Detail Information for IndEnz0002012948
IED ID IndEnz0002012948
Enzyme Type ID protease012948
Protein Name Intestinal-type alkaline phosphatase
IAP
Intestinal alkaline phosphatase
EC 3.1.3.1
Alkaline phosphatase 3
Gene Name Iap Akp-3 Akp3
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 MQGPWVLLLLGLRLQLSLSVIPVEEENPAFWNKKAAEALDAAKKLQPIQTSAKNLIIFLGDGMGVPTVTATRILKGQLEGHLGPETPLAMDRFPYMALSKTYSVDRQVPDSASTATAYLCGVKTNYKTIGLSAAARFDQCNTTFGNEVFSVMYRAKKAGKSVGVVTTTRVQHASPSGTYVHTVNRNWYGDADMPASALREGCKDIATQLISNMDINVILGGGRKYMFPAGTPDPEYPNDANETGTRLDGRNLVQEWLSKHQGSQYVWNREQLIQKAQDPSVTYLMGLFEPVDTKFDIQRDPLMDPSLKDMTETAVKVLSRNPKGFYLFVEGGRIDRGHHLGTAYLALTEAVMFDLAIERASQLTSERDTLTIVTADHSHVFSFGGYTLRGTSIFGLAPLNALDGKPYTSILYGNGPGYVGTGERPNVTAAESSGSSYRRQAAVPVKSETHGGEDVAIFARGPQAHLVHGVQEQNYIAHVMASAGCLEPYTDCGLAPPADESQTTTTTRQTTITTTTTTTTTTTTPVHNSARSLGPATAPLALALLAGMLMLLLGAPAES
Enzyme Length 559
Uniprot Accession Number P24822
Absorption
Active Site ACT_SITE 111; /note=Phosphoserine intermediate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10042
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=3.1.3.1; Evidence={ECO:0000250|UniProtKB:P15693, 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:P15693}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Compositional bias (1); Disulfide bond (2); Glycosylation (3); Lipidation (1); Metal binding (14); Propeptide (1); Region (1); 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 {ECO:0000250|UniProtKB:P15693}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P15693}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..19; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10878613; 11015594; 1358796; 14560000; 14681479; 15745951; 1611911; 16537572; 1676979; 1682057; 17332477; 17901166; 18292227; 2045114; 20844955; 21267068; 2133555; 22114352; 23306083; 23322734; 23569246; 24722905; 25348635; 2566635; 2575484; 28167773; 30064292; 30212831; 30308156; 32213701; 33391458; 6626138; 7533563; 7698765; 8188220; 9061447; 9107685; 9291464; 9486188;
Motif
Gene Encoded By
Mass 60,285
Kinetics
Metal Binding METAL 61; /note=Magnesium; /evidence=ECO:0000250|UniProtKB:P15693; METAL 61; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:P15693; METAL 111; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:P15693; METAL 174; /note=Magnesium; /evidence=ECO:0000250|UniProtKB:P15693; METAL 235; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P05186; METAL 288; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P05186; METAL 289; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P05186; METAL 304; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P05186; METAL 330; /note=Magnesium; /evidence=ECO:0000250|UniProtKB:P15693; METAL 335; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:P15693; METAL 339; /note=Zinc 2; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:P15693; METAL 376; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:P15693; METAL 377; /note=Zinc 1; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:P15693; METAL 450; /note=Zinc 2; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:P15693
Rhea ID RHEA:15017
Cross Reference Brenda 3.1.3.1;