Detail Information for IndEnz0002010056
IED ID IndEnz0002010056
Enzyme Type ID protease010056
Protein Name Intestinal-type alkaline phosphatase
IAP
Intestinal alkaline phosphatase
EC 3.1.3.1
Gene Name ALPI
Organism Homo sapiens (Human)
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MQGPWVLLLLGLRLQLSLGVIPAEEENPAFWNRQAAEALDAAKKLQPIQKVAKNLILFLGDGLGVPTVTATRILKGQKNGKLGPETPLAMDRFPYLALSKTYNVDRQVPDSAATATAYLCGVKANFQTIGLSAAARFNQCNTTRGNEVISVMNRAKQAGKSVGVVTTTRVQHASPAGTYAHTVNRNWYSDADMPASARQEGCQDIATQLISNMDIDVILGGGRKYMFPMGTPDPEYPADASQNGIRLDGKNLVQEWLAKHQGAWYVWNRTELMQASLDQSVTHLMGLFEPGDTKYEIHRDPTLDPSLMEMTEAALRLLSRNPRGFYLFVEGGRIDHGHHEGVAYQALTEAVMFDDAIERAGQLTSEEDTLTLVTADHSHVFSFGGYTLRGSSIFGLAPSKAQDSKAYTSILYGNGPGYVFNSGVRPDVNESESGSPDYQQQAAVPLSSETHGGEDVAVFARGPQAHLVHGVQEQSFVAHVMAFAACLEPYTACDLAPPACTTDAAHPVAASLPLLAGTLLLLGASAAP
Enzyme Length 528
Uniprot Accession Number P09923
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); Disulfide bond (2); Glycosylation (3); Lipidation (1); Metal binding (14); Natural variant (2); Propeptide (1); Sequence conflict (3); Signal peptide (1)
Keywords Calcium;Cell membrane;Direct protein sequencing;Disulfide bond;GPI-anchor;Glycoprotein;Hydrolase;Lipoprotein;Magnesium;Membrane;Metal-binding;Reference proteome;Signal;Zinc
Interact With P60410; P60411; Q7Z3S9
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:0000269|PubMed:1458595, ECO:0000269|PubMed:3458202"
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11072085; 12372831; 12919939; 14595869; 15143152; 15715171; 15774940; 15831710; 17353931; 17498884; 18292227; 18307834; 19407215; 19570815; 20489044; 22157815; 22262031; 22333159; 22783049; 24019514; 24043717; 24247025; 24296104; 2443973; 24856042; 24966474; 25037223; 25277244; 25409280; 25416956; 25609649; 25906119; 26299896; 26496610; 26844282; 26988336; 27083970; 27106638; 27384524; 27865621; 28931466; 29970708; 30417313; 31915470; 32472757; 32728117; 32906115; 32918806; 32934082; 33391458; 3422494; 34831233;
Motif
Gene Encoded By
Mass 56,812
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 451; /note=Zinc 2; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:P15693
Rhea ID RHEA:15017
Cross Reference Brenda