| IED ID | IndEnz0002010509 |
| Enzyme Type ID | protease010509 |
| Protein Name |
Alkaline phosphatase, germ cell type EC 3.1.3.1 Alkaline phosphatase 5 Alkaline phosphatase, placental-like Embryonic alkaline phosphatase EAP Embryonic-type alkaline phosphatase |
| Gene Name | Alpg Akp5 Alppl2 Eap |
| 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 | MWGACLLLLGLSLQVCPSVIPVEEENPAFWNRKAAEALDAAKKLKPIQTSAKNLVILMGDGMGVSTVTATRILKGQQQGHLGPETQLAMDRFPHMALSKTYNTDKQIPDSAGTGTAFLCGVKTNMKVIGLSAAARFNQCNTTWGNEVVSVMHRAKKAGKSVGVVTTTSVQHASPAGTYAHTVNRGWYSDAQMPASALQDGCKDISTQLISNMDIDVILGGGRKFMFPKGTPDQEYPTDTKQAGTRLDGRNLVQEWLAKHQGARYVWNRSELIQASLNRSVTHLMGLFEPNDMKYEIHRDPAQDPSLAEMTEVAVRMLSRNPKGFYLFVEGGRIDHGHHETVAYRALTEAVMFDSAVDKADKLTSEQDTMILVTADHSHVFSFGGYTQRGASIFGLAPFKAEDGKSFTSILYGNGPGYKLHNGARADVTEEESSNPTYQQQAAVPLSSETHSGEDVAIFARGPQAHLVHGVQEQNYIAHVMAFAACLEPYTDCGLASPAGQSSAVSPGYMSTLLCLLAGKMLMLMAAAEP |
| Enzyme Length | 529 |
| Uniprot Accession Number | P24823 |
| Absorption | |
| Active Site | ACT_SITE 110; /note=Phosphoserine intermediate |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by L-leucine, EDTA and heat. {ECO:0000250|UniProtKB:P10696}. |
| 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=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042}; |
| DNA Binding | |
| EC Number | 3.1.3.1 |
| Enzyme Function | FUNCTION: Alkaline phosphatase that can hydrolyze various phosphate compounds. {ECO:0000250|UniProtKB:P10696}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (2); Glycosylation (3); Lipidation (1); Metal binding (14); Propeptide (1); Sequence conflict (3); Signal peptide (1) |
| Keywords | Calcium;Cell membrane;Disulfide bond;GPI-anchor;Glycoprotein;Hydrolase;Lipoprotein;Magnesium;Membrane;Metal-binding;Reference proteome;Signal;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10725249; 10767088; 10878613; 14681479; 16537572; 17901166; 19531352; 2133555; 22675556; 26902285; 31289197; 9061447; 9291464; |
| Motif | |
| Gene Encoded By | |
| Mass | 57,202 |
| Kinetics | |
| Metal Binding | METAL 60; /note=Magnesium; /evidence=ECO:0000250|UniProtKB:P05187; METAL 60; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:P05187; METAL 110; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:P05187; METAL 173; /note=Magnesium; /evidence=ECO:0000250|UniProtKB:P05187; METAL 234; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P05186; METAL 287; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P05186; METAL 288; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P05186; METAL 303; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P05186; METAL 329; /note=Magnesium; /evidence=ECO:0000250|UniProtKB:P05187; METAL 334; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:P05187; METAL 338; /note=Zinc 2; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:P05187; METAL 375; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:P05187; METAL 376; /note=Zinc 1; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:P05187; METAL 450; /note=Zinc 2; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:P05187 |
| Rhea ID | RHEA:15017 |
| Cross Reference Brenda |