Detail Information for IndEnz0002010381
IED ID IndEnz0002010381
Enzyme Type ID protease010381
Protein Name Lysosomal acid phosphatase
LAP
EC 3.1.3.2
Gene Name acp2
Organism Xenopus laevis (African clawed frog)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Pipoidea Pipidae Xenopodinae Xenopus Xenopus Xenopus laevis (African clawed frog)
Enzyme Sequence MADGSCLGSGPQLGLIALLVVLLFSAVPLAQSRELRFVTLVYRHGDRSPVHGYPTDVHKESVWPQGYGQLTQVGMKQHWDLGQELRARYKGFLNESYNRHEIYVRSTDVDRTLMSAEANLAGLYPPEGPQIFNPNITWQPIPIHTIPESEDQLLKFPISPCPAYVKLQEETRQSAEYINMTTTYKAFLQMVANKTGLSDCTLESVWSVYDTLFCEKTHNFSLPTWATADVLSKLNKLKDFSFVFLFGVHERVKKARLQGGVLVDQILKNMTAAANNASNGLKLLAYSAHDSTLGALQLALDVYNGKQAPYASCHIFELYKEDSGNFTVQMYFRNESGKTPYPVSLPGCAHACPLQDFQSLLQPILAQDWEEECQTTSFIMTEETIIGLTIGAIALFIIIVVLMLLSCNEPKDDGYQHVSDEGDDHETKGLAM
Enzyme Length 432
Uniprot Accession Number B1H1P9
Absorption
Active Site ACT_SITE 44; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 290; /note=Proton donor; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
DNA Binding
EC Number 3.1.3.2
Enzyme Function
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Disulfide bond (3); Glycosylation (7); Signal peptide (1); Topological domain (2); Transmembrane (1)
Keywords Disulfide bond;Glycoprotein;Hydrolase;Lysosome;Membrane;Signal;Transmembrane;Transmembrane helix
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:P11117}; Single-pass membrane protein {ECO:0000255}; Lumenal side {ECO:0000250|UniProtKB:P11117}. Lysosome lumen {ECO:0000250|UniProtKB:P11117}. Note=The soluble form arises by proteolytic processing of the membrane-bound form. {ECO:0000250|UniProtKB:P11117}.
Modified Residue
Post Translational Modification PTM: The membrane-bound form is converted to the soluble form by sequential proteolytic processing. First, the C-terminal cytoplasmic tail is removed. Cleavage by a lysosomal protease releases the soluble form in the lysosome lumen (By similarity). {ECO:0000250}.
Signal Peptide SIGNAL 1..32; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 48,243
Kinetics
Metal Binding
Rhea ID RHEA:15017
Cross Reference Brenda