ID LONP2_MAIZE Reviewed; 885 AA. AC P93647; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 02-SEP-2026, entry version 159. 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=LON1; OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade; OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea. OX NCBI_TaxID=4577; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. B73; RX PubMed=9620272; DOI=10.1023/a:1005912831051; RA Barakat S., Pearce D.A., Sherman F., Rapp W.D.; RT "Maize contains a Lon protease gene that can partially complement a yeast RT pim1-deletion mutant."; RL Plant Mol. Biol. 37:141-154(1998). 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U85494; AAC50011.1; -; mRNA. DR PIR; T04321; T04321. DR RefSeq; NP_001105903.1; NM_001112433.2. DR AlphaFoldDB; P93647; -. DR SMR; P93647; -. DR FunCoup; P93647; 678. DR STRING; 4577.P93647; -. DR MEROPS; S16.003; -. DR PaxDb; 4577-P93647; -. DR EnsemblPlants; Zm00001eb319680_T001; Zm00001eb319680_P001; Zm00001eb319680. DR GeneID; 732820; -. DR Gramene; Zm00001eb319680_T001; Zm00001eb319680_P001; Zm00001eb319680. DR KEGG; zma:732820; -. DR eggNOG; KOG2004; Eukaryota. DR HOGENOM; CLU_004109_4_0_1; -. DR InParanoid; P93647; -. DR OrthoDB; 2411602at2759; -. DR BRENDA; 3.6.4.7; 6752. DR Proteomes; UP000007305; Chromosome 7. DR ExpressionAtlas; P93647; baseline and differential. DR GO; GO:0005739; C:mitochondrion; IEA:GOC. 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:0008233; F:peptidase activity; IBA:GO_Central. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0032042; P:mitochondrial DNA metabolic process; IDA:AgBase. 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:0009408; P:response to heat; IDA:AgBase. DR CDD; cd19500; RecA-like_Lon; 1. DR FunFam; 1.20.5.5270:FF:000002; Lon protease homolog; 1. DR FunFam; 1.10.8.60:FF:000095; Lon protease homolog 2, peroxisomal; 1. DR FunFam; 1.20.58.1480:FF:000005; Lon protease homolog 2, peroxisomal; 1. DR FunFam; 3.30.230.10:FF:000019; Lon protease homolog 2, peroxisomal; 1. DR FunFam; 3.40.50.300:FF:000651; Lon protease homolog 2, peroxisomal; 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; IPR054594; Lon_lid. 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 Pfam; PF00004; AAA; 1. DR Pfam; PF05362; Lon_C; 1. DR Pfam; PF22667; Lon_lid; 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..885 FT /note="Lon protease homolog 2, peroxisomal" FT /id="PRO_0000026737" FT DOMAIN 12..256 FT /note="Lon N-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123" FT DOMAIN 690..875 FT /note="Lon proteolytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122" FT REGION 70..104 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 883..885 FT /note="Microbody targeting signal" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121" FT COMPBIAS 77..86 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 94..104 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 781 FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121" FT ACT_SITE 824 FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121" FT BINDING 409..416 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121" SQ SEQUENCE 885 AA; 97733 MW; 331A321B56C75407 CRC64; MSDSPVELPS RLAVLPFRNK VLLPGAIVRI RCTNPSSVKL VEQELWQKEE KGLIGVLPVR DSEATAVGSL LSPGVGSDSG EGGSKVGGSA VESSKQDTKN GKEPIHWHSK GVAARALHLS RGVEKPSGRV TYIVVLEGLC RFSVQELSAR GPYHVARVSR LDMTKTELEQ AEQDPDLIAL SRQFKATAME LISVLEQKQK TVGRTKVLLD TVPVYRLADI FVASFEISFE EQLSMLDSVH LKVRLSKATE LVDRHLQSIL VAEKITQKVE GQLSKSQKEF LLRQQMRAIK EELGDNDDDE DDVAALERKM QNAGMPANIW KHAQREMRRL RKMQPQQPGY SSSRAYLELL ADLPWQKVSE ERELDLRVAK ESLDQDHYGL TKVKQRIIEY LAVRKLKPDA RGPVLCFVGP PGVGKTSLAS SIAKALNRKF IRISLGGVKD EADIRGHRRT YIGSMPGRLI DGLKRVSVSN PVMLLDEIDK TGSDVRGDPA SALLEVLDPE QNKAFNDHYL NVPFDLSKVI FVATANRMQP IPPPLLDRME IIELPGYTPE EKLKIAMKHL IPRVLEQHGL STTNLQIPEA MVKLVIERYT REAGVRNLER NLAALARAAA VKVAEQVKTL RLGKEIQPIT TTLLDSRLAD GGEVEMEVIP MEHDISNTYE NPSPMIVDEA MLEKVLGPPR FDDREAADRV ASPGVSVGLV WTSVGGEVQF VEATAMVGKG DLHLTGQLGD VIKESAQLAL TWVRARAADL NLSPTSDINL LESRDIHIHF PAGAVPKDGP SAGVTLVTAL VSLFSNRKVR ADTAMTGEMT LRGLVLPVGG VKDKVLAAHR YGIKRVILPE RNLKDLSEVP LPILSDMEIL LVKRIEEVLD HAFEGRCPLR SRSKL //