ALPI

Alkaline phosphatase, intestinal
Identifiers
Symbols	ALPI; IAP
External IDs	OMIM: 171740 MGI: 1924018 HomoloGene: 79555 GeneCards: ALPI Gene
EC number	3.1.3.1
Gene Ontology Molecular function • alkaline phosphatase activity • hydrolase activity • metal ion binding Cellular component • plasma membrane • membrane • integral to membrane • anchored to membrane Biological process • phosphorylation Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	248	76768
Ensembl	ENSG00000163295	ENSMUSG00000079440
UniProt	P09923	Q0VD75
RefSeq (mRNA)	NM_001631.3	NM_001081082.2
RefSeq (protein)	NP_001622.2	NP_001074551.1
Location (UCSC)	Chr 2: 233.32 – 233.32 Mb	Chr 1: 88.99 – 89 Mb
PubMed search	[1]	[2]
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Alkaline phosphatase, intestinal also known as ALPI is a type of alkaline phosphatase that in humans is encoded by the ALPI gene.^[1][2]

References

1. ^ Berger J, Garattini E, Hua JC, Udenfriend S (February 1987). "Cloning and sequencing of human intestinal alkaline phosphatase cDNA". Proc. Natl. Acad. Sci. U.S.A. 84 (3): 695–8. doi:10.1073/pnas.84.3.695. PMC 304282. PMID 3468508. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=304282. 
2. ^ Henthorn PS, Raducha M, Edwards YH, Weiss MJ, Slaughter C, Lafferty MA, Harris H (March 1987). "Nucleotide and amino acid sequences of human intestinal alkaline phosphatase: close homology to placental alkaline phosphatase". Proc. Natl. Acad. Sci. U.S.A. 84 (5): 1234–8. doi:10.1073/pnas.84.5.1234. PMC 304401. PMID 3469665. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=304401. 

Further reading

• Hirasaka K, Tokuoka K, Nakao R, et al. (2008). "Cathepsin C propeptide interacts with intestinal alkaline phosphatase and heat shock cognate protein 70 in human Caco-2 cells.". J Physiol Sci 58 (2): 105–11. doi:10.2170/physiolsci.RP013007. PMID 18307834. 
• Mahmood A, Shao JS, Alpers DH (2003). "Rat enterocytes secrete SLPs containing alkaline phosphatase and cubilin in response to corn oil feeding.". Am. J. Physiol. Gastrointest. Liver Physiol. 285 (2): G433–41. doi:10.1152/ajpgi.00466.2002. PMID 12660142. 
• Wada A, Wang AP, Isomoto H, et al. (2005). "Placental and intestinal alkaline phosphatases are receptors for Aeromonas sobria hemolysin.". Int. J. Med. Microbiol. 294 (7): 427–35. doi:10.1016/j.ijmm.2004.09.012. PMID 15715171. 
• Nakano T, Inoue I, Alpers DH, et al. (2009). "Role of lysophosphatidylcholine in brush-border intestinal alkaline phosphatase release and restoration.". Am. J. Physiol. Gastrointest. Liver Physiol. 297 (1): G207–14. doi:10.1152/ajpgi.90590.2008. PMID 19407215. 
• Malo MS, Zhang W, Alkhoury F, et al. (2004). "Thyroid hormone positively regulates the enterocyte differentiation marker intestinal alkaline phosphatase gene via an atypical response element.". Mol. Endocrinol. 18 (8): 1941–62. doi:10.1210/me.2003-0351. PMID 15143152. 
• Rump A, Kasper G, Hayes C, et al. (2001). "Complex arrangement of genes within a 220-kb region of double-duplicated DNA on human 2q37.1.". Genomics 73 (1): 50–5. doi:10.1006/geno.2000.6504. PMID 11352565. 
• Nauli AM, Zheng S, Yang Q, et al. (2003). "Intestinal alkaline phosphatase release is not associated with chylomicron formation.". Am. J. Physiol. Gastrointest. Liver Physiol. 284 (4): G583–7. doi:10.1152/ajpgi.00482.2002. PMID 12466148. 
• Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1356129. 
• Alkhoury F, Malo MS, Mozumder M, et al. (2005). "Differential regulation of intestinal alkaline phosphatase gene expression by Cdx1 and Cdx2.". Am. J. Physiol. Gastrointest. Liver Physiol. 289 (2): G285–90. doi:10.1152/ajpgi.00037.2005. PMID 15774940. 
• Giatromanolaki A, Sivridis E, Maltezos E, Koukourakis MI (2002). "Down-regulation of intestinal-type alkaline phosphatase in the tumor vasculature and stroma provides a strong basis for explaining amifostine selectivity.". Semin. Oncol. 29 (6 Suppl 19): 14–21. doi:10.1053/sonc.2002.37356. PMID 12577238. 
• Torres MI, Lorite P, López-Casado MA, Ríos A (2007). "A new approach using tissue alkaline phosphatase histochemistry to identify Crohn's disease.". Pathol. Res. Pract. 203 (6): 485–7. doi:10.1016/j.prp.2007.02.003. PMID 17498884. 
• Hinnebusch BF, Siddique A, Henderson JW, et al. (2004). "Enterocyte differentiation marker intestinal alkaline phosphatase is a target gene of the gut-enriched Kruppel-like factor.". Am. J. Physiol. Gastrointest. Liver Physiol. 286 (1): G23–30. doi:10.1152/ajpgi.00203.2003. PMID 12919939. 
• Le Du MH, Millan JL (2002). "Structural evidence of functional divergence in human alkaline phosphatases.". J. Biol. Chem. 277 (51): 49808–14. doi:10.1074/jbc.M207394200. PMID 12372831. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Goldberg RF, Austen WG, Zhang X, et al. (2008). "Intestinal alkaline phosphatase is a gut mucosal defense factor maintained by enteral nutrition.". Proc. Natl. Acad. Sci. U.S.A. 105 (9): 3551–6. doi:10.1073/pnas.0712140105. PMC 2265168. PMID 18292227. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2265168. 
• Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins.". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=514446. 
• Olsen L, Bressendorff S, Troelsen JT, Olsen J (2005). "Differentiation-dependent activation of the human intestinal alkaline phosphatase promoter by HNF-4 in intestinal cells.". Am. J. Physiol. Gastrointest. Liver Physiol. 289 (2): G220–6. doi:10.1152/ajpgi.00449.2004. PMID 15831710. 
• Fumoto K, Hoogenraad CC, Kikuchi A (2006). "GSK-3beta-regulated interaction of BICD with dynein is involved in microtubule anchorage at centrosome.". EMBO J. 25 (24): 5670–82. doi:10.1038/sj.emboj.7601459. PMC 1698904. PMID 17139249. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1698904. 
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1847948. 

v t e Hydrolase: esterases (EC 3.1) 3.1.1: Carboxylic ester hydrolases Cholinesterase (Acetylcholinesterase, Butyrylcholinesterase) · Pectinesterase · 6-phosphogluconolactonase · PAF acetylhydrolase Lipase (Bile salt-dependent, Gastric/Lingual, Pancreatic, Lysosomal, Hormone-sensitive, Endothelial, Hepatic, Lipoprotein, Monoacylglycerol, Diacylglycerol) Phospholipase (A1, A2, B) 3.1.2: Thioesterase Palmitoyl protein thioesterase · Ubiquitin carboxy-terminal hydrolase L1 3.1.3: Phosphatase Alkaline phosphatase (ALPI, ALPL, ALPP) · Acid phosphatase (Prostatic)/Tartrate-resistant acid phosphatase/Purple acid phosphatases · Nucleotidase · Glucose 6-phosphatase · Fructose 1,6-bisphosphatase · Calcineurin · Phosphoprotein phosphatase (PP2A) · OCRL · Pyruvate dehydrogenase phosphatase · Fructose 6-P,2-kinase:fructose 2,6-bisphosphatase · PTEN · Phytase · Inositol-phosphate phosphatase (IMPA1) Phosphoprotein phosphatase: Protein tyrosine phosphatase · Protein serine/threonine phosphatase · Dual-specificity phosphatase 3.1.4: Phosphodiesterase Autotaxin · Phospholipase (C, D) · Sphingomyelin phosphodiesterase (1) · PDE1 · PDE2 · PDE3 · PDE4A/PDE4B · PDE5 · Lecithinase (Clostridium perfringens alpha toxin) · Cyclic nucleotide phosphodiesterase 3.1.6: Sulfatase arylsulfatase (Arylsulfatase A, Arylsulfatase B, Arylsulfatase E, Steroid sulfatase) · Galactosamine-6 sulfatase · Iduronate-2-sulfatase · N-acetylglucosamine-6-sulfatase Nuclease (includes deoxyribonuclease and ribonuclease) 3.1.11-16: Exonuclease Exodeoxyribonuclease RecBCD Exoribonuclease Oligonucleotidase 3.1.21-31: Endonuclease Endodeoxyribonuclease Deoxyribonuclease I · Deoxyribonuclease II · Deoxyribonuclease IV · Restriction enzyme · UvrABC endonuclease Endoribonuclease RNase III · RNase H (1, 2A, 2B, 2C) · RNase P · RNase A (1, 2, 3, 4/5) · RNase T1 · RNA-induced silencing complex either deoxy- or ribo- Aspergillus nuclease S1 · Micrococcal nuclease B enzm 1.1 2 3 4 5 6 7 8 10 11 13 14 15-18 2.1 2 3 4 5 6 7 8 2.7.10 2.7.11-12 3.1 2 3 4 5 6 7 3.1.3.48 3.4.21 22 23 24 4.1 2 3 4 5 6 5.1 2 3 4 99 6.1-3 4 5-6

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