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

 PPBI_HUMAN              Reviewed;         528 AA.
P09923; B2R7Y4; Q53S80; Q9UBV5; Q9UCL2;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 2.
27-SEP-2017, entry version 178.
RecName: Full=Intestinal-type alkaline phosphatase;
Short=IAP;
Short=Intestinal alkaline phosphatase;
EC=3.1.3.1;
Flags: Precursor;
Name=ALPI;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=3468508; DOI=10.1073/pnas.84.3.695;
Berger J., Garattini E., Hua J.-C., Udenfriend S.;
"Cloning and sequencing of human intestinal alkaline phosphatase
cDNA.";
Proc. Natl. Acad. Sci. U.S.A. 84:695-698(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3469665; DOI=10.1073/pnas.84.5.1234;
Henthorn P.S., Raducha M., Edwards Y.H., Weiss M.J., Slaughter C.,
Lafferty M.A., Harris H.;
"Nucleotide and amino acid sequences of human intestinal alkaline
phosphatase: close homology to placental alkaline phosphatase.";
Proc. Natl. Acad. Sci. U.S.A. 84:1234-1238(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2841341;
Henthorn P.S., Raducha M., Kadesch T., Weiss M.J., Harris H.;
"Sequence and characterization of the human intestinal alkaline
phosphatase gene.";
J. Biol. Chem. 263:12011-12019(1988).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100.
PubMed=3697102; DOI=10.1093/nar/15.24.10599;
Millan J.L.;
"Promoter structure of the human intestinal alkaline phosphatase
gene.";
Nucleic Acids Res. 15:10599-10599(1987).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-73.
PubMed=3443302; DOI=10.1016/0378-1119(87)90235-6;
Knoll B.J., Rothblum K.N., Longley M.;
"Two gene duplication events in the evolution of the human heat-stable
alkaline phosphatases.";
Gene 60:267-276(1987).
[10]
PROTEIN SEQUENCE OF 20-58.
PubMed=3458202; DOI=10.1073/pnas.83.8.2368;
Hua J.-C., Berger J., Pan Y.C.E., Hulmes J.D., Udenfriend S.;
"Partial sequencing of human adult, human fetal, and bovine intestinal
alkaline phosphatases: comparison with the human placental and liver
isozymes.";
Proc. Natl. Acad. Sci. U.S.A. 83:2368-2372(1986).
[11]
PROTEIN SEQUENCE OF 20-49.
PubMed=1458595;
Nishihara Y., Hayashi Y., Adachi T., Koyama I., Stigbrand T.,
Hirano K.;
"Chemical nature of intestinal-type alkaline phosphatase in human
kidney.";
Clin. Chem. 38:2539-2542(1992).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
-!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
phosphate. {ECO:0000255|PROSITE-ProRule:PRU10042}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 1 Mg(2+) ion. {ECO:0000250};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 2 Zn(2+) ions. {ECO:0000250};
-!- SUBUNIT: Homodimer.
-!- INTERACTION:
P60410:KRTAP10-8; NbExp=3; IntAct=EBI-1052631, EBI-10171774;
P60411:KRTAP10-9; NbExp=3; IntAct=EBI-1052631, EBI-10172052;
Q7Z3S9:NOTCH2NL; NbExp=3; IntAct=EBI-1052631, EBI-945833;
-!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
-!- MISCELLANEOUS: In most mammals there are four different isozymes:
placental, placental-like, intestinal and tissue non-specific
(liver/bone/kidney).
-!- SIMILARITY: Belongs to the alkaline phosphatase family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Alkaline phosphatase entry;
URL="https://en.wikipedia.org/wiki/Alkaline_phosphatase";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M15694; AAA51703.1; -; mRNA.
EMBL; M31008; AAA51704.1; -; mRNA.
EMBL; J03930; AAA98617.1; -; Genomic_DNA.
EMBL; AK313163; BAG35981.1; -; mRNA.
EMBL; AC068134; AAY24089.1; -; Genomic_DNA.
EMBL; CH471063; EAW70997.1; -; Genomic_DNA.
EMBL; BC132678; AAI32679.1; -; mRNA.
EMBL; Y00512; CAA68564.1; -; Genomic_DNA.
EMBL; M19161; AAA51705.1; -; Genomic_DNA.
CCDS; CCDS2492.1; -.
PIR; A31073; PAHUI.
RefSeq; NP_001622.2; NM_001631.4.
UniGene; Hs.284255; -.
UniGene; Hs.37009; -.
ProteinModelPortal; P09923; -.
SMR; P09923; -.
BioGrid; 106749; 18.
IntAct; P09923; 9.
MINT; MINT-2800762; -.
STRING; 9606.ENSP00000295463; -.
BindingDB; P09923; -.
ChEMBL; CHEMBL5573; -.
DEPOD; P09923; -.
iPTMnet; P09923; -.
PhosphoSitePlus; P09923; -.
UniCarbKB; P09923; -.
BioMuta; ALPI; -.
DMDM; 130744; -.
EPD; P09923; -.
MaxQB; P09923; -.
PaxDb; P09923; -.
PeptideAtlas; P09923; -.
PRIDE; P09923; -.
Ensembl; ENST00000295463; ENSP00000295463; ENSG00000163295.
GeneID; 248; -.
KEGG; hsa:248; -.
UCSC; uc002vst.4; human.
CTD; 248; -.
DisGeNET; 248; -.
EuPathDB; HostDB:ENSG00000163295.4; -.
GeneCards; ALPI; -.
HGNC; HGNC:437; ALPI.
HPA; HPA038764; -.
HPA; HPA038765; -.
HPA; HPA051699; -.
MIM; 171740; gene.
neXtProt; NX_P09923; -.
OpenTargets; ENSG00000163295; -.
PharmGKB; PA24728; -.
eggNOG; KOG4126; Eukaryota.
eggNOG; COG1785; LUCA.
GeneTree; ENSGT00390000008704; -.
HOGENOM; HOG000099118; -.
HOVERGEN; HBG007345; -.
InParanoid; P09923; -.
KO; K01077; -.
OMA; YVWSRKG; -.
OrthoDB; EOG091G067H; -.
PhylomeDB; P09923; -.
TreeFam; TF323513; -.
Reactome; R-HSA-1483166; Synthesis of PA.
Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
Reactome; R-HSA-8935690; Digestion.
SABIO-RK; P09923; -.
ChiTaRS; ALPI; human.
GeneWiki; ALPI; -.
GenomeRNAi; 248; -.
PRO; PR:P09923; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000163295; -.
CleanEx; HS_ALPI; -.
ExpressionAtlas; P09923; baseline and differential.
Genevisible; P09923; HS.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0004035; F:alkaline phosphatase activity; ISS:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
GO; GO:0002020; F:protease binding; IPI:ParkinsonsUK-UCL.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0006501; P:C-terminal protein lipidation; TAS:Reactome.
GO; GO:0016311; P:dephosphorylation; ISS:UniProtKB.
GO; GO:0007586; P:digestion; TAS:Reactome.
GO; GO:0006654; P:phosphatidic acid biosynthetic process; TAS:Reactome.
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;
Cell membrane; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein;
Magnesium; Membrane; Metal-binding; Polymorphism; Reference proteome;
Signal; Transmembrane; Zinc.
SIGNAL 1 19 {ECO:0000269|PubMed:1458595,
ECO:0000269|PubMed:3458202}.
CHAIN 20 503 Intestinal-type alkaline phosphatase.
/FTId=PRO_0000024037.
PROPEP 504 528 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000024038.
ACT_SITE 111 111 Phosphoserine intermediate.
METAL 61 61 Magnesium. {ECO:0000250}.
METAL 61 61 Zinc 1. {ECO:0000250}.
METAL 111 111 Zinc 1. {ECO:0000250}.
METAL 174 174 Magnesium. {ECO:0000250}.
METAL 330 330 Magnesium. {ECO:0000250}.
METAL 335 335 Zinc 2. {ECO:0000250}.
METAL 339 339 Zinc 2; via tele nitrogen. {ECO:0000250}.
METAL 376 376 Zinc 1. {ECO:0000250}.
METAL 377 377 Zinc 1; via tele nitrogen. {ECO:0000250}.
METAL 451 451 Zinc 2; via tele nitrogen. {ECO:0000250}.
LIPID 503 503 GPI-anchor amidated aspartate.
{ECO:0000250}.
CARBOHYD 141 141 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 268 268 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 429 429 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 140 202 {ECO:0000250}.
DISULFID 486 493 {ECO:0000250}.
VARIANT 144 144 R -> H (in dbSNP:rs7559279).
/FTId=VAR_050524.
VARIANT 298 298 H -> L (in dbSNP:rs1047223).
/FTId=VAR_011816.
CONFLICT 347 347 L -> V (in Ref. 2; AAA51703).
{ECO:0000305}.
CONFLICT 410 410 I -> T (in Ref. 1; AAA51704).
{ECO:0000305}.
CONFLICT 497 497 P -> L (in Ref. 2; AAA51703).
{ECO:0000305}.
SEQUENCE 528 AA; 56812 MW; 465306BEDF9F0B79 CRC64;
MQGPWVLLLL GLRLQLSLGV IPAEEENPAF WNRQAAEALD AAKKLQPIQK VAKNLILFLG
DGLGVPTVTA TRILKGQKNG KLGPETPLAM DRFPYLALSK TYNVDRQVPD SAATATAYLC
GVKANFQTIG LSAAARFNQC NTTRGNEVIS VMNRAKQAGK SVGVVTTTRV QHASPAGTYA
HTVNRNWYSD ADMPASARQE GCQDIATQLI SNMDIDVILG GGRKYMFPMG TPDPEYPADA
SQNGIRLDGK NLVQEWLAKH QGAWYVWNRT ELMQASLDQS VTHLMGLFEP GDTKYEIHRD
PTLDPSLMEM TEAALRLLSR NPRGFYLFVE GGRIDHGHHE GVAYQALTEA VMFDDAIERA
GQLTSEEDTL TLVTADHSHV FSFGGYTLRG SSIFGLAPSK AQDSKAYTSI LYGNGPGYVF
NSGVRPDVNE SESGSPDYQQ QAAVPLSSET HGGEDVAVFA RGPQAHLVHG VQEQSFVAHV
MAFAACLEPY TACDLAPPAC TTDAAHPVAA SLPLLAGTLL LLGASAAP


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