ID   LONP2_ORYSJ             Reviewed;         884 AA.
AC   Q0J032; Q69SH2;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 112.
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   OrderedLocusNames=Os09g0533400, LOC_Os09g36300;
GN   ORFNames=OJ1112_E07.9, OsJ_30122, P0515E01.28;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 587-884.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
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   -!- SEQUENCE CAUTION:
CC       Sequence=BAD33324.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAD46033.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP005092; BAD33324.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP005314; BAD46033.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP008215; BAF25683.1; -; Genomic_DNA.
DR   EMBL; AP014965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CM000146; EEE70111.1; -; Genomic_DNA.
DR   EMBL; AK061670; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_015611598.1; XM_015756112.1.
DR   AlphaFoldDB; Q0J032; -.
DR   SMR; Q0J032; -.
DR   STRING; 4530.OS09T0533400-01; -.
DR   MEROPS; S16.003; -.
DR   PaxDb; Q0J032; -.
DR   PRIDE; Q0J032; -.
DR   GeneID; 4347683; -.
DR   KEGG; osa:4347683; -.
DR   eggNOG; KOG2004; Eukaryota.
DR   HOGENOM; CLU_091305_0_0_1; -.
DR   InParanoid; Q0J032; -.
DR   OrthoDB; 528132at2759; -.
DR   Proteomes; UP000000763; Chromosome 9.
DR   Proteomes; UP000007752; Chromosome 9.
DR   Proteomes; UP000059680; Chromosome 9.
DR   Genevisible; Q0J032; OS.
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..884
FT                   /note="Lon protease homolog 2, peroxisomal"
FT                   /id="PRO_0000395787"
FT   DOMAIN          12..253
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          689..874
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   REGION          67..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           882..884
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   ACT_SITE        780
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   ACT_SITE        823
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   884 AA;  97278 MW;  E6D1B26154BB974F CRC64;
     MADAAVELPG RLAILPFRNK VLLPGAIVRI RCTNPSSVKL VEQELWQREE KGLIGVLPVH
     DSEAAGSLLS PGVGSDSGEG GSKAPGGSAG ESTKQDTKNG KETIHWHSRG VAARALHLSR
     GVEKPSGRVT YIVVLEGLCR FSVQELSARG SYHVARVSRL DMTKTELEHA EQDPDLIALS
     RQFKATAMEL ISVLEQKQKT VGRTKVLLET VPVYRLADIF VASFEIGFEE QLSMLDSVDL
     KVRLSKATEL VDRHLQSILV AEKITQKVEG QLSKSQKEFL LRQQMRAIKE ELGDNDDDED
     DVAALERKMQ NAGMPANIWK HAQRELRRLR KMQPQQPGYS SSRTYLELLA ELPWQKVSEE
     RELDLRAAKE SLDRDHYGLT KVKQRIIEYL AVRKLKPDAR GPVLCFVGPP GVGKTSLASS
     IAKALNRKFI RISLGGVKDE ADIRGHRRTY IGSMPGRLID GLKRVSVSNP VMLLDEIDKT
     GSDVRGDPAS ALLEVLDPEQ NKTFNDHYLN VPFDLSKVIF VATANRMQPI PPPLLDRMEV
     IELPGYTPEE KLKIAMKHLI PRVLEQHGLS STYLQIPEAM VRLIIERYTR EAGVRNLERN
     LAALARAAAV KVAEQDSALR LGKEIQPITT TLLDSRLADG GEVEMEVIPM GQDISNTYEN
     PSPMIVDEAM LEKVLGPPRF DDSEAADRVA SPGVSVGLVW TSFGGEVQFV EATAMVGKGD
     LHLTGQLGDV IKESAQLALT WVRARAADLN LSPTSDINLL ESRDIHIHFP AGAVPKDGPS
     AGVTLVTSLV SLFSHRKVRA DTAMTGEMTL RGLVLPVGGV KDKVLAAHRY GIKRVILPER
     NMKDLAEVPA PILSGLEILL VKRIEEVLDH AFEGGCPLRP HSKL