INFO: Beginning work on ALPP... {December 18, 2007 6:06:25 AM PST}
AMBIGUITY: Did not locate an acceptable page to update. {December 18, 2007 6:07:07 AM PST}
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{{GNF_Protein_box
| image = PBB_Protein_ALPP_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ew2.
| PDB = {{PDB2|1ew2}}, {{PDB2|1zeb}}, {{PDB2|1zed}}, {{PDB2|1zef}}, {{PDB2|2glq}}
| Name = Alkaline phosphatase, placental (Regan isozyme)
| HGNCid = 439
| Symbol = ALPP
| AltSymbols =; ALP; PLAP; ALPG; ALPPL; GCAP
| OMIM = 171800
| ECnumber =
| Homologene = 55592
| MGIid = 108009
| GeneAtlas_image1 = PBB_GE_ALPP_204664_at_tn.png
| GeneAtlas_image2 = PBB_GE_ALPP_211619_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_ALPP_210431_at_tn.png
| Function = {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004035 |text = alkaline phosphatase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0048503 |text = GPI anchor binding}}
| Component = {{GNF_GO|id=GO:0009986 |text = cell surface}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0016310 |text = phosphorylation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 250
| Hs_Ensembl = ENSG00000163283
| Hs_RefseqProtein = NP_001623
| Hs_RefseqmRNA = NM_001632
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 232951627
| Hs_GenLoc_end = 232955832
| Hs_Uniprot = P05187
| Mm_EntrezGene = 11650
| Mm_Ensembl = ENSMUSG00000026246
| Mm_RefseqmRNA = NM_007433
| Mm_RefseqProtein = NP_031459
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 88917861
| Mm_GenLoc_end = 88921082
| Mm_Uniprot = Q3ULC9
}}
}}
'''Alkaline phosphatase, placental (Regan isozyme)''', also known as '''ALPP''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ALPP alkaline phosphatase, placental (Regan isozyme)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=250| accessdate = }}</ref>
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{{PBB_Summary
| section_title =
| summary_text = There are at least four distinct but related alkaline phosphatases: intestinal, placental, placental-like, and liver/bone/kidney (tissue non-specific). The first three are located together on chromosome 2 while the tissue non-specific form is located on chromosome 1. The product of this gene is a membrane bound glycosylated enzyme, also referred to as the heat stable form, that is expressed primarily in the placenta although it is closely related to the intestinal form of the enzyme as well as to the placental-like form. The coding sequence for this form of alkaline phosphatase is unique in that the 3' untranslated region contains multiple copies of an Alu family repeat. In addition, this gene is polymorphic and three common alleles (type 1, type 2 and type 3) for this form of alkaline phosphatase have been well characterized.<ref name="entrez">{{cite web | title = Entrez Gene: ALPP alkaline phosphatase, placental (Regan isozyme)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=250| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Nye KE, Riley GA, Pinching AJ |title=The defect seen in the phosphatidylinositol hydrolysis pathway in HIV-infected lymphocytes and lymphoblastoid cells is due to inhibition of the inositol 1,4,5-trisphosphate 1,3,4,5-tetrakisphosphate 5-phosphomonoesterase. |journal=Clin. Exp. Immunol. |volume=89 |issue= 1 |pages= 89-93 |year= 1992 |pmid= 1321014 |doi= }}
*{{cite journal | author=Lowe ME |title=Site-specific mutations in the COOH-terminus of placental alkaline phosphatase: a single amino acid change converts a phosphatidylinositol-glycan-anchored protein to a secreted protein. |journal=J. Cell Biol. |volume=116 |issue= 3 |pages= 799-807 |year= 1992 |pmid= 1730777 |doi= }}
*{{cite journal | author=Micanovic R, Gerber LD, Berger J, ''et al.'' |title=Selectivity of the cleavage/attachment site of phosphatidylinositol-glycan-anchored membrane proteins determined by site-specific mutagenesis at Asp-484 of placental alkaline phosphatase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 1 |pages= 157-61 |year= 1990 |pmid= 2153284 |doi= }}
*{{cite journal | author=Martin D, Spurr NK, Trowsdale J |title=RFLP of the human placental alkaline phosphatase gene (PLAP). |journal=Nucleic Acids Res. |volume=15 |issue= 21 |pages= 9104 |year= 1988 |pmid= 2891112 |doi= }}
*{{cite journal | author=Kam W, Clauser E, Kim YS, ''et al.'' |title=Cloning, sequencing, and chromosomal localization of human term placental alkaline phosphatase cDNA. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 24 |pages= 8715-9 |year= 1986 |pmid= 3001717 |doi= }}
*{{cite journal | author=Knoll BJ, Rothblum KN, Longley M |title=Nucleotide sequence of the human placental alkaline phosphatase gene. Evolution of the 5' flanking region by deletion/substitution. |journal=J. Biol. Chem. |volume=263 |issue= 24 |pages= 12020-7 |year= 1988 |pmid= 3042787 |doi= }}
*{{cite journal | author=Micanovic R, Bailey CA, Brink L, ''et al.'' |title=Aspartic acid-484 of nascent placental alkaline phosphatase condenses with a phosphatidylinositol glycan to become the carboxyl terminus of the mature enzyme. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 5 |pages= 1398-402 |year= 1988 |pmid= 3422741 |doi= }}
*{{cite journal | author=Knoll BJ, Rothblum KN, Longley M |title=Two gene duplication events in the evolution of the human heat-stable alkaline phosphatases. |journal=Gene |volume=60 |issue= 2-3 |pages= 267-76 |year= 1988 |pmid= 3443302 |doi= }}
*{{cite journal | author=Ovitt CE, Strauss AW, Alpers DH, ''et al.'' |title=Expression of different-sized placental alkaline phosphatase mRNAs in placenta and choriocarcinoma cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 11 |pages= 3781-5 |year= 1986 |pmid= 3459156 |doi= }}
*{{cite journal | author=Henthorn PS, Knoll BJ, Raducha M, ''et al.'' |title=Products of two common alleles at the locus for human placental alkaline phosphatase differ by seven amino acids. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 15 |pages= 5597-601 |year= 1986 |pmid= 3461452 |doi= }}
*{{cite journal | author=Millán JL |title=Molecular cloning and sequence analysis of human placental alkaline phosphatase. |journal=J. Biol. Chem. |volume=261 |issue= 7 |pages= 3112-5 |year= 1986 |pmid= 3512548 |doi= }}
*{{cite journal | author=Ezra E, Blacher R, Udenfriend S |title=Purification and partial sequencing of human placental alkaline phosphatase. |journal=Biochem. Biophys. Res. Commun. |volume=116 |issue= 3 |pages= 1076-83 |year= 1984 |pmid= 6651840 |doi= }}
*{{cite journal | author=Le Du MH, Stigbrand T, Taussig MJ, ''et al.'' |title=Crystal structure of alkaline phosphatase from human placenta at 1.8 A resolution. Implication for a substrate specificity. |journal=J. Biol. Chem. |volume=276 |issue= 12 |pages= 9158-65 |year= 2001 |pmid= 11124260 |doi= 10.1074/jbc.M009250200 }}
*{{cite journal | author=Spurway TD, Dalley JA, High S, Bulleid NJ |title=Early events in glycosylphosphatidylinositol anchor addition. substrate proteins associate with the transamidase subunit gpi8p. |journal=J. Biol. Chem. |volume=276 |issue= 19 |pages= 15975-82 |year= 2001 |pmid= 11278620 |doi= 10.1074/jbc.M010128200 }}
*{{cite journal | author=Rump A, Kasper G, Hayes C, ''et al.'' |title=Complex arrangement of genes within a 220-kb region of double-duplicated DNA on human 2q37.1. |journal=Genomics |volume=73 |issue= 1 |pages= 50-5 |year= 2001 |pmid= 11352565 |doi= 10.1006/geno.2000.6504 }}
*{{cite journal | author=Wennberg C, Kozlenkov A, Di Mauro S, ''et al.'' |title=Structure, genomic DNA typing, and kinetic characterization of the D allozyme of placental alkaline phosphatase (PLAP/ALPP). |journal=Hum. Mutat. |volume=19 |issue= 3 |pages= 258-67 |year= 2002 |pmid= 11857742 |doi= 10.1002/humu.10052 }}
*{{cite journal | author=Kozlenkov A, Manes T, Hoylaerts MF, Millán JL |title=Function assignment to conserved residues in mammalian alkaline phosphatases. |journal=J. Biol. Chem. |volume=277 |issue= 25 |pages= 22992-9 |year= 2002 |pmid= 11937510 |doi= 10.1074/jbc.M202298200 }}
*{{cite journal | author=Tang J, Li W |title=[Methodological study on the assay of glycosylphosphatidylinositol-specific phospholipase D activity in serum] |journal=Hunan Yi Ke Da Xue Xue Bao |volume=24 |issue= 2 |pages= 119-22 |year= 2002 |pmid= 11938765 |doi= }}
*{{cite journal | author=Lehto MT, Sharom FJ |title=Proximity of the protein moiety of a GPI-anchored protein to the membrane surface: a FRET study. |journal=Biochemistry |volume=41 |issue= 26 |pages= 8368-76 |year= 2002 |pmid= 12081485 |doi= }}
*{{cite journal | author=Le Du MH, Millan JL |title=Structural evidence of functional divergence in human alkaline phosphatases. |journal=J. Biol. Chem. |volume=277 |issue= 51 |pages= 49808-14 |year= 2003 |pmid= 12372831 |doi= 10.1074/jbc.M207394200 }}
}}
{{refend}}
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{December 18, 2007 6:32:10 AM PST} 
