PPBI1_RAT
ID PPBI1_RAT Reviewed; 540 AA.
AC P15693;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Intestinal-type alkaline phosphatase 1;
DE Short=IAP-1;
DE Short=Intestinal alkaline phosphatase 1;
DE EC=3.1.3.1;
DE AltName: Full=Intestinal alkaline phosphatase I;
DE Short=IAP-I;
DE Flags: Precursor;
GN Name=Alpi;
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], PROTEIN SEQUENCE OF 21-34 AND 287-300,
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=2155025; DOI=10.1016/0167-4838(90)90164-b;
RA Lowe M., Strauss A.W., Alpers R., Seetharam S., Alpers D.H.;
RT "Molecular cloning and expression of a cDNA encoding the membrane-
RT associated rat intestinal alkaline phosphatase.";
RL Biochim. Biophys. Acta 1037:170-177(1990).
RN [2]
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 21-502 IN COMPLEX WITH MAGNESIUM
RP AND ZINC, GLYCOSYLATION AT ASN-301 AND ASN-428, DISULFIDE BOND, COFACTOR,
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND ACTIVE SITE.
RX PubMed=24076154; DOI=10.1016/j.jsb.2013.09.017;
RA Ghosh K., Mazumder Tagore D., Anumula R., Lakshmaiah B., Kumar P.P.,
RA Singaram S., Matan T., Kallipatti S., Selvam S., Krishnamurthy P.,
RA Ramarao M.;
RT "Crystal structure of rat intestinal alkaline phosphatase - Role of crown
RT domain in mammalian alkaline phosphatases.";
RL J. Struct. Biol. 184:182-192(2013).
CC -!- FUNCTION: Alkaline phosphatase that can hydrolyze various phosphate
CC compounds. {ECO:0000269|PubMed:2155025, ECO:0000269|PubMed:24076154}.
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:0000255|PROSITE-ProRule:PRU10042,
CC ECO:0000269|PubMed:2155025, ECO:0000269|PubMed:24076154};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:24076154};
CC Note=Binds 1 Mg(2+) ion. {ECO:0000269|PubMed:24076154};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:24076154};
CC Note=Binds 2 Zn(2+) ions. {ECO:0000269|PubMed:24076154};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P05186};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24076154}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2155025};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:2155025}.
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; X17611; CAA35613.1; -; mRNA.
DR PIR; S08214; S08214.
DR PDB; 4KJD; X-ray; 2.21 A; A/B=21-502.
DR PDB; 4KJG; X-ray; 2.38 A; A/B=21-502.
DR PDBsum; 4KJD; -.
DR PDBsum; 4KJG; -.
DR AlphaFoldDB; P15693; -.
DR SMR; P15693; -.
DR STRING; 10116.ENSRNOP00000026190; -.
DR BindingDB; P15693; -.
DR GlyGen; P15693; 3 sites.
DR iPTMnet; P15693; -.
DR PaxDb; P15693; -.
DR PRIDE; P15693; -.
DR UCSC; RGD:2099; rat.
DR RGD; 2099; Alpi.
DR eggNOG; KOG4126; Eukaryota.
DR InParanoid; P15693; -.
DR PhylomeDB; P15693; -.
DR Reactome; R-RNO-1483166; Synthesis of PA.
DR Reactome; R-RNO-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR Reactome; R-RNO-6811438; Intra-Golgi traffic.
DR Reactome; R-RNO-8935690; Digestion.
DR SABIO-RK; P15693; -.
DR PRO; PR:P15693; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004035; F:alkaline phosphatase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0002020; F:protease binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0071773; P:cellular response to BMP stimulus; ISO:RGD.
DR GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
DR GO; GO:0006793; P:phosphorus metabolic process; IDA:RGD.
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 3D-structure; Calcium; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein;
KW Magnesium; Membrane; Metal-binding; Reference proteome; Signal; Zinc.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:2155025"
FT CHAIN 21..511
FT /note="Intestinal-type alkaline phosphatase 1"
FT /id="PRO_0000024041"
FT PROPEP 512..540
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000024042"
FT ACT_SITE 112
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10042,
FT ECO:0000269|PubMed:24076154"
FT BINDING 62
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24076154"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24076154"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24076154"
FT BINDING 175
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24076154"
FT BINDING 236
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 290
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P05186"
FT BINDING 305
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P05186"
FT BINDING 331
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24076154"
FT BINDING 336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24076154"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24076154"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24076154"
FT BINDING 378
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24076154"
FT BINDING 452
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24076154"
FT LIPID 511
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24076154"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24076154"
FT DISULFID 141..203
FT /evidence="ECO:0000269|PubMed:24076154"
FT DISULFID 487..494
FT /evidence="ECO:0000269|PubMed:24076154"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:4KJD"
FT HELIX 29..45
FT /evidence="ECO:0007829|PDB:4KJD"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:4KJD"
FT HELIX 66..79
FT /evidence="ECO:0007829|PDB:4KJD"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:4KJD"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:4KJD"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:4KJD"
FT HELIX 112..121
FT /evidence="ECO:0007829|PDB:4KJD"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:4KJD"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:4KJD"
FT HELIX 152..158
FT /evidence="ECO:0007829|PDB:4KJD"
FT STRAND 162..170
FT /evidence="ECO:0007829|PDB:4KJD"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:4KJD"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:4KJD"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:4KJD"
FT HELIX 196..200
FT /evidence="ECO:0007829|PDB:4KJD"
FT HELIX 206..212
FT /evidence="ECO:0007829|PDB:4KJD"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:4KJD"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:4KJD"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:4KJD"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:4KJD"
FT HELIX 253..258
FT /evidence="ECO:0007829|PDB:4KJD"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:4KJD"
FT HELIX 270..278
FT /evidence="ECO:0007829|PDB:4KJD"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:4KJD"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:4KJD"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:4KJD"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:4KJD"
FT HELIX 308..319
FT /evidence="ECO:0007829|PDB:4KJD"
FT STRAND 326..332
FT /evidence="ECO:0007829|PDB:4KJD"
FT HELIX 335..338
FT /evidence="ECO:0007829|PDB:4KJD"
FT HELIX 344..364
FT /evidence="ECO:0007829|PDB:4KJD"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:4KJD"
FT STRAND 370..378
FT /evidence="ECO:0007829|PDB:4KJD"
FT STRAND 379..384
FT /evidence="ECO:0007829|PDB:4KJG"
FT STRAND 409..416
FT /evidence="ECO:0007829|PDB:4KJG"
FT HELIX 431..434
FT /evidence="ECO:0007829|PDB:4KJG"
FT STRAND 443..446
FT /evidence="ECO:0007829|PDB:4KJG"
FT STRAND 457..463
FT /evidence="ECO:0007829|PDB:4KJD"
FT HELIX 466..468
FT /evidence="ECO:0007829|PDB:4KJD"
FT STRAND 471..474
FT /evidence="ECO:0007829|PDB:4KJD"
FT HELIX 477..485
FT /evidence="ECO:0007829|PDB:4KJD"
SQ SEQUENCE 540 AA; 58402 MW; 29AC2B543CBE6B52 CRC64;
MQGDWVLLLL LGLRIHLSFG VIPVEEENPV FWNQKAKEAL DVAKKLQPIQ TSAKNLILFL
GDGMGVPTVT ATRILKGQLG GHLGPETPLA MDHFPFTALS KTYNVDRQVP DSAGTATAYL
CGVKANYKTI GVSAAARFNQ CNSTFGNEVF SVMHRAKKAG KSVGVVTTTR VQHASPAGTY
AHTVNRDWYS DADMPSSALQ EGCKDIATQL ISNMDIDVIL GGGRKFMFPK GTPDPEYPGD
SDQSGVRLDS RNLVEEWLAK YQGTRYVWNR EQLMQASQDP AVTRLMGLFE PTEMKYDVNR
NASADPSLAE MTEVAVRLLS RNPQGFYLFV EGGRIDQGHH AGTAYLALTE AVMFDSAIEK
ASQLTNEKDT LTLITADHSH VFAFGGYTLR GTSIFGLAPL NAQDGKSYTS ILYGNGPGYV
LNSGNRPNVT DAESGDVNYK QQAAVPLSSE THGGEDVAIF ARGPQAHLVH GVQEQNYIAH
VMAFAGCLEP YTDCGLAPPA DENRPTTPVQ NSAITMNNVL LSLQLLVSML LLVGTALVVS
