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Phospholipid phosphatase 1 (EC 3.1.3.4) (35 kDa PAP) (mPAP) (Hydrogen peroxide-inducible protein 53) (Hic53) (Lipid phosphate phosphohydrolase 1) (PAP2-alpha) (Phosphatidate phosphohydrolase type 2a) (Phosphatidic acid phosphatase 2a) (PAP-2a) (PAP2a)

 PLPP1_MOUSE             Reviewed;         283 AA.
Q61469; Q61690; Q6GT30; Q8BPB8;
15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
28-FEB-2018, entry version 141.
RecName: Full=Phospholipid phosphatase 1 {ECO:0000250|UniProtKB:O14494};
EC=3.1.3.4;
AltName: Full=35 kDa PAP;
Short=mPAP;
AltName: Full=Hydrogen peroxide-inducible protein 53;
Short=Hic53;
AltName: Full=Lipid phosphate phosphohydrolase 1;
AltName: Full=PAP2-alpha;
AltName: Full=Phosphatidate phosphohydrolase type 2a;
AltName: Full=Phosphatidic acid phosphatase 2a;
Short=PAP-2a;
Short=PAP2a;
Name=Plpp1 {ECO:0000250|UniProtKB:O14494};
Synonyms=Hpic53, Lpp1, Ppap2a;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INDUCTION.
TISSUE=Calvaria;
PubMed=7556647; DOI=10.1016/0014-5793(95)00957-B;
Egawa K., Yoshiwara M., Shibanuma M., Nose K.;
"Isolation of a novel ras-recision gene that is induced by hydrogen
peroxide from a mouse osteoblastic cell line, MC3T3-E1.";
FEBS Lett. 372:74-77(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Kidney;
PubMed=8702556; DOI=10.1074/jbc.271.31.18931;
Kai M., Wada I., Imai S., Sakane F., Kanoh H.;
"Identification and cDNA cloning of 35-kDa phosphatidic acid
phosphatase (type 2) bound to plasma membranes.";
J. Biol. Chem. 271:18931-18938(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
STRAIN=FVB/N;
Yokoyama K., Tigyi G.;
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Ovary, and Uterus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
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).
[6]
CHARACTERIZATION.
TISSUE=Liver;
PubMed=10359651; DOI=10.1042/bj3400677;
Jasinska R., Zhang Q.-X., Pilquil C., Singh I., Xu J., Dewald J.,
Dillon D.A., Berthiaume L.G., Carman G.M., Waggoner D.W.,
Brindley D.N.;
"Lipid phosphate phosphohydrolase-1 degrades exogenous glycerolipid
and sphingolipid phosphate esters.";
Biochem. J. 340:677-686(1999).
[7]
SUBUNIT.
PubMed=14725715; DOI=10.1186/1471-2091-5-2;
Burnett C., Makridou P., Hewlett L., Howard K.;
"Lipid phosphate phosphatases dimerise, but this interaction is not
required for in vivo activity.";
BMC Biochem. 5:2-2(2004).
[8]
OVEREXPRESSION.
PubMed=14687668; DOI=10.1016/j.cellsig.2003.08.012;
Yue J., Yokoyama K., Balazs L., Baker D.L., Smalley D., Pilquil C.,
Brindley D.N., Tigyi G.;
"Mice with transgenic overexpression of lipid phosphate phosphatase-1
display multiple organotypic deficits without alteration in
circulating lysophosphatidate level.";
Cell. Signal. 16:385-399(2004).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Kidney, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Broad-specificity phosphohydrolase that dephosphorylates
exogenous bioactive glycerolipids and sphingolipids. Catalyzes the
conversion of phosphatidic acid (PA) to diacylglycerol (DG). In
addition it hydrolyzes lysophosphatidic acid (LPA), diacyl
glycerol pyrophosphate (DGPP), ceramide-1-phosphate (C-1-P) and
sphingosine-1-phosphate (S-1-P). The relative catalytic efficiency
is LPA > PA > C-1-P > S-1-P.
-!- CATALYTIC ACTIVITY: A 1,2-diacylglycerol 3-phosphate + H(2)O = a
1,2-diacyl-sn-glycerol + phosphate.
-!- SUBUNIT: Homodimer. This complex seems not to be involved in
substrate recognition, it may confer only structural or functional
stability. {ECO:0000269|PubMed:14725715}.
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
Note=Found predominantly in plasma membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q61469-1; Sequence=Displayed;
Name=2;
IsoId=Q61469-2; Sequence=VSP_009652;
-!- TISSUE SPECIFICITY: Highly expressed in kidney and lung. Almost
undetectable in brain, heart, bone, muscle or spleen.
-!- INDUCTION: Moderately, by hydrogen peroxide, calcium ionophore and
dexamethasone. {ECO:0000269|PubMed:7556647}.
-!- PTM: N-glycosylated. Contains high-mannose oligosaccharide.
-!- MISCELLANEOUS: Overexpression elicited a number of phenotypic
alteration without affecting several aspects of LPA signaling.
Phenotypic abnormalities affect primarily three organs: the liver,
the skin, and the reproductive organs. There is a reduction on
body size, birth weight, abnormalities in fur growth, and a
severely impaired spermatogenesis.
-!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA85353.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; L43371; AAA85353.1; ALT_SEQ; mRNA.
EMBL; D84376; BAA12335.1; -; mRNA.
EMBL; AY247795; AAP04434.1; -; mRNA.
EMBL; AY247796; AAP04435.1; -; mRNA.
EMBL; AK077275; BAC36724.1; -; mRNA.
EMBL; BC061161; AAH61161.1; -; mRNA.
CCDS; CCDS26776.1; -. [Q61469-2]
CCDS; CCDS26777.1; -. [Q61469-1]
PIR; S66668; S66668.
RefSeq; NP_032273.1; NM_008247.3. [Q61469-2]
RefSeq; NP_032929.1; NM_008903.2. [Q61469-1]
UniGene; Mm.291029; -.
UniGene; Mm.317186; -.
ProteinModelPortal; Q61469; -.
IntAct; Q61469; 1.
iPTMnet; Q61469; -.
PhosphoSitePlus; Q61469; -.
PeptideAtlas; Q61469; -.
PRIDE; Q61469; -.
Ensembl; ENSMUST00000016144; ENSMUSP00000016144; ENSMUSG00000021759. [Q61469-2]
Ensembl; ENSMUST00000070951; ENSMUSP00000064423; ENSMUSG00000021759. [Q61469-1]
GeneID; 19012; -.
KEGG; mmu:19012; -.
UCSC; uc007rwq.2; mouse. [Q61469-1]
UCSC; uc007rwr.2; mouse. [Q61469-2]
CTD; 8611; -.
MGI; MGI:108412; Plpp1.
GeneTree; ENSGT00620000087654; -.
HOGENOM; HOG000041307; -.
HOVERGEN; HBG002048; -.
InParanoid; Q61469; -.
KO; K01080; -.
OMA; GNHYRNS; -.
OrthoDB; EOG091G0K5H; -.
PhylomeDB; Q61469; -.
TreeFam; TF316040; -.
BRENDA; 3.1.3.81; 3474.
Reactome; R-MMU-1660661; Sphingolipid de novo biosynthesis.
ChiTaRS; Plpp1; mouse.
PRO; PR:Q61469; -.
Proteomes; UP000000589; Chromosome 13.
Bgee; ENSMUSG00000021759; -.
CleanEx; MM_PPAP2A; -.
Genevisible; Q61469; MM.
GO; GO:0005887; C:integral component of plasma membrane; TAS:MGI.
GO; GO:0016020; C:membrane; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:MGI.
GO; GO:0042577; F:lipid phosphatase activity; IBA:GO_Central.
GO; GO:0008195; F:phosphatidate phosphatase activity; IDA:MGI.
GO; GO:0006672; P:ceramide metabolic process; TAS:MGI.
GO; GO:0006651; P:diacylglycerol biosynthetic process; TAS:MGI.
GO; GO:0046839; P:phospholipid dephosphorylation; IBA:GO_Central.
GO; GO:0006644; P:phospholipid metabolic process; IBA:GO_Central.
GO; GO:0006470; P:protein dephosphorylation; IDA:MGI.
GO; GO:0007165; P:signal transduction; TAS:MGI.
GO; GO:0006670; P:sphingosine metabolic process; TAS:MGI.
InterPro; IPR028670; LPP1.
InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
PANTHER; PTHR10165:SF26; PTHR10165:SF26; 1.
Pfam; PF01569; PAP2; 1.
SMART; SM00014; acidPPc; 1.
SUPFAM; SSF48317; SSF48317; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome; Glycoprotein;
Hydrolase; Membrane; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 283 Phospholipid phosphatase 1.
/FTId=PRO_0000220906.
TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.
TRANSMEM 7 27 Helical. {ECO:0000255}.
TOPO_DOM 28 53 Extracellular. {ECO:0000255}.
TRANSMEM 54 74 Helical. {ECO:0000255}.
TOPO_DOM 75 88 Cytoplasmic. {ECO:0000255}.
TRANSMEM 89 109 Helical. {ECO:0000255}.
TOPO_DOM 110 164 Extracellular. {ECO:0000255}.
TRANSMEM 165 185 Helical. {ECO:0000255}.
TOPO_DOM 186 199 Cytoplasmic. {ECO:0000255}.
TRANSMEM 200 220 Helical. {ECO:0000255}.
TOPO_DOM 221 229 Extracellular. {ECO:0000255}.
TRANSMEM 230 250 Helical. {ECO:0000255}.
TOPO_DOM 251 283 Cytoplasmic. {ECO:0000255}.
CARBOHYD 142 142 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 21 70 GLPFAILTSRHTPFQRGIFCNDDSIKYPYKEDTIPYALLGG
IVIPFCIIV -> AMPMTILKLGKVYPFQRGFFCTDNSVKY
PYHDSTIPSRILAILGLGLPIFS (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072,
ECO:0000303|Ref.3}.
/FTId=VSP_009652.
SEQUENCE 283 AA; 31892 MW; 669690568E549CC6 CRC64;
MFDKTRLPYV ALDVICVLLA GLPFAILTSR HTPFQRGIFC NDDSIKYPYK EDTIPYALLG
GIVIPFCIIV MSIGESLSVY FNVLHSNSFV GNPYIATIYK AVGAFLFGVS ASQSLTDIAK
YTIGSLRPHF LAICNPDWSK INCSDGYIED YICQGNEEKV KEGRLSFYSG HSSFSMYCML
FVALYLQARM KGDWARLLRP MLQFGLIAFS IYVGLSRVSD YKHHWSDVTV GLIQGAAMAI
LVALYVSDFF KDTHSYKERK EEDPHTTLHE TASSRNYSTN HEP


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