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 Genevisible; O64948; AT.
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.
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
//
