ID PPBI_BOVIN Reviewed; 533 AA. AC P19111; Q28124; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 02-SEP-2026, entry version 154. DE RecName: Full=Intestinal-type alkaline phosphatase; DE Short=IAP; DE Short=Intestinal alkaline phosphatase; DE EC=3.1.3.1; DE Flags: Precursor; GN Name=ALPI; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Liver; RX PubMed=8452539; DOI=10.1042/bj2900503; RA Weissig H., Schildge A., Hoylaerts M.F., Iqbal M., Millan J.L.; RT "Cloning and expression of the bovine intestinal alkaline phosphatase gene: RT biochemical characterization of the recombinant enzyme."; RL Biochem. J. 290:503-508(1993). RN [2] RP PROTEIN SEQUENCE OF 20-35 AND 91-152, AND ACTIVE SITE. RC TISSUE=Intestine; RX PubMed=3902089; DOI=10.1016/0167-4838(85)90115-3; RA Culp J.S., Hermodson M., Butler L.G.; RT "The active-site and amino-terminal amino acid sequence of bovine RT intestinal alkaline phosphatase."; RL Biochim. Biophys. Acta 831:330-334(1985). RN [3] RP PROTEIN SEQUENCE OF 20-63. RX PubMed=3458202; DOI=10.1073/pnas.83.8.2368; RA Hua J.-C., Berger J., Pan Y.C.E., Hulmes J.D., Udenfriend S.; RT "Partial sequencing of human adult, human fetal, and bovine intestinal RT alkaline phosphatases: comparison with the human placental and liver RT isozymes."; RL Proc. Natl. Acad. Sci. U.S.A. 83:2368-2372(1986). CC -!- FUNCTION: Alkaline phosphatase that can hydrolyze various phosphate CC compounds. {ECO:0000250|UniProtKB:P15693}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate; CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; CC Evidence={ECO:0000250|UniProtKB:P15693, ECO:0000255|PROSITE- CC ProRule:PRU10042}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P15693}; CC Note=Binds 1 Mg(2+) ion. {ECO:0000250|UniProtKB:P15693}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000250|UniProtKB:P15693}; CC Note=Binds 2 Zn(2+) ions. {ECO:0000250|UniProtKB:P15693}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000250|UniProtKB:P05186}; CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P15693}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15693}; CC Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P15693}. CC -!- MISCELLANEOUS: In most mammals there are four different isozymes: CC placental (ALPP), germ cell (ALPG), intestinal (ALPI) and tissue non- CC specific (liver/bone/kidney) (ALPL/TNAP). CC -!- SIMILARITY: Belongs to the alkaline phosphatase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L07733; AAA30571.1; -; Genomic_DNA. DR PIR; S30364; S30364. DR AlphaFoldDB; P19111; -. DR SMR; P19111; -. DR FunCoup; P19111; 28. DR IntAct; P19111; 2. DR MINT; P19111; -. DR STRING; 9913.ENSBTAP00000005937; -. DR BindingDB; P19111; -. DR ChEMBL; CHEMBL5695; -. DR DrugCentral; P19111; -. DR GlyCosmos; P19111; 2 sites, No reported glycans. DR GlyGen; P19111; 2 sites. DR PaxDb; 9913-ENSBTAP00000005937; -. DR eggNOG; KOG4126; Eukaryota. DR InParanoid; P19111; -. DR BRENDA; 3.1.3.1; 908. DR SABIO-RK; P19111; -. DR STRENDA-DB; Y9CBQW; Alkaline phosphatase. DR Proteomes; UP000009136; Unplaced. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0004035; F:alkaline phosphatase activity; ISS:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB. DR GO; GO:0016311; P:dephosphorylation; ISS:UniProtKB. DR CDD; cd16012; ALP; 1. DR FunFam; 3.40.720.10:FF:000008; Alkaline phosphatase; 1. DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1. DR InterPro; IPR001952; Alkaline_phosphatase. DR InterPro; IPR018299; Alkaline_phosphatase_AS. DR InterPro; IPR017850; Alkaline_phosphatase_core_sf. DR PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1. DR PANTHER; PTHR11596:SF30; INTESTINAL-TYPE ALKALINE PHOSPHATASE; 1. DR Pfam; PF00245; Alk_phosphatase; 1. DR PRINTS; PR00113; ALKPHPHTASE. DR SMART; SM00098; alkPPc; 1. DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1. DR PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1. PE 1: Evidence at protein level; KW Calcium; Cell membrane; Direct protein sequencing; Disulfide bond; KW Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Magnesium; Membrane; KW Metal-binding; Reference proteome; Signal; Zinc. FT SIGNAL 1..19 FT /evidence="ECO:0000269|PubMed:3458202, FT ECO:0000269|PubMed:3902089" FT CHAIN 20..506 FT /note="Intestinal-type alkaline phosphatase" FT /id="PRO_0000024035" FT PROPEP 507..533 FT /note="Removed in mature form" FT /evidence="ECO:0000255" FT /id="PRO_0000024036" FT ACT_SITE 111 FT /note="Phosphoserine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10042, FT ECO:0000269|PubMed:3902089" FT BINDING 61 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P15693" FT BINDING 61 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P15693" FT BINDING 111 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P15693" FT BINDING 174 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P15693" FT BINDING 235 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P05186" FT BINDING 288 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P05186" FT BINDING 289 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P05186" FT BINDING 304 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P05186" FT BINDING 330 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P15693" FT BINDING 335 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P15693" FT BINDING 339 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P15693" FT BINDING 376 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P15693" FT BINDING 377 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P15693" FT BINDING 451 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P15693" FT LIPID 506 FT /note="GPI-anchor amidated aspartate" FT /evidence="ECO:0000255" FT CARBOHYD 268 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 429 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 140..202 FT /evidence="ECO:0000250|UniProtKB:P15693" FT DISULFID 486..493 FT /evidence="ECO:0000250|UniProtKB:P15693" FT CONFLICT 148..150 FT /note="VTS -> TSV (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 533 AA; 57100 MW; D74456F3F1F06714 CRC64; MQGACVLLLL GLHLQLSLGL VPVEEEDPAF WNRQAAQALD VAKKLQPIQT AAKNVILFLG DGMGVPTVTA TRILKGQMNG KLGPETPLAM DQFPYVALSK TYNVDRQVPD SAGTATAYLC GVKGNYRTIG VSAAARYNQC KTTRGNEVTS VMNRAKKAGK SVGVVTTTRV QHASPAGAYA HTVNRNWYSD ADLPADAQMN GCQDIAAQLV NNMDIDVILG GGRKYMFPVG TPDPEYPDDA SVNGVRKRKQ NLVQAWQAKH QGAQYVWNRT ALLQAADDSS VTHLMGLFEP ADMKYNVQQD HTKDPTLQEM TEVALRVVSR NPRGFYLFVE GGRIDHGHHD DKAYMALTEA GMFDNAIAKA NELTSELDTL ILVTADHSHV FSFGGYTLRG TSIFGLAPSK ALDSKSYTSI LYGNGPGYAL GGGSRPDVND STSEDPSYQQ QAAVPQASET HGGEDVAVFA RGPQAHLVHG VEEETFVAHI MAFAGCVEPY TDCNLPAPTT ATSIPDAAHL AASPPPLALL AGAMLLLLAP TLY //