ID   LONP2_ARATH             Reviewed;         888 AA.
AC   O64948; Q8GT60;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   24-JAN-2024, entry version 164.
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=LON2; OrderedLocusNames=At5g47040; ORFNames=MQD22.18;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Landsberg erecta;
RA   Murray C., Christeller J.T., Gatehouse L.N., Laing W.A.;
RT   "Isolation and sequence analysis of a genomic clone of Arabidopsis thaliana
RT   encoding a LON protein.";
RL   (er) Plant Gene Register PGR98-023(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA   Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT   features of the regions of 1,367,185 bp covered by 19 physically assigned
RT   P1 and TAC clones.";
RL   DNA Res. 5:203-216(1998).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 317-888.
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=19329564; DOI=10.1104/pp.109.137703;
RA   Reumann S., Quan S., Aung K., Yang P., Manandhar-Shrestha K., Holbrook D.,
RA   Linka N., Switzenberg R., Wilkerson C.G., Weber A.P., Olsen L.J., Hu J.;
RT   "In-depth proteome analysis of Arabidopsis leaf peroxisomes combined with
RT   in vivo subcellular targeting verification indicates novel metabolic and
RT   regulatory functions of peroxisomes.";
RL   Plant Physiol. 150:125-143(2009).
RN   [6]
RP   FUNCTION.
RX   PubMed=19748917; DOI=10.1104/pp.109.142505;
RA   Lingard M.J., Bartel B.;
RT   "Arabidopsis LON2 is necessary for peroxisomal function and sustained
RT   matrix protein import.";
RL   Plant Physiol. 151:1354-1365(2009).
CC   -!- FUNCTION: ATP-dependent serine protease that mediates the selective
CC       degradation of misfolded and unassembled polypeptides in the
CC       peroxisomal matrix (By similarity). Necessary for type 2 peroxisome
CC       targeting signal (PTS2)-containing protein processing and facilitates
CC       peroxisome matrix protein import. {ECO:0000255|HAMAP-Rule:MF_03121,
CC       ECO:0000269|PubMed:19748917}.
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, ECO:0000269|PubMed:19329564}.
CC   -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03121}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO00734.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF033862; AAC05085.1; -; Genomic_DNA.
DR   EMBL; AB013394; BAB10243.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED95460.1; -; Genomic_DNA.
DR   EMBL; BT002374; AAO00734.1; ALT_INIT; mRNA.
DR   EMBL; BT010392; AAQ56835.1; -; mRNA.
DR   RefSeq; NP_568675.1; NM_124075.4.
DR   AlphaFoldDB; O64948; -.
DR   SMR; O64948; -.
DR   BioGRID; 19998; 1.
DR   STRING; 3702.O64948; -.
DR   MEROPS; S16.003; -.
DR   iPTMnet; O64948; -.
DR   PaxDb; 3702-AT5G47040-1; -.
DR   ProteomicsDB; 238521; -.
DR   EnsemblPlants; AT5G47040.1; AT5G47040.1; AT5G47040.
DR   GeneID; 834750; -.
DR   Gramene; AT5G47040.1; AT5G47040.1; AT5G47040.
DR   KEGG; ath:AT5G47040; -.
DR   Araport; AT5G47040; -.
DR   TAIR; AT5G47040; LON2.
DR   eggNOG; KOG2004; Eukaryota.
DR   HOGENOM; CLU_004109_4_0_1; -.
DR   InParanoid; O64948; -.
DR   OMA; GAWQVVD; -.
DR   OrthoDB; 1103874at2759; -.
DR   PhylomeDB; O64948; -.
DR   BRENDA; 3.4.21.53; 399.
DR   BRENDA; 3.6.4.7; 399.
DR   PRO; PR:O64948; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; O64948; baseline and differential.
DR   GO; GO:0070013; C:intracellular organelle lumen; IDA:TAIR.
DR   GO; GO:0005782; C:peroxisomal matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005777; C:peroxisome; IDA:TAIR.
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:0048527; P:lateral root development; IMP:TAIR.
DR   GO; GO:0016560; P:protein import into peroxisome matrix, docking; IDA:TAIR.
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   CDD; cd19500; RecA-like_Lon; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.20.5.5270; -; 1.
DR   Gene3D; 1.20.58.1480; -; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 2.30.130.40; LON domain-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   NCBIfam; TIGR00763; lon; 1.
DR   PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10046:SF24; LON PROTEASE HOMOLOG 2, PEROXISOMAL; 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   PRINTS; PR00830; ENDOLAPTASE.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00464; LON; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF88697; PUA domain-like; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS51787; LON_N; 1.
DR   PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR   PROSITE; PS01046; LON_SER; 1.
DR   Genevisible; O64948; AT.
PE   2: Evidence at transcript level;
KW   ATP-binding; Hydrolase; Nucleotide-binding; Peroxisome; Protease;
KW   Reference proteome; Serine protease.
FT   CHAIN           1..888
FT                   /note="Lon protease homolog 2, peroxisomal"
FT                   /id="PRO_0000026736"
FT   DOMAIN          11..255
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          692..877
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   MOTIF           886..888
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   ACT_SITE        783
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   ACT_SITE        826
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   BINDING         408..415
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
SQ   SEQUENCE   888 AA;  97862 MW;  D7BAE741926A6F2F CRC64;
     MAETVELPSR LAILPFRNKV LLPGAIIRIR CTSHSSVTLV EQELWQKEEK GLIGILPVRD
     DAEGSSIGTM INPGAGSDSG ERSLKFLVGT TDAQKSDAKD QQDLQWHTRG VAARALHLSR
     GVEKPSGRVT YVVVLEGLSR FNVQELGKRG PYSVARITSL EMTKAELEQV KQDPDFVALS
     RQFKTTAMEL VSVLEQKQKT GGRTKVLLET VPIHKLADIF VASFEMSFEE QLSMLDSVDL
     KVRLSKATEL VDRHLQSIRV AEKITQKVEG QLSKSQKEYL LRQQMRAIKE ELGDNDDDED
     DVAALERKMQ AAGMPSNIWK HAQRELRRLK KMQPQQPGYN SSRVYLELLA DLPWDKASEE
     HELDLKAAKE RLDSDHYGLA KVKQRIIEYL AVRKLKPDAR GPVLCFVGPP GVGKTSLASS
     IAAALGRKFV RLSLGGVKDE ADIRGHRRTY IGSMPGRLID GLKRVGVCNP VMLLDEIDKT
     GSDVRGDPAS ALLEVLDPEQ NKSFNDHYLN VPYDLSKVVF VATANRVQPI PPPLLDRMEL
     IELPGYTQEE KLKIAMRHLI PRVLDQHGLS SEFLKIPEAM VKNIIQRYTR EAGVRSLERN
     LAALARAAAV MVAEHEQSLP LSKDVQKLTS PLLNGRMAEG GEVEMEVIPM GVNDHEIGGT
     FQSPSALVVD ETMLEKILGP PRFDDSEAAD RVASAGVSVG LVWTTFGGEV QFVEATSMVG
     KGEMHLTGQL GDVIKESAQL ALTWVRARAS DFKLALAGDM NVLDGRDIHI HFPAGAVPKD
     GPSAGVTLVT ALVSLFSQKR VRADTAMTGE MTLRGLVLPV GGIKDKILAA HRYGIKRVIL
     PQRNSKDLVE VPAAVLSSLE VILAKRMEDV LENAFEGGCP WRNNYSKL
//