LONP2_BOVIN
ID LONP2_BOVIN Reviewed; 852 AA.
AC Q3SX23;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-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. 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. May interact with
CC enzymes involved in beta-oxidation of fatty acids, including ACOX1/AOX
CC (By similarity). {ECO:0000250|UniProtKB:Q86WA8, ECO:0000255|HAMAP-
CC 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; BC104547; AAI04548.1; -; mRNA.
DR RefSeq; NP_001029895.1; NM_001034723.1.
DR AlphaFoldDB; Q3SX23; -.
DR SMR; Q3SX23; -.
DR STRING; 9913.ENSBTAP00000014427; -.
DR PaxDb; Q3SX23; -.
DR PRIDE; Q3SX23; -.
DR Ensembl; ENSBTAT00000014427; ENSBTAP00000014427; ENSBTAG00000010867.
DR GeneID; 541085; -.
DR KEGG; bta:541085; -.
DR CTD; 83752; -.
DR VEuPathDB; HostDB:ENSBTAG00000010867; -.
DR VGNC; VGNC:30948; LONP2.
DR eggNOG; KOG2004; Eukaryota.
DR GeneTree; ENSGT00530000063553; -.
DR HOGENOM; CLU_004109_4_2_1; -.
DR InParanoid; Q3SX23; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 528132at2759; -.
DR TreeFam; TF317215; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000010867; Expressed in liver and 107 other tissues.
DR ExpressionAtlas; Q3SX23; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
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:0002020; F:protease binding; IEA:Ensembl.
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 GO; GO:0031998; P:regulation of fatty acid beta-oxidation; IEA:Ensembl.
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_0000287639"
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; 94310 MW; 1D8493964F0DC9B3 CRC64;
MSSVSPIQIP SRLPLLLTHE GVLLPGSTMR TSVDSARNLQ LVRSRLLKGT SLQSTILGVI
PNTPDPASDA QDLPPLHRIG TAALAVQVVG SNWPKPHYTL LITGLCRFQI TQVVREKPYP
VAEVEQLDRL EEFPNTCKTR EELGELSEQF YKYAVQLVEM LDMSVPAVAK LRRLLDSLPR
EALPDILTSI IRTSNKEKLQ ILDAVSLEER FKMTIPLLVR QIEGLKLLQK TRKHKQDDDK
RVIAIRPMRR ITHVPGALAD EDEDEDNDDI VMLEKKIRTS SMPEQAHKVC VKEIKRLKKM
PQSMPEYALT RNYLELMVEL PWNKSTTDRL DIRAARVLLD NDHYAMEKLK KRVLEYLAVR
QLKNNLKGPI LCFVGPPGVG KTSVGRSVAK TLGREFHRIA LGGVCDQSDI RGHRRTYVGS
MPGRIINGLK TVGVNNPVFL LDEVDKLGKS LQGDPAAALL EVLDPEQNHN FTDHYLNVAF
DLSQVLFIAT ANTTASIPPA LLDRMEIIQV PGYTQEEKIE IAHRHLIPKQ LEQHGLTPQQ
IQIPQVTTLD IITRYTREAG VRSLDRKLGA ICRAVAVKVA EGQHREAKLD RPDVAEGEGC
KEHLLEDGKS DPVSDTTDLA LPPEMPILID FHALKDILGP PMYEMEVSER LSQPGVAIGL
AWTPLGGEIM FVEASRMDGE GQLTLTGQLG NVMKESAHLA ISWLRSNAKK YHLTNASGSF
DLLENTDIHL HFPAGAVTKD GPSAGVTIAT CLASLFSGRL VRSDVAMTGE ITLRGLVLPV
GGIKDKALAA HRAGLKRVII PQRNEKDLEE IPANVRQDLS FITASCLDEV LNAAFDGGFT
VKARPGLLNS KL
