PPBI2_RAT
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 03-AUG-2022, entry version 137.
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.ENSRNOP00000066949; -.
DR GlyGen; P51740; 4 sites.
DR PaxDb; P51740; -.
DR PRIDE; P51740; -.
DR UCSC; RGD:621650; rat.
DR eggNOG; KOG4126; Eukaryota.
DR PhylomeDB; P51740; -.
DR SABIO-RK; P51740; -.
DR Proteomes; UP000002494; 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; 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; -; 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: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
