Detail Information for IndEnz0002004668
IED ID IndEnz0002004668
Enzyme Type ID protease004668
Protein Name Lon protease homolog 2, peroxisomal
EC 3.4.21.53
Lon protease-like protein 2
Lon protease 2
Peroxisomal Lon protease
pLon
Gene Name LONP2 LONP
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MSSVSPIQIPSRLPLLLTHEGVLLPGSTMRTSVDSARNLQLVRSRLLKGTSLQSTILGVIPNTPDPASDAQDLPPLHRIGTAALAVQVVGSNWPKPHYTLLITGLCRFQIVQVLKEKPYPIAEVEQLDRLEEFPNTCKMREELGELSEQFYKYAVQLVEMLDMSVPAVAKLRRLLDSLPREALPDILTSIIRTSNKEKLQILDAVSLEERFKMTIPLLVRQIEGLKLLQKTRKPKQDDDKRVIAIRPIRRITHISGTLEDEDEDEDNDDIVMLEKKIRTSSMPEQAHKVCVKEIKRLKKMPQSMPEYALTRNYLELMVELPWNKSTTDRLDIRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATANTTATIPAALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLEQHGLTPQQIQIPQVTTLDIITRYTREAGVRSLDRKLGAICRAVAVKVAEGQHKEAKLDRSDVTEREGCREHILEDEKPESISDTTDLALPPEMPILIDFHALKDILGPPMYEMEVSQRLSQPGVAIGLAWTPLGGEIMFVEASRMDGEGQLTLTGQLGDVMKESAHLAISWLRSNAKKYQLTNAFGSFDLLDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRAGLKQVIIPRRNEKDLEGIPGNVRQDLSFVTASCLDEVLNAAFDGGFTVKTRPGLLNSKL
Enzyme Length 852
Uniprot Accession Number Q86WA8
Absorption
Active Site ACT_SITE 743; /evidence=ECO:0000255|HAMAP-Rule:MF_03121; ACT_SITE 786; /evidence=ECO:0000255|HAMAP-Rule:MF_03121
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53; Evidence={ECO:0000255|HAMAP-Rule:MF_03121};
DNA Binding
EC Number 3.4.21.53
Enzyme Function FUNCTION: ATP-dependent serine protease that mediates the selective degradation of misfolded and unassembled polypeptides in the peroxisomal matrix. Necessary for type 2 peroxisome targeting signal (PTS2)-containing protein processing and facilitates peroxisome matrix protein import (By similarity). May indirectly regulate peroxisomal fatty acid beta-oxidation through degradation of the self-processed forms of TYSND1. {ECO:0000255|HAMAP-Rule:MF_03121, ECO:0000269|PubMed:22002062}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 375..382; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_03121
Features Active site (2); Alternative sequence (1); Chain (1); Domain (2); Erroneous initiation (1); Initiator methionine (1); Modified residue (1); Motif (1); Mutagenesis (2); Nucleotide binding (1); Sequence conflict (2)
Keywords ATP-binding;Acetylation;Alternative splicing;Hydrolase;Nucleotide-binding;Peroxisome;Protease;Reference proteome;Serine protease
Interact With Q9H1X1; Q8N0S2
Induction
Subcellular Location SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000255|HAMAP-Rule:MF_03121, ECO:0000269|PubMed:14561759, ECO:0000269|PubMed:18281296, ECO:0000269|PubMed:22002062}.
Modified Residue MOD_RES 2; /note=N-acetylserine; /evidence=ECO:0007744|PubMed:22814378
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10022913; 11101887; 12456682; 12502735; 12559034; 12578380; 12885776; 17007944; 18712838; 19011634; 19197237; 19584060; 19615732; 19632994; 20178365; 20562859; 21098288; 21976670; 21995946; 22747494; 23747015; 23963456; 24235149; 24756126; 25342745; 25467444; 25854684; 26220973; 28765278; 28787099; 7719337; 7790377; 8824437; 8858165; 9653144; 9668159; 9819444; 9837948;
Motif MOTIF 850..852; /note=Microbody targeting signal; /evidence=ECO:0000255|HAMAP-Rule:MF_03121
Gene Encoded By
Mass 94,617
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda