PPAP2A: Difference between revisions

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{{Infobox_gene}}
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'''Lipid phosphate phosphohydrolase 1''' also known as  '''phosphatidic acid phosphatase 2a''' is an [[enzyme]] that in humans is encoded by the ''PPAP2A'' [[gene]].<ref name="pmid9305923">{{cite journal |vauthors=Kai M, Wada I, Imai S, Sakane F, Kanoh H | title = Cloning and characterization of two human isozymes of Mg2+-independent phosphatidic acid phosphatase | journal = J Biol Chem | volume = 272 | issue = 39 | pages = 24572–24578 |date=Oct 1997 | pmid = 9305923 | pmc =  | doi =10.1074/jbc.272.39.24572  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PPAP2A phosphatidic acid phosphatase type 2A| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8611| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Phosphatidic acid phosphatase type 2A
| HGNCid = 9228
| Symbol = PPAP2A
| AltSymbols =; LLP1a; LPP1; PAP-2a; PAP2; PAP2a2; PAP2alpha2; PAPalpha1
| OMIM = 607124
| ECnumber = 
| Homologene = 7484
| MGIid = 108412
| GeneAtlas_image1 = PBB_GE_PPAP2A_210946_at_tn.png
| GeneAtlas_image2 = PBB_GE_PPAP2A_209147_s_at_tn.png
| Function = {{GNF_GO|id=GO:0008195 |text = phosphatidate phosphatase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}}
| Process = {{GNF_GO|id=GO:0007205 |text = protein kinase C activation}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0008354 |text = germ cell migration}} {{GNF_GO|id=GO:0019216 |text = regulation of lipid metabolic process}} {{GNF_GO|id=GO:0030521 |text = androgen receptor signaling pathway}} {{GNF_GO|id=GO:0046839 |text = phospholipid dephosphorylation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 8611
    | Hs_Ensembl = ENSG00000067113
    | Hs_RefseqProtein = NP_003702
    | Hs_RefseqmRNA = NM_003711
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 5
    | Hs_GenLoc_start = 54756260
    | Hs_GenLoc_end = 54973626
    | Hs_Uniprot = O14494
    | Mm_EntrezGene = 19012
    | Mm_Ensembl = ENSMUSG00000021759
    | Mm_RefseqmRNA = NM_008247
    | Mm_RefseqProtein = NP_032273
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 13
    | Mm_GenLoc_start = 113921772
    | Mm_GenLoc_end = 113988759
    | Mm_Uniprot = Q80XY1
  }}
}}
'''Phosphatidic acid phosphatase type 2A''', also known as '''PPAP2A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PPAP2A phosphatidic acid phosphatase type 2A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8611| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Lipid phosphate phosphohydrolase 1 is a member of the [[phosphatidate phosphatase|phosphatidic acid phosphatase]] (PAP) family. PAPs convert [[phosphatidic acid]] to [[diglyceride|diacylglycerol]], and function in de novo synthesis of [[glycerolipid]]s as well as in receptor-activated signal transduction mediated by [[phospholipase D]]. This protein is an integral membrane glycoprotein, and has been shown to be a surface enzyme that plays an active role in the hydrolysis and uptake of lipids from extracellular space. The expression of this gene is found to be regulated by androgen in a prostatic adenocarcinoma cell line. At least two alternatively spliced transcript variants encoding distinct isoforms have been described.<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the phosphatidic acid phosphatase (PAP) family. PAPs convert phosphatidic acid to diacylglycerol, and function in de novo synthesis of glycerolipids as well as in receptor-activated signal transduction mediated by phospholipase D. This protein is an integral membrane glycoprotein, and has been shown to be a surface enzyme that plays an active role in the hydrolysis and uptake of lipids from extracellular space. The expression of this gene is found to be regulated by androgen in a prostatic adenocarcinoma cell line. At least two alternatively spliced transcript variants encoding distinct isoforms have been described.<ref name="entrez">{{cite web | title = Entrez Gene: PPAP2A phosphatidic acid phosphatase type 2A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8611| accessdate = }}</ref>
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Kanoh H, Kai M, Wada I |title=Molecular characterization of the type 2 phosphatidic acid phosphatase. |journal=Chem. Phys. Lipids |volume=98 |issue= 1-2 |pages= 119-26 |year= 1999 |pmid= 10358934 |doi=  }}
*{{cite journal  |vauthors=Kanoh H, Kai M, Wada I |title=Molecular characterization of the type 2 phosphatidic acid phosphatase |journal=Chem. Phys. Lipids |volume=98 |issue= 1–2 |pages= 119–126 |year= 1999 |pmid= 10358934 |doi=10.1016/S0009-3084(99)00024-9 }}
*{{cite journal  | author=Nanjundan M, Possmayer F |title=Pulmonary phosphatidic acid phosphatase and lipid phosphate phosphohydrolase. |journal=Am. J. Physiol. Lung Cell Mol. Physiol. |volume=284 |issue= 1 |pages= L1-23 |year= 2003 |pmid= 12471011 |doi= 10.1152/ajplung.00029.2002 }}
*{{cite journal  |vauthors=Nanjundan M, Possmayer F |title=Pulmonary phosphatidic acid phosphatase and lipid phosphate phosphohydrolase |journal=Am. J. Physiol. Lung Cell Mol. Physiol. |volume=284 |issue= 1 |pages= L1–23 |year= 2003 |pmid= 12471011 |doi= 10.1152/ajplung.00029.2002 }}
*{{cite journal  | author=Kai M, Wada I, Imai S, ''et al.'' |title=Cloning and characterization of two human isozymes of Mg2+-independent phosphatidic acid phosphatase. |journal=J. Biol. Chem. |volume=272 |issue= 39 |pages= 24572-8 |year= 1997 |pmid= 9305923 |doi= }}
*{{cite journal  |vauthors=Ulrix W, Swinnen JV, Heyns W, Verhoeven G |title=Identification of the phosphatidic acid phosphatase type 2a isozyme as an androgen-regulated gene in the human prostatic adenocarcinoma cell line LNCaP |journal=J. Biol. Chem. |volume=273 |issue= 8 |pages= 4660–4665 |year= 1998 |pmid= 9468526 |doi=10.1074/jbc.273.8.4660  }}
*{{cite journal  | author=Ulrix W, Swinnen JV, Heyns W, Verhoeven G |title=Identification of the phosphatidic acid phosphatase type 2a isozyme as an androgen-regulated gene in the human prostatic adenocarcinoma cell line LNCaP. |journal=J. Biol. Chem. |volume=273 |issue= 8 |pages= 4660-5 |year= 1998 |pmid= 9468526 |doi= }}
*{{cite journal  |vauthors=Leung DW, Tompkins CK, White T |title=Molecular cloning of two alternatively spliced forms of human phosphatidic acid phosphatase cDNAs that are differentially expressed in normal and tumor cells |journal=DNA Cell Biol. |volume=17 |issue= 4 |pages= 377–385 |year= 1998 |pmid= 9570154 |doi=10.1089/dna.1998.17.377  }}
*{{cite journal  | author=Leung DW, Tompkins CK, White T |title=Molecular cloning of two alternatively spliced forms of human phosphatidic acid phosphatase cDNAs that are differentially expressed in normal and tumor cells. |journal=DNA Cell Biol. |volume=17 |issue= 4 |pages= 377-85 |year= 1998 |pmid= 9570154 |doi=  }}
*{{cite journal  |vauthors=Hooks SB, Ragan SP, Lynch KR |title=Identification of a novel human phosphatidic acid phosphatase type 2 isoform |journal=FEBS Lett. |volume=427 |issue= 2 |pages= 188–192 |year= 1998 |pmid= 9607309 |doi=10.1016/S0014-5793(98)00421-9 }}
*{{cite journal  | author=Hooks SB, Ragan SP, Lynch KR |title=Identification of a novel human phosphatidic acid phosphatase type 2 isoform. |journal=FEBS Lett. |volume=427 |issue= 2 |pages= 188-92 |year= 1998 |pmid= 9607309 |doi=  }}
*{{cite journal  |vauthors=Roberts R, Sciorra VA, Morris AJ |title=Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform |journal=J. Biol. Chem. |volume=273 |issue= 34 |pages= 22059–22067 |year= 1998 |pmid= 9705349 |doi=10.1074/jbc.273.34.22059 }}
*{{cite journal  | author=Roberts R, Sciorra VA, Morris AJ |title=Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform. |journal=J. Biol. Chem. |volume=273 |issue= 34 |pages= 22059-67 |year= 1998 |pmid= 9705349 |doi=  }}
*{{cite journal  | author=Neumann J |title=Pharmacological characterization of protein phosphatase activities in preparations from failing human hearts |journal=J. Pharmacol. Exp. Ther. |volume=289 |issue= 1 |pages= 188–93 |year= 1999 |pmid= 10087003 |doi=  |name-list-format=vanc| author2=Maas R | author3=Bokník P | display-authors=3  | last4=Jones  | first4=LR  | last5=Zimmermann  | first5=N  | last6=Scholz  | first6=H }}
*{{cite journal  | author=Neumann J, Maas R, Bokník P, ''et al.'' |title=Pharmacological characterization of protein phosphatase activities in preparations from failing human hearts. |journal=J. Pharmacol. Exp. Ther. |volume=289 |issue= 1 |pages= 188-93 |year= 1999 |pmid= 10087003 |doi=  }}
*{{cite journal  | author=Moreno CS |title=WD40 repeat proteins striatin and S/G(2) nuclear autoantigen are members of a novel family of calmodulin-binding proteins that associate with protein phosphatase 2A |journal=J. Biol. Chem. |volume=275 |issue= 8 |pages= 5257–5263 |year= 2000 |pmid= 10681496 |doi=10.1074/jbc.275.8.5257 |name-list-format=vanc| author2=Park S | author3=Nelson K  | display-authors=3  | last4=Ashby  | first4=D  | last5=Hubalek  | first5=F  | last6=Lane  | first6=WS  | last7=Pallas | first7=DC | pmc=3505218}}
*{{cite journal  | author=Moreno CS, Park S, Nelson K, ''et al.'' |title=WD40 repeat proteins striatin and S/G(2) nuclear autoantigen are members of a novel family of calmodulin-binding proteins that associate with protein phosphatase 2A. |journal=J. Biol. Chem. |volume=275 |issue= 8 |pages= 5257-63 |year= 2000 |pmid= 10681496 |doi=  }}
*{{cite journal  |vauthors=Roberts RZ, Morris AJ |title=Role of phosphatidic acid phosphatase 2a in uptake of extracellular lipid phosphate mediators |journal=Biochim. Biophys. Acta |volume=1487 |issue= 1 |pages= 33–49 |year= 2001 |pmid= 10962286 |doi= 10.1016/s1388-1981(00)00081-0}}
*{{cite journal | author=Roberts RZ, Morris AJ |title=Role of phosphatidic acid phosphatase 2a in uptake of extracellular lipid phosphate mediators. |journal=Biochim. Biophys. Acta |volume=1487 |issue= 1 |pages= 33-49 |year= 2001 |pmid= 10962286 |doi=  }}
*{{cite journal  | author=Woetmann A |title=Protein phosphatase 2A (PP2A) regulates interleukin-4-mediated STAT6 signaling |journal=J. Biol. Chem. |volume=278 |issue= 5 |pages= 2787–2791 |year= 2003 |pmid= 12426308 |doi= 10.1074/jbc.M210196200 |name-list-format=vanc| author2=Brockdorff J  | author3=Lovato P  | display-authors=3  | last4=Nielsen  | first4=M.  | last5=Leick  | first5=V.  | last6=Rieneck  | first6=K.  | last7=Svejgaard  | first7=A. | last8=Geisler  | first8=C.  | last9=Odum  | first9=N. }}
*{{cite journal  | author=Woetmann A, Brockdorff J, Lovato P, ''et al.'' |title=Protein phosphatase 2A (PP2A) regulates interleukin-4-mediated STAT6 signaling. |journal=J. Biol. Chem. |volume=278 |issue= 5 |pages= 2787-91 |year= 2003 |pmid= 12426308 |doi= 10.1074/jbc.M210196200 }}
*{{cite journal  |vauthors=Pandey AV, Mellon SH, Miller WL |title=Protein phosphatase 2A and phosphoprotein SET regulate androgen production by P450c17 |journal=J. Biol. Chem. |volume=278 |issue= 5 |pages= 2837–2844 |year= 2003 |pmid= 12444089 |doi= 10.1074/jbc.M209527200 }}
*{{cite journal  | author=Pandey AV, Mellon SH, Miller WL |title=Protein phosphatase 2A and phosphoprotein SET regulate androgen production by P450c17. |journal=J. Biol. Chem. |volume=278 |issue= 5 |pages= 2837-44 |year= 2003 |pmid= 12444089 |doi= 10.1074/jbc.M209527200 }}
*{{cite journal  | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–16903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 |name-list-format=vanc| author2=Feingold EA | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Smyth SS |title=Lipid phosphate phosphatases regulate lysophosphatidic acid production and signaling in platelets: studies using chemical inhibitors of lipid phosphate phosphatase activity |journal=J. Biol. Chem. |volume=278 |issue= 44 |pages= 43214–43223 |year= 2003 |pmid= 12909631 |doi= 10.1074/jbc.M306709200 |name-list-format=vanc| author2=Sciorra VA  | author3=Sigal YJ  | display-authors=3  | last4=Pamuklar  | first4=Z  | last5=Wang  | first5=Z  | last6=Xu  | first6=Y  | last7=Prestwich  | first7=GD  | last8=Morris  | first8=AJ }}
*{{cite journal | author=Smyth SS, Sciorra VA, Sigal YJ, ''et al.'' |title=Lipid phosphate phosphatases regulate lysophosphatidic acid production and signaling in platelets: studies using chemical inhibitors of lipid phosphate phosphatase activity. |journal=J. Biol. Chem. |volume=278 |issue= 44 |pages= 43214-23 |year= 2003 |pmid= 12909631 |doi= 10.1074/jbc.M306709200 }}
*{{cite journal  | author=Tanyi JL |title=Role of decreased levels of lipid phosphate phosphatase-1 in accumulation of lysophosphatidic acid in ovarian cancer |journal=Clin. Cancer Res. |volume=9 |issue= 10 Pt 1 |pages= 3534–45 |year= 2004 |pmid= 14506139 |doi=  |name-list-format=vanc| author2=Hasegawa Y  | author3=Lapushin R  | display-authors=3  | last4=Morris  | first4=AJ  | last5=Wolf  | first5=JK  | last6=Berchuck  | first6=A  | last7=Lu  | first7=K  | last8=Smith  | first8=DI  | last9=Kalli  | first9=K  }}
*{{cite journal  | author=Tanyi JL, Hasegawa Y, Lapushin R, ''et al.'' |title=Role of decreased levels of lipid phosphate phosphatase-1 in accumulation of lysophosphatidic acid in ovarian cancer. |journal=Clin. Cancer Res. |volume=9 |issue= 10 Pt 1 |pages= 3534-45 |year= 2004 |pmid= 14506139 |doi= }}
*{{cite journal  | author=Gerhard DS |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–2127 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928  |name-list-format=vanc| author2=Wagner L  | author3=Feingold EA  | display-authors=3  | last4=Shenmen  | first4=CM  | last5=Grouse  | first5=LH  | last6=Schuler  | first6=G  | last7=Klein  | first7=SL  | last8=Old  | first8=S  | last9=Rasooly  | first9=R }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  |vauthors=Grkovich A, Johnson CA, Buczynski MW, Dennis EA |title=Lipopolysaccharide-induced cyclooxygenase-2 expression in human U937 macrophages is phosphatidic acid phosphohydrolase-1-dependent |journal=J. Biol. Chem. |volume=281 |issue= 44 |pages= 32978–32987 |year= 2006 |pmid= 16950767 |doi= 10.1074/jbc.M605935200 }}
*{{cite journal  | author=Grkovich A, Johnson CA, Buczynski MW, Dennis EA |title=Lipopolysaccharide-induced cyclooxygenase-2 expression in human U937 macrophages is phosphatidic acid phosphohydrolase-1-dependent. |journal=J. Biol. Chem. |volume=281 |issue= 44 |pages= 32978-87 |year= 2006 |pmid= 16950767 |doi= 10.1074/jbc.M605935200 }}
*{{cite journal  | author=Kai M |title=Lipid phosphate phosphatases 1 and 3 are localized in distinct lipid rafts |journal=J. Biochem. |volume=140 |issue= 5 |pages= 677–686 |year= 2007 |pmid= 17005594 |doi= 10.1093/jb/mvj195 |name-list-format=vanc| author2=Sakane F  | author3=Jia YJ  | display-authors=3  | last4=Imai  | first4=S.-i.  | last5=Yasuda  | first5=S.  | last6=Kanoh  | first6=H. }}
*{{cite journal | author=Kai M, Sakane F, Jia YJ, ''et al.'' |title=Lipid phosphate phosphatases 1 and 3 are localized in distinct lipid rafts. |journal=J. Biochem. |volume=140 |issue= 5 |pages= 677-86 |year= 2007 |pmid= 17005594 |doi= 10.1093/jb/mvj195 }}
}}
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Latest revision as of 18:30, 7 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
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Wikidata
View/Edit Human

Lipid phosphate phosphohydrolase 1 also known as phosphatidic acid phosphatase 2a is an enzyme that in humans is encoded by the PPAP2A gene.[1][2]

Function

Lipid phosphate phosphohydrolase 1 is a member of the phosphatidic acid phosphatase (PAP) family. PAPs convert phosphatidic acid to diacylglycerol, and function in de novo synthesis of glycerolipids as well as in receptor-activated signal transduction mediated by phospholipase D. This protein is an integral membrane glycoprotein, and has been shown to be a surface enzyme that plays an active role in the hydrolysis and uptake of lipids from extracellular space. The expression of this gene is found to be regulated by androgen in a prostatic adenocarcinoma cell line. At least two alternatively spliced transcript variants encoding distinct isoforms have been described.[2]

References

  1. ↑ Kai M, Wada I, Imai S, Sakane F, Kanoh H (Oct 1997). "Cloning and characterization of two human isozymes of Mg2+-independent phosphatidic acid phosphatase". J Biol Chem. 272 (39): 24572–24578. doi:10.1074/jbc.272.39.24572. PMID 9305923.
  2. ↑ 2.0 2.1 "Entrez Gene: PPAP2A phosphatidic acid phosphatase type 2A".

Further reading



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