PPBI_MOUSE
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 03-AUG-2022, entry version 142.
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}.
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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 GlyGen; P24822; 3 sites.
DR iPTMnet; P24822; -.
DR PhosphoSitePlus; P24822; -.
DR MaxQB; P24822; -.
DR PaxDb; P24822; -.
DR PeptideAtlas; P24822; -.
DR PRIDE; P24822; -.
DR ProteomicsDB; 291780; -.
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:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
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:0006793; P:phosphorus metabolic process; ISO:MGI.
DR GO; GO:0036342; P:post-anal tail morphogenesis; IMP:MGI.
DR CDD; cd16012; ALP; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR001952; Alkaline_phosphatase.
DR InterPro; IPR018299; Alkaline_phosphatase_AS.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR PANTHER; PTHR11596; PTHR11596; 1.
DR Pfam; PF00245; Alk_phosphatase; 1.
DR PRINTS; PR00113; ALKPHPHTASE.
DR SMART; SM00098; alkPPc; 1.
DR SUPFAM; SSF53649; SSF53649; 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
