Detail Information for IndEnz0002016752
IED ID IndEnz0002016752
Enzyme Type ID protease016752
Protein Name Cytosol aminopeptidase
EC 3.4.11.1
Cysteinylglycine-S-conjugate dipeptidase
EC 3.4.13.23
Leucine aminopeptidase 3
LAP-3
Leucyl aminopeptidase
Peptidase S
Proline aminopeptidase
EC 3.4.11.5
Prolyl aminopeptidase
Gene Name Lap3 Lapep
Organism Mus musculus (Mouse)
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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MYLLPLPAAARVALRRLGVRGLWDRGLSTADMTKGLVLGIYAKDKDDDLPQFTSAGESFNKLVSGKLREMLNISGPPLKAGKTRTFYGLHQDFPSVVVVGLGKRSAGVDDQENWHEGKENIRAAVAAGCRQVQDLELPSVEVDPCGDAQAAAEGAVLGLYEYDDLKQKKKVAVSAKLHGSGDLEAWEKGVLFASGQNLARHLMESPANEMTPTRFAEIIEKNLKSASSKTKVHIRPKSWIEEQEMGSFLSVAKGSEEPPVFLEIHYMGSPNATEAPLVFVGKGITFDSGGISIKASANMDLMRADMGGAATICSAIVSAAKLNLPINIIGLAPLCENMPSGKANKPGDVVRARNGKTIQVDNTDAEGRLILADALCYAHTFNPKVIINAATLTGAMDVALGSGATGVFTNSSWLWNKLFEASVETGDRVWRMPLFEHYTRQVIDCQLADVNNLGKYRSAGACTAAAFLREFVTHTKWAHLDIAGVMTNKDEIPYLRKGMSGRPTRTLIEFLLRFSKDSS
Enzyme Length 519
Uniprot Accession Number Q9CPY7
Absorption
Active Site ACT_SITE 294; /evidence=ECO:0000250|UniProtKB:P00727; ACT_SITE 368; /evidence=ECO:0000250|UniProtKB:P00727
Activity Regulation
Binding Site BINDING 282; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00727; BINDING 287; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00727; BINDING 292; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00727; BINDING 294; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00727; BINDING 305; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00727; BINDING 364; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00727
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.; EC=3.4.11.1; Evidence={ECO:0000250|UniProtKB:P00727}; CATALYTIC ACTIVITY: Reaction=an S-substituted L-cysteinylglycine + H2O = an S-substituted L-cysteine + glycine; Xref=Rhea:RHEA:60444, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305, ChEBI:CHEBI:58717, ChEBI:CHEBI:143103; EC=3.4.13.23; Evidence={ECO:0000250|UniProtKB:P00727};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60445; Evidence={ECO:0000250|UniProtKB:P00727}; CATALYTIC ACTIVITY: Reaction=H2O + L-cysteinylglycine = glycine + L-cysteine; Xref=Rhea:RHEA:28783, ChEBI:CHEBI:15377, ChEBI:CHEBI:35235, ChEBI:CHEBI:57305, ChEBI:CHEBI:61694; Evidence={ECO:0000250|UniProtKB:P00727};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28784; Evidence={ECO:0000250|UniProtKB:P00727}; CATALYTIC ACTIVITY: Reaction=H2O + S-benzyl-L-cysteinylglycine = glycine + S-benzyl-L-cysteine; Xref=Rhea:RHEA:62568, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305, ChEBI:CHEBI:145802, ChEBI:CHEBI:145803; Evidence={ECO:0000250|UniProtKB:Q68FS4};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62569; Evidence={ECO:0000250|UniProtKB:Q68FS4}; CATALYTIC ACTIVITY: Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5; Evidence={ECO:0000250|UniProtKB:P28839};
DNA Binding
EC Number 3.4.11.1; 3.4.13.23; 3.4.11.5
Enzyme Function FUNCTION: Cytosolic metallopeptidase that catalyzes the removal of unsubstituted N-terminal hydrophobic amino acids from various peptides. The presence of Zn(2+) ions is essential for the peptidase activity, and the association with other cofactors can modulate the substrate spectificity of the enzyme. For instance, in the presence of Mn(2+), it displays a specific Cys-Gly hydrolyzing activity of Cys-Gly-S-conjugates. Involved in the metabolism of glutathione and in the degradation of glutathione S-conjugates, which may play a role in the control of the cell redox status. {ECO:0000250|UniProtKB:P00727}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Alternative sequence (1); Binding site (6); Chain (1); Erroneous initiation (5); Metal binding (13); Modified residue (14); Sequence conflict (3)
Keywords Acetylation;Alternative initiation;Aminopeptidase;Cytoplasm;Direct protein sequencing;Hydrolase;Magnesium;Manganese;Metal-binding;Phosphoprotein;Protease;Reference proteome;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q68FS4}.
Modified Residue MOD_RES 45; /note="N6-succinyllysine"; /evidence="ECO:0007744|PubMed:23806337"; MOD_RES 54; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q68FS4"; MOD_RES 61; /note="N6-succinyllysine"; /evidence="ECO:0007744|PubMed:23806337"; MOD_RES 103; /note="N6-succinyllysine"; /evidence="ECO:0007744|PubMed:23806337"; MOD_RES 180; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"; MOD_RES 194; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P28838"; MOD_RES 221; /note="N6-acetyllysine; alternate"; /evidence="ECO:0007744|PubMed:23576753"; MOD_RES 221; /note="N6-succinyllysine; alternate"; /evidence="ECO:0007744|PubMed:23806337"; MOD_RES 238; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 455; /note="N6-acetyllysine; alternate"; /evidence="ECO:0007744|PubMed:23576753"; MOD_RES 455; /note="N6-succinyllysine; alternate"; /evidence="ECO:0007744|PubMed:23806337"; MOD_RES 476; /note="N6-succinyllysine"; /evidence="ECO:0007744|PubMed:23806337"; MOD_RES 489; /note="N6-acetyllysine; alternate"; /evidence="ECO:0007744|PubMed:23576753"; MOD_RES 489; /note="N6-succinyllysine; alternate"; /evidence="ECO:0007744|PubMed:23806337"
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11217851; 12466851; 12520002; 12904583; 14559211; 14610273; 14651853; 14681479; 16272315; 16615898; 17513741; 18614015; 1914521; 19455133; 19474315; 21267068; 6228526; 662012; 6626149; 752543;
Motif
Gene Encoded By
Mass 56,141
Kinetics
Metal Binding METAL 202; /note=Zinc 3; via carbonyl oxygen; structural; /evidence=ECO:0000250|UniProtKB:P00727; METAL 203; /note=Zinc 3; via carbonyl oxygen; structural; /evidence=ECO:0000250|UniProtKB:P00727; METAL 282; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P00727; METAL 287; /note=Magnesium; catalytic; /evidence=ECO:0000250|UniProtKB:P00727; METAL 287; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P00727; METAL 287; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P00727; METAL 303; /note=Zinc 3; via carbonyl oxygen; structural; /evidence=ECO:0000250|UniProtKB:P00727; METAL 305; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P00727; METAL 364; /note=Magnesium; catalytic; /evidence=ECO:0000250|UniProtKB:P00727; METAL 364; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P00727; METAL 366; /note=Magnesium; catalytic; /evidence=ECO:0000250|UniProtKB:P00727; METAL 366; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P00727; METAL 366; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P00727
Rhea ID RHEA:60444; RHEA:60445; RHEA:28783; RHEA:28784; RHEA:62568; RHEA:62569
Cross Reference Brenda