PPBI_BOVIN
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 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 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}.
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DR EMBL; L07733; AAA30571.1; -; Genomic_DNA.
DR PIR; S30364; S30364.
DR AlphaFoldDB; P19111; -.
DR SMR; P19111; -.
DR IntAct; P19111; 2.
DR MINT; P19111; -.
DR STRING; 9913.ENSBTAP00000005937; -.
DR BindingDB; P19111; -.
DR ChEMBL; CHEMBL5695; -.
DR DrugCentral; P19111; -.
DR PaxDb; P19111; -.
DR eggNOG; KOG4126; Eukaryota.
DR InParanoid; P19111; -.
DR BRENDA; 3.1.3.1; 908.
DR SABIO-RK; P19111; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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 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 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
