ID PPBI_MOUSE Reviewed; 559 AA. AC P24822; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-1992, sequence version 1. DT 08-NOV-2023, entry version 146. DE RecName: Full=Intestinal-type alkaline phosphatase; DE Short=IAP; DE Short=Intestinal alkaline phosphatase; DE EC=3.1.3.1; DE AltName: Full=Alkaline phosphatase 3; DE Flags: Precursor; GN Name=Iap; Synonyms=Akp-3, Akp3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY. RX PubMed=2286375; DOI=10.1016/0888-7543(90)90042-s; RA Manes T., Glade K., Ziomek C.A., Millan J.L.; RT "Genomic structure and comparison of mouse tissue-specific alkaline RT phosphatase genes."; RL Genomics 8:541-554(1990). 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 -!- TISSUE SPECIFICITY: Intestine and thymus. {ECO:0000269|PubMed:2286375}. 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; M61705; AAA37873.1; -; Genomic_DNA. DR CCDS; CCDS15127.1; -. DR PIR; B36307; B36307. DR AlphaFoldDB; P24822; -. DR SMR; P24822; -. DR STRING; 10090.ENSMUSP00000037497; -. DR BindingDB; P24822; -. DR ChEMBL; CHEMBL3151; -. DR GlyCosmos; P24822; 3 sites, No reported glycans. DR GlyGen; P24822; 3 sites. DR iPTMnet; P24822; -. DR PhosphoSitePlus; P24822; -. DR MaxQB; P24822; -. DR PaxDb; 10090-ENSMUSP00000037497; -. DR PeptideAtlas; P24822; -. DR ProteomicsDB; 291780; -. DR AGR; MGI:87984; -. DR MGI; MGI:87984; Akp3. DR eggNOG; KOG4126; Eukaryota. DR InParanoid; P24822; -. DR PhylomeDB; P24822; -. DR BRENDA; 3.1.3.1; 3474. DR Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins. DR Reactome; R-MMU-6811438; Intra-Golgi traffic. DR PRO; PR:P24822; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; P24822; Protein. DR GO; GO:0005903; C:brush border; IDA:UniProtKB. DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0004035; F:alkaline phosphatase activity; ISS:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB. DR GO; GO:0002020; F:protease binding; ISO:MGI. DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB. DR GO; GO:0016311; P:dephosphorylation; ISS:UniProtKB. DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI. DR GO; GO:0021915; P:neural tube development; IMP:MGI. DR GO; GO:0022008; P:neurogenesis; IMP:MGI. DR GO; GO:0036342; P:post-anal tail morphogenesis; IMP:MGI. DR CDD; cd16012; ALP; 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:SF43; 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 2: Evidence at transcript level; KW Calcium; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; KW Hydrolase; Lipoprotein; Magnesium; Membrane; Metal-binding; KW Reference proteome; Signal; Zinc. FT SIGNAL 1..19 FT /evidence="ECO:0000255" FT CHAIN 20..528 FT /note="Intestinal-type alkaline phosphatase" FT /id="PRO_0000024039" FT PROPEP 529..559 FT /note="Removed in mature form" FT /evidence="ECO:0000255" FT /id="PRO_0000024040" FT REGION 496..531 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 497..531 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 111 FT /note="Phosphoserine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10042" 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 450 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P15693" FT LIPID 528 FT /note="GPI-anchor amidated asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 141 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 241 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 426 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 140..202 FT /evidence="ECO:0000250|UniProtKB:P15693" FT DISULFID 485..492 FT /evidence="ECO:0000250|UniProtKB:P15693" SQ SEQUENCE 559 AA; 60285 MW; 019EBB4363950878 CRC64; MQGPWVLLLL GLRLQLSLSV IPVEEENPAF WNKKAAEALD AAKKLQPIQT SAKNLIIFLG DGMGVPTVTA TRILKGQLEG HLGPETPLAM DRFPYMALSK TYSVDRQVPD SASTATAYLC GVKTNYKTIG LSAAARFDQC NTTFGNEVFS VMYRAKKAGK SVGVVTTTRV QHASPSGTYV HTVNRNWYGD ADMPASALRE GCKDIATQLI SNMDINVILG GGRKYMFPAG TPDPEYPNDA NETGTRLDGR NLVQEWLSKH QGSQYVWNRE QLIQKAQDPS VTYLMGLFEP VDTKFDIQRD PLMDPSLKDM TETAVKVLSR NPKGFYLFVE GGRIDRGHHL GTAYLALTEA VMFDLAIERA SQLTSERDTL TIVTADHSHV FSFGGYTLRG TSIFGLAPLN ALDGKPYTSI LYGNGPGYVG TGERPNVTAA ESSGSSYRRQ AAVPVKSETH GGEDVAIFAR GPQAHLVHGV QEQNYIAHVM ASAGCLEPYT DCGLAPPADE SQTTTTTRQT TITTTTTTTT TTTTPVHNSA RSLGPATAPL ALALLAGMLM LLLGAPAES //