQI TEILKERPYP
VAEVEQLDRL EQLSSKEEFK EALGDLSEQF YKYAVQLVDM LDNSVPAVAK LKRLLNNLPK
ELLPDVLTSI IRTTNEEKLQ ILDAVSLEER FKVTIPLLLR QIEGLKLLQK TRNPKQDDDK
RIVAIRPPRK LGNISSKSFS LENTDDDDED SDDIIILERK IKSSNMPEPA LKVCVKEIKR
LKKMPQSMPE YALTRNYLEL MSELPWSKTT RDRLDIRAAR ILLDNDHYAM AKLKKRVLEY
LAVRQLKNNL KGPILCFVGP PGVGKTSVGR SIAKTLGREF HRIALGGVCD QSDIRGHRRT
YVGSMPGRII NGLKIVGVNN PVFLLDEVDK LGKSLQGDPA AALLEVLDPE QNHNFTDHYL
NVAFDLSQVL FIATANTTAT IPPALLDRME VLEVPGYSQE EKLEIAHRHL ISKQLAQHGL
TPEQIQIPQE ATLEIITRYT REAGVRSLDR KLGAICRAVA VKVAEGQHRE HKSEHLEAPE
GEERKESVPE GSKSATINDT ADFALPPEMP ILIDHHALKD ILGPPMYETE VFGRLNQPGV
AIGLAWTPLG GEIMFVEASR MDGEGQLTLT GQLGDVMKES AHLAISWLRS NAKKYQLTNA
SGSFDLLDNT DIHLHFPAGA VTKDGPSAGV AIVTCLASLF SGRLVCSDVA MTGEITLRGL
VLPVGGIKDK VLAAHRAGLK RVILPKRNET DLEEIPLNVR QDLEFVLAGS LDEVLNAAFD
GGFSLKTTPD LLNSKL
