ID   PPBI2_RAT               Reviewed;         551 AA.
AC   P51740;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   24-JAN-2024, entry version 144.
DE   RecName: Full=Intestinal-type alkaline phosphatase 2;
DE            Short=IAP-2;
DE            Short=Intestinal alkaline phosphatase 2;
DE            EC=3.1.3.1;
DE   AltName: Full=Intestinal alkaline phosphatase II;
DE            Short=IAP-II;
DE   Flags: Precursor;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1954251; DOI=10.1016/0167-4781(91)90193-p;
RA   Strom M., Krisinger J., Deluca H.F.;
RT   "Isolation of a mRNA that encodes a putative intestinal alkaline
RT   phosphatase regulated by 1,25-dihydroxyvitamin D-3.";
RL   Biochim. Biophys. Acta 1090:299-304(1991).
RN   [2]
RP   PARTIAL NUCLEOTIDE SEQUENCE.
RC   STRAIN=Sprague-Dawley;
RX   PubMed=1458592;
RA   Engle M.J., Aleprs D.H.;
RT   "The two mRNAs encoding rat intestinal alkaline phosphatase represent two
RT   distinct nucleotide sequences.";
RL   Clin. Chem. 38:2506-2509(1992).
RN   [3]
RP   PROTEIN SEQUENCE OF 20-29, AND VARIANT VAL-29.
RX   PubMed=1654110; DOI=10.1016/0304-4165(91)90077-t;
RA   Yang W.-J., Matsuda Y., Sano S., Masutani H., Nakagawa H.;
RT   "Purification and characterization of phytase from rat intestinal mucosa.";
RL   Biochim. Biophys. Acta 1075:75-82(1991).
RN   [4]
RP   GPI-ANCHOR.
RX   PubMed=7744844; DOI=10.1074/jbc.270.20.11935;
RA   Engle M.J., Mahmood A., Alpers D.H.;
RT   "Two rat intestinal alkaline phosphatase isoforms with different carboxyl-
RT   terminal peptides are both membrane-bound by a glycan phosphatidylinositol
RT   linkage.";
RL   J. Biol. Chem. 270:11935-11940(1995).
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:0000269|PubMed:7744844}.
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). Rat has two genes for the
CC       intestinal isozyme.
CC   -!- SIMILARITY: Belongs to the alkaline phosphatase family. {ECO:0000305}.
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DR   EMBL; S66545; AAB20378.2; -; mRNA.
DR   PIR; B56888; B56888.
DR   PIR; S18408; S18408.
DR   AlphaFoldDB; P51740; -.
DR   SMR; P51740; -.
DR   STRING; 10116.ENSRNOP00000071091; -.
DR   GlyGen; P51740; 4 sites.
DR   PhosphoSitePlus; P51740; -.
DR   PaxDb; 10116-ENSRNOP00000066949; -.
DR   UCSC; RGD:621650; rat.
DR   AGR; RGD:621650; -.
DR   eggNOG; KOG4126; Eukaryota.
DR   InParanoid; P51740; -.
DR   PhylomeDB; P51740; -.
DR   SABIO-RK; P51740; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004035; F:alkaline phosphatase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
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   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:1654110"
FT   CHAIN           20..531
FT                   /note="Intestinal-type alkaline phosphatase 2"
FT                   /id="PRO_0000024043"
FT   PROPEP          532..551
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000024044"
FT   REGION          496..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        502..537
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   LIPID           531
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   CARBOHYD        509
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"
FT   VARIANT         29
FT                   /note="A -> V"
FT                   /evidence="ECO:0000269|PubMed:1654110"
SQ   SEQUENCE   551 AA;  59797 MW;  486206A5A9A11C3B CRC64;
     MQGAWVLLLL GFRLQLSLSV IPVEEENPAF WTQKAADALN VAKKLQPIQT SAKNLIIFLG
     DGMGVATVTA TRILKGQLEG NLGPETPLAM DHFPYMALSK TYSVDRQVPD SASTATAYLC
     GVKTNYKTIG VSAAARFDQC NTTFGNEVLS VMYRAKKAGK SVGVGDHTRV QHASPAGTYV
     HTVTSNWYGD ADMPALPLQE GCKDIATQLI SNMDINVILG GGRKYMFPAG TPDPEYPNDV
     NETGTRLDGK NLVQEWLSKH QGSQYVWNRQ ELIQKSLDPS VTYLMGLFEP VDTKFEIQRD
     PLMDPSLKDM TEAALHVLSR NPKGFYLFVE GGRIDRGHHL GTAYLALTEA VMFDSAIERA
     SLQASEQDTL TIVTADHSHV FSFGGYTLRG TSIFGLAPLN ALDGKPYTSI LYGNGPGYVG
     TGERPNVTDA ESHDPSYQQQ AAVPVKSETT VGKDVAIFAR GPQAHLLHGV QEQNYIAHVM
     AFAGCLEPYT DCGLAPPADE NRPTTPVQNS TTTTTTTTTT TTTTTTTRVQ NSASSLGPAT
     APLAWHYWPR R
//