Detail Information for IndEnz0002011889
IED ID IndEnz0002011889
Enzyme Type ID protease011889
Protein Name Peroxisomal leader peptide-processing protease
EC 3.4.21.-
Trypsin domain-containing protein 1

Cleaved into: Peroxisomal leader peptide-processing protease, 15 kDa form; Peroxisomal leader peptide-processing protease, 45 kDa form
Gene Name TYSND1
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 MRRQWGSAMRAAEQAGCMVSASRAGQPEAGPWSCSGVILSRSPGLVLCHGGIFVPFLRAGSEVLTAAGAVFLPGDSCRDDLRLHVQWAPTAAGPGGGAERGRPGLCTPQCASLEPGPPAPSRGRPLQPRLPAELLLLLSCPAFWAHFARLFGDEAAEQWRFSSAARDDEVSEDEEADQLRALGWFALLGVRLGQEEVEEERGPAMAVSPLGAVPKGAPLLVCGSPFGAFCPDIFLNTLSCGVLSNVAGPLLLTDARCLPGTEGGGVFTARPAGALVALVVAPLCWKAGEWVGFTLLCAAAPLFRAARDALHRLPHSTAALAALLPPEVGVPWGLPLRDSGPLWAAAAVLVECGTVWGSGVAVAPRLVVTCRHVSPREAARVLVRSTTPKSVAIWGRVVFATQETCPYDIAVVSLEEDLDDVPIPVPAEHFHEGEAVSVVGFGVFGQSCGPSVTSGILSAVVQVNGTPVMLQTTCAVHSGSSGGPLFSNHSGNLLGIITSNTRDNNTGATYPHLNFSIPITVLQPALQQYSQTQDLGGLRELDRAAEPVRVVWRLQRPLAEAPRSKL
Enzyme Length 566
Uniprot Accession Number Q2T9J0
Absorption
Active Site ACT_SITE 372; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 408; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 481; /note=Charge relay system; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.21.-
Enzyme Function FUNCTION: Peroxisomal protease that mediates both the removal of the leader peptide from proteins containing a PTS2 target sequence and processes several PTS1-containing proteins. Catalyzes the processing of PTS1-proteins involved in the peroxisomal beta-oxidation of fatty acids. {ECO:0000269|PubMed:22002062}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Alternative sequence (2); Chain (3); Mutagenesis (1); Natural variant (1); Region (1); Sequence conflict (1); Site (1)
Keywords Alternative splicing;Hydrolase;Peroxisome;Protease;Reference proteome;Serine protease
Interact With Itself
Induction
Subcellular Location SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:22002062}.
Modified Residue
Post Translational Modification PTM: Self-cleavage gives rise to an N-terminal 15-kDa fragment and C-terminal 45-kDa fragment upon import into the peroxisomes. The full-lengh TYSND1 is the active the proteolytic processing of PTS1- and PTS2-proteins and in self-cleavage, and intermolecular self-cleavage of TYSND1 down-regulates its protease activity.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10022913; 11101887; 12456682; 12559034; 12578380; 12885776; 16385451; 16766224; 17007944; 17255948; 18712838; 19197237; 19584060; 19615732; 19632994; 20178365; 20379614; 21976670; 22190034; 22747494; 23459139; 23963456; 24235149; 25854684; 26220973; 28765278; 28787099; 7719337; 7790377; 8824437; 8858165; 9089413; 9653144; 9668159; 9837948;
Motif
Gene Encoded By
Mass 59,309
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda