LONP2_DANRE
ID LONP2_DANRE Reviewed; 840 AA.
AC Q5PQY6;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
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; ORFNames=zgc:92557;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2004) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC086968; AAH86968.1; -; mRNA.
DR RefSeq; NP_001008573.1; NM_001008573.2.
DR AlphaFoldDB; Q5PQY6; -.
DR SMR; Q5PQY6; -.
DR STRING; 7955.ENSDARP00000036252; -.
DR PaxDb; Q5PQY6; -.
DR GeneID; 494030; -.
DR KEGG; dre:494030; -.
DR CTD; 83752; -.
DR ZFIN; ZDB-GENE-041212-1; lonp2.
DR eggNOG; KOG2004; Eukaryota.
DR InParanoid; Q5PQY6; -.
DR OrthoDB; 528132at2759; -.
DR PhylomeDB; Q5PQY6; -.
DR Reactome; R-DRE-9033241; Peroxisomal protein import.
DR PRO; PR:Q5PQY6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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; 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..840
FT /note="Lon protease homolog 2, peroxisomal"
FT /id="PRO_0000287644"
FT DOMAIN 13..220
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 641..825
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 583..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 838..840
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT COMPBIAS 588..602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 731
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT ACT_SITE 774
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT BINDING 375..382
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
SQ SEQUENCE 840 AA; 92221 MW; C1EC6FC9CCCC4EE1 CRC64;
MSSNSGIQIP SRLPLLCTHD GVLLPGSTMR VSVDTARNMQ LVKSRLLKGT SLKSTIIGVI
PNTRDPEHDS DELPSLHSIG TAGLAVQVVG SNWPKPHYTL LITGLCRFRV SQLLRERPFP
VAEVEQLDKL EQYTEGDPAD GELGELSQRF YQAAVQLVGM LDMSVPVVAK LRRLLDSLPK
ETLPDVLAAM IRTSNKEKLQ VLDAVDLEER FKKALPLLTR QIEGLKLLQK TRKLRPDDDK
RVLSIRKGGV FPGRQFSLDE EVEDEDSDDT ALLERKVKAA AMPEAALRVC LKELRRLKKM
PQSMPEYALT RNYLEMMVEL PWSKSTTDCL DIRAARVLLD NDHYAMEKLK KRVLEYLAVR
QLKSTLKGPI LCFVGPPGVG KTSVGRSIAR TLGREFHRIA LGGVCDQSDI RGHRRTYVGS
MPGRIINGLK TVGVNNPVFL LDEVDKLGKS LQGDPAAALL EVLDPEQNHS FTDHYLNVPF
DLSQVLFIAT ANTTATIPPA LLDRMEVLQV PGYTQEEKVE IAHRHLIPHQ LEQHGLTPQQ
LQIPQDTTLQ IISKYTREAG VRSLERKIGA VCRAVAVKVA EGQKVSRSEA PTEQHAEQNT
DSKVEDSGIA APPEMPIVID HVALKDILGP PLFEMEVSER LTLPGVAIGL AWTPMGGEIM
FVEASRMEGE GQLTLTGQLG DVMKESAHLA ISWLRSNAKT YLLNDGSADL LEGTDIHLHF
PAGAVTKDGP SAGVTIVTCL ASLLSGRLVR SDVAMTGEIT LRGLVLPVGG IKDKVLAAHR
ANLKRIIIPK RNEKDLEEIP ANVRADLDFV LAGTLDEVLN AAFDGGFPSA VNHPQVLSKL
