LONP2_PONAB
ID LONP2_PONAB Reviewed; 852 AA.
AC Q5R6M5;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
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};
DE AltName: Full=Lon protease-like protein 2 {ECO:0000255|HAMAP-Rule:MF_03121};
DE Short=Lon protease 2 {ECO:0000255|HAMAP-Rule:MF_03121};
DE AltName: Full=Peroxisomal Lon protease {ECO:0000255|HAMAP-Rule:MF_03121};
GN Name=LONP2 {ECO:0000255|HAMAP-Rule:MF_03121};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-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. May indirectly regulate peroxisomal fatty acid beta-
CC oxidation through degradation of the self-processed forms of TYSND1.
CC {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 -!- SUBUNIT: Interacts with PEX5. Interacts with TYSND1 (By similarity).
CC May interact with enzymes involved in beta-oxidation of fatty acids,
CC including ACOX1/AOX (By similarity). {ECO:0000250|UniProtKB:Q86WA8,
CC ECO:0000255|HAMAP-Rule:MF_03121}.
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000250|UniProtKB:Q86WA8,
CC ECO:0000255|HAMAP-Rule:MF_03121}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC Rule:MF_03121}.
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DR EMBL; CR860463; CAH92585.1; -; mRNA.
DR RefSeq; NP_001126515.1; NM_001133043.2.
DR AlphaFoldDB; Q5R6M5; -.
DR SMR; Q5R6M5; -.
DR STRING; 9601.ENSPPYP00000008277; -.
DR GeneID; 100173503; -.
DR KEGG; pon:100173503; -.
DR CTD; 83752; -.
DR eggNOG; KOG2004; Eukaryota.
DR InParanoid; Q5R6M5; -.
DR OrthoDB; 528132at2759; -.
DR Proteomes; UP000001595; Unplaced.
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 Acetylation; ATP-binding; Hydrolase; Nucleotide-binding; Peroxisome;
KW Protease; Reference proteome; Serine protease.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q86WA8"
FT CHAIN 2..852
FT /note="Lon protease homolog 2, peroxisomal"
FT /id="PRO_0000287643"
FT DOMAIN 13..220
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 651..837
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT MOTIF 850..852
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT ACT_SITE 743
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT ACT_SITE 786
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"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WA8"
SQ SEQUENCE 852 AA; 94745 MW; AF64885EAB46DE89 CRC64;
MSSVSPIQIP SRLPLLLTHE GVLLPGSTMR TSVDSARNLQ LVRSRLLKGT SLQSTILGVI
PNTPDPASDA QDLPPLHRIG TAALAVQVVG SNWPKPHYTL LITGLCRFQI VQVLKEKPYP
IAEVEQLDRL EEFPSTCKMR EELGELSEQF YKYAVQLVEM LDMSVPAVAK LRRLLDSLPR
EALPDILTSI IRTSNKEKLQ ILDAVSLEER FKMTIPLLVR QIEGLKLLQK TRKPKQDDDK
RVIAIRPIRR ITHISGTLED EDEDEDNDDI VMLEKEIRTS SMPEQAHKVC VKEIKRLKKM
PQSMPEYALT RNYLELMVEL PWNKSTTDRL DIRAARILLD NDHYAMEKLK KRVLEYLVVR
QLKNNLKGPI LCFVGPPGVG KTSVGRLVAK TLGREFHRIA LGGVCDQSDI RGHRRTYVGS
MPGRIINGLK TVGVNNPVFL LDEVDKLGKS LQGDPAAALL EVLDPEQNHN FTDHYLNVAF
DLSRVLFIAT ANTTATIPAA LLDRMEIIQV PGYTQEEKIE IAHRHLIPKQ LEQHGLTPQQ
IQIPQVTTLD IITRYTREAG VRSLDRKLGA ICRAVAVKVA EGQHKEAKLD RSDVTEREGC
REHILEDEKP ESISDTTDLA LPPEMPILID FHALKDILGP PMYEMEVSQR LSQPGVAIGL
AWTPLGGEIM FVEASRMDGE GQLTLTGQLG DVMKESAHLA ISWLRSNAKK YQLTNAFGSF
DLLDNTDIHL HFPAGAVTKD GPSAGVTIVT CLASLFSERL VRSDVAMTGE ITLRGLVLPV
GGIKDKVLAA HRAGLKQVII PRRNEKDLEG IPGNVRQDLS FVTASCLDEV LNAAFDGGFT
VKTRPGLLNS KL
