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Intestinal-type alkaline phosphatase 1 (IAP-1) (Intestinal alkaline phosphatase 1) (EC 3.1.3.1) (Intestinal alkaline phosphatase I) (IAP-I)

 PPBI1_RAT               Reviewed;         540 AA.
P15693;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
30-AUG-2017, entry version 129.
RecName: Full=Intestinal-type alkaline phosphatase 1;
Short=IAP-1;
Short=Intestinal alkaline phosphatase 1;
EC=3.1.3.1;
AltName: Full=Intestinal alkaline phosphatase I;
Short=IAP-I;
Flags: Precursor;
Name=Alpi;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-34 AND 287-300,
CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
PubMed=2155025; DOI=10.1016/0167-4838(90)90164-B;
Lowe M., Strauss A.W., Alpers R., Seetharam S., Alpers D.H.;
"Molecular cloning and expression of a cDNA encoding the membrane-
associated rat intestinal alkaline phosphatase.";
Biochim. Biophys. Acta 1037:170-177(1990).
[2]
GPI-ANCHOR.
PubMed=7744844; DOI=10.1074/jbc.270.20.11935;
Engle M.J., Mahmood A., Alpers D.H.;
"Two rat intestinal alkaline phosphatase isoforms with different
carboxyl-terminal peptides are both membrane-bound by a glycan
phosphatidylinositol linkage.";
J. Biol. Chem. 270:11935-11940(1995).
[3]
X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 21-502 IN COMPLEX WITH
MAGNESIUM AND ZINC, GLYCOSYLATION AT ASN-301 AND ASN-428, DISULFIDE
BOND, COFACTOR, CATALYTIC ACTIVITY, SUBUNIT, AND ACTIVE SITE.
PubMed=24076154; DOI=10.1016/j.jsb.2013.09.017;
Ghosh K., Mazumder Tagore D., Anumula R., Lakshmaiah B., Kumar P.P.,
Singaram S., Matan T., Kallipatti S., Selvam S., Krishnamurthy P.,
Ramarao M.;
"Crystal structure of rat intestinal alkaline phosphatase - Role of
crown domain in mammalian alkaline phosphatases.";
J. Struct. Biol. 184:182-192(2013).
-!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
phosphate. {ECO:0000255|PROSITE-ProRule:PRU10042,
ECO:0000269|PubMed:2155025, ECO:0000269|PubMed:24076154}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:24076154};
Note=Binds 1 Mg(2+) ion. {ECO:0000269|PubMed:24076154};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:24076154};
Note=Binds 2 Zn(2+) ions. {ECO:0000269|PubMed:24076154};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24076154}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2155025};
Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:2155025}.
-!- MISCELLANEOUS: In most mammals there are four different isozymes:
placental, placental-like, intestinal and tissue non-specific
(liver/bone/kidney). Rat has two genes for the intestinal isozyme.
-!- SIMILARITY: Belongs to the alkaline phosphatase family.
{ECO:0000305}.
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EMBL; X17611; CAA35613.1; -; mRNA.
PIR; S08214; S08214.
UniGene; Rn.48774; -.
PDB; 4KJD; X-ray; 2.21 A; A/B=21-502.
PDB; 4KJG; X-ray; 2.38 A; A/B=21-502.
PDBsum; 4KJD; -.
PDBsum; 4KJG; -.
ProteinModelPortal; P15693; -.
SMR; P15693; -.
STRING; 10116.ENSRNOP00000026190; -.
BindingDB; P15693; -.
PaxDb; P15693; -.
PRIDE; P15693; -.
UCSC; RGD:2099; rat.
RGD; 2099; Alpi.
eggNOG; KOG4126; Eukaryota.
eggNOG; COG1785; LUCA.
HOGENOM; HOG000099118; -.
HOVERGEN; HBG007345; -.
InParanoid; P15693; -.
PhylomeDB; P15693; -.
SABIO-RK; P15693; -.
PRO; PR:P15693; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0009897; C:external side of plasma membrane; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0004035; F:alkaline phosphatase activity; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
GO; GO:0006793; P:phosphorus metabolic process; IDA:RGD.
CDD; cd16012; ALP; 1.
Gene3D; 3.40.720.10; -; 1.
InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
InterPro; IPR001952; Alkaline_phosphatase.
InterPro; IPR018299; Alkaline_phosphatase_AS.
InterPro; IPR017850; Alkaline_phosphatase_core.
PANTHER; PTHR11596; PTHR11596; 1.
Pfam; PF00245; Alk_phosphatase; 1.
PRINTS; PR00113; ALKPHPHTASE.
SMART; SM00098; alkPPc; 1.
SUPFAM; SSF53649; SSF53649; 1.
PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor;
Hydrolase; Lipoprotein; Magnesium; Membrane; Metal-binding;
Reference proteome; Signal; Transmembrane; Zinc.
SIGNAL 1 20 {ECO:0000269|PubMed:2155025}.
CHAIN 21 511 Intestinal-type alkaline phosphatase 1.
/FTId=PRO_0000024041.
PROPEP 512 540 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000024042.
ACT_SITE 112 112 Phosphoserine intermediate.
{ECO:0000255|PROSITE-ProRule:PRU10042,
ECO:0000269|PubMed:24076154}.
METAL 62 62 Magnesium. {ECO:0000269|PubMed:24076154}.
METAL 62 62 Zinc 1. {ECO:0000269|PubMed:24076154}.
METAL 112 112 Zinc 1. {ECO:0000269|PubMed:24076154}.
METAL 175 175 Magnesium. {ECO:0000269|PubMed:24076154}.
METAL 331 331 Magnesium. {ECO:0000269|PubMed:24076154}.
METAL 336 336 Zinc 2. {ECO:0000269|PubMed:24076154}.
METAL 340 340 Zinc 2; via tele nitrogen.
{ECO:0000269|PubMed:24076154}.
METAL 377 377 Zinc 1. {ECO:0000269|PubMed:24076154}.
METAL 378 378 Zinc 1; via tele nitrogen.
{ECO:0000269|PubMed:24076154}.
METAL 452 452 Zinc 2; via tele nitrogen.
{ECO:0000269|PubMed:24076154}.
LIPID 511 511 GPI-anchor amidated asparagine.
{ECO:0000255}.
CARBOHYD 142 142 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 301 301 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:24076154}.
CARBOHYD 428 428 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:24076154}.
DISULFID 141 203 {ECO:0000269|PubMed:24076154}.
DISULFID 487 494 {ECO:0000269|PubMed:24076154}.
HELIX 25 27 {ECO:0000244|PDB:4KJD}.
HELIX 29 45 {ECO:0000244|PDB:4KJD}.
STRAND 54 61 {ECO:0000244|PDB:4KJD}.
HELIX 66 79 {ECO:0000244|PDB:4KJD}.
HELIX 91 93 {ECO:0000244|PDB:4KJD}.
STRAND 95 101 {ECO:0000244|PDB:4KJD}.
STRAND 105 109 {ECO:0000244|PDB:4KJD}.
HELIX 112 121 {ECO:0000244|PDB:4KJD}.
STRAND 130 132 {ECO:0000244|PDB:4KJD}.
HELIX 141 144 {ECO:0000244|PDB:4KJD}.
HELIX 152 158 {ECO:0000244|PDB:4KJD}.
STRAND 162 170 {ECO:0000244|PDB:4KJD}.
HELIX 174 177 {ECO:0000244|PDB:4KJD}.
TURN 178 180 {ECO:0000244|PDB:4KJD}.
HELIX 191 193 {ECO:0000244|PDB:4KJD}.
HELIX 196 200 {ECO:0000244|PDB:4KJD}.
HELIX 206 212 {ECO:0000244|PDB:4KJD}.
STRAND 217 222 {ECO:0000244|PDB:4KJD}.
HELIX 224 227 {ECO:0000244|PDB:4KJD}.
HELIX 241 243 {ECO:0000244|PDB:4KJD}.
STRAND 247 249 {ECO:0000244|PDB:4KJD}.
HELIX 253 258 {ECO:0000244|PDB:4KJD}.
STRAND 264 267 {ECO:0000244|PDB:4KJD}.
HELIX 270 278 {ECO:0000244|PDB:4KJD}.
STRAND 284 288 {ECO:0000244|PDB:4KJD}.
STRAND 290 293 {ECO:0000244|PDB:4KJD}.
HELIX 297 299 {ECO:0000244|PDB:4KJD}.
TURN 302 304 {ECO:0000244|PDB:4KJD}.
HELIX 308 319 {ECO:0000244|PDB:4KJD}.
STRAND 326 332 {ECO:0000244|PDB:4KJD}.
HELIX 335 338 {ECO:0000244|PDB:4KJD}.
HELIX 344 364 {ECO:0000244|PDB:4KJD}.
TURN 367 369 {ECO:0000244|PDB:4KJD}.
STRAND 370 378 {ECO:0000244|PDB:4KJD}.
STRAND 379 384 {ECO:0000244|PDB:4KJG}.
STRAND 409 416 {ECO:0000244|PDB:4KJG}.
HELIX 431 434 {ECO:0000244|PDB:4KJG}.
STRAND 443 446 {ECO:0000244|PDB:4KJG}.
STRAND 457 463 {ECO:0000244|PDB:4KJD}.
HELIX 466 468 {ECO:0000244|PDB:4KJD}.
STRAND 471 474 {ECO:0000244|PDB:4KJD}.
HELIX 477 485 {ECO:0000244|PDB:4KJD}.
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


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