Detail Information for IndEnz0002014385
IED ID IndEnz0002014385
Enzyme Type ID protease014385
Protein Name Cysteine protease atg-4.2
EC 3.4.22.-
Autophagy-related protein 4 homolog 2
Gene Name atg-4.2 ZK792.8
Organism Caenorhabditis elegans
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans
Enzyme Sequence MNNIPDDFKKIASSSRLPRKYCSSESSLSDDDGHEIEHVLKHGAPEEALTPDTERMVVLGQDVVQSAPASLVPGGNLSWMSKIKSAGASMMGSIRPSSSSQDVHSTGEIEKHSKKKWKARLWSTWNNIKYSSTWMSDRSDEYGGENDVVFLGRRYSTSVDESGLRSGFENFCSDYYSRLWITYRTDFPALLDTDTTTDCGWGCMIRTTQMMVAQAIMVNRFGRDWRFTRRKRSHVAAHGDEDDFDREKIQEWMILKLFEDKPTAPLGIHKMVGIAAMGKGKKAVGSWYSPSEAVFIMKKALTESSSPLTGNTAMLLSIDGRVHIRDIEVETKNWMKKLILVIVVRLGAAELNPIYVPHLMRLFAMESCLGITGGRPDHSSWFVGYYGDQIIYLDPHVAHEYIPIDINPNTNVVDSDSKKAKKCPEKSYHCRLLSKMHFFDMDPSCALCFQFESREQFDNDMRQLNLSQFIDIDQGEEHGMKRVRDPMFSVVYGERRQPPSYEREVSETEQAQADKHGFEML
Enzyme Length 521
Uniprot Accession Number Q9U1N6
Absorption
Active Site ACT_SITE 203; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:Q9Y4P1; ACT_SITE 394; /evidence=ECO:0000250|UniProtKB:Q9Y4P1; ACT_SITE 396; /evidence=ECO:0000250|UniProtKB:Q9Y4P1
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=[protein]-C-terminal L-amino acid-glycyl-phosphatidylethanolamide + H2O = [protein]-C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:67548, Rhea:RHEA-COMP:17323, Rhea:RHEA-COMP:17324, ChEBI:CHEBI:15377, ChEBI:CHEBI:64612, ChEBI:CHEBI:172940, ChEBI:CHEBI:172941; Evidence={ECO:0000250|UniProtKB:Q9Y4P1};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67549; Evidence={ECO:0000250|UniProtKB:Q9Y4P1};
DNA Binding
EC Number 3.4.22.-
Enzyme Function FUNCTION: Cysteine protease required for autophagy (PubMed:22767594, PubMed:30880001). Cleaves the C-terminal amino acid of ATG8 family proteins lgg-1, to reveal a C-terminal glycine (Probable). Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy (Probable). Its cleavage activity is functionally redundant to atg-4.1, but it cleaves lgg-1 precursors less efficiently than atg-4.1 (Probable). In contrast to atg-4.1, plays a more significant role in the later phases of autophagy and in addition has a role in autophagosome maturation (PubMed:30880001). Acts redundantly with atg-4.1 to promote the lgg-1 delipidation to release the protein from membranes, which facilitates multiple events during macroautophagy (PubMed:30880001). Regulates the accumulation of autophagic structures in neurons and is specifically, required for the maturation and elimination of autophagosomes from the synaptic region of AIY interneurons (PubMed:30880001). {ECO:0000269|PubMed:22767594, ECO:0000269|PubMed:30880001, ECO:0000305|PubMed:22767594}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Mutagenesis (3); Region (2)
Keywords Autophagy;Cytoplasm;Hydrolase;Protease;Protein transport;Reference proteome;Thiol protease;Transport
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|RuleBase:RU363115, ECO:0000269|PubMed:30880001}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10778742; 12097347; 17164286; 19343510; 20439776; 21177967; 21367940; 22267497; 22286215; 22347378; 22560298; 23549480; 23800452; 24165672; 24884423; 25487147; 27294288; 31291815; 6593563;
Motif
Gene Encoded By
Mass 59,276
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20.7 uM for lgg-1 {ECO:0000269|PubMed:22767594};
Metal Binding
Rhea ID RHEA:67548; RHEA:67549
Cross Reference Brenda