Entry euk:PLPP1_MOUSE

ID   PLPP1_MOUSE             Reviewed;         283 AA.
AC   Q61469; Q61690; Q6GT30; Q8BPB8;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   10-MAY-2017, entry version 135.
DE   RecName: Full=Phospholipid phosphatase 1 {ECO:0000250|UniProtKB:O14494};
DE            EC=3.1.3.4;
DE   AltName: Full=35 kDa PAP;
DE            Short=mPAP;
DE   AltName: Full=Hydrogen peroxide-inducible protein 53;
DE            Short=Hic53;
DE   AltName: Full=Lipid phosphate phosphohydrolase 1;
DE   AltName: Full=PAP2-alpha;
DE   AltName: Full=Phosphatidate phosphohydrolase type 2a;
DE   AltName: Full=Phosphatidic acid phosphatase 2a;
DE            Short=PAP-2a;
DE            Short=PAP2a;
GN   Name=Plpp1 {ECO:0000250|UniProtKB:O14494};
GN   Synonyms=Hpic53, Lpp1, Ppap2a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INDUCTION.
RC   TISSUE=Calvaria;
RX   PubMed=7556647; DOI=10.1016/0014-5793(95)00957-B;
RA   Egawa K., Yoshiwara M., Shibanuma M., Nose K.;
RT   "Isolation of a novel ras-recision gene that is induced by hydrogen
RT   peroxide from a mouse osteoblastic cell line, MC3T3-E1.";
RL   FEBS Lett. 372:74-77(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Kidney;
RX   PubMed=8702556; DOI=10.1074/jbc.271.31.18931;
RA   Kai M., Wada I., Imai S., Sakane F., Kanoh H.;
RT   "Identification and cDNA cloning of 35-kDa phosphatidic acid
RT   phosphatase (type 2) bound to plasma membranes.";
RL   J. Biol. Chem. 271:18931-18938(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=FVB/N;
RA   Yokoyama K., Tigyi G.;
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Ovary, and Uterus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   CHARACTERIZATION.
RC   TISSUE=Liver;
RX   PubMed=10359651; DOI=10.1042/bj3400677;
RA   Jasinska R., Zhang Q.-X., Pilquil C., Singh I., Xu J., Dewald J.,
RA   Dillon D.A., Berthiaume L.G., Carman G.M., Waggoner D.W.,
RA   Brindley D.N.;
RT   "Lipid phosphate phosphohydrolase-1 degrades exogenous glycerolipid
RT   and sphingolipid phosphate esters.";
RL   Biochem. J. 340:677-686(1999).
RN   [7]
RP   SUBUNIT.
RX   PubMed=14725715; DOI=10.1186/1471-2091-5-2;
RA   Burnett C., Makridou P., Hewlett L., Howard K.;
RT   "Lipid phosphate phosphatases dimerise, but this interaction is not
RT   required for in vivo activity.";
RL   BMC Biochem. 5:2-2(2004).
RN   [8]
RP   OVEREXPRESSION.
RX   PubMed=14687668; DOI=10.1016/j.cellsig.2003.08.012;
RA   Yue J., Yokoyama K., Balazs L., Baker D.L., Smalley D., Pilquil C.,
RA   Brindley D.N., Tigyi G.;
RT   "Mice with transgenic overexpression of lipid phosphate phosphatase-1
RT   display multiple organotypic deficits without alteration in
RT   circulating lysophosphatidate level.";
RL   Cell. Signal. 16:385-399(2004).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Heart, Kidney, Lung, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Broad-specificity phosphohydrolase that dephosphorylates
CC       exogenous bioactive glycerolipids and sphingolipids. Catalyzes the
CC       conversion of phosphatidic acid (PA) to diacylglycerol (DG). In
CC       addition it hydrolyzes lysophosphatidic acid (LPA), diacyl
CC       glycerol pyrophosphate (DGPP), ceramide-1-phosphate (C-1-P) and
CC       sphingosine-1-phosphate (S-1-P). The relative catalytic efficiency
CC       is LPA > PA > C-1-P > S-1-P.
CC   -!- CATALYTIC ACTIVITY: A 1,2-diacylglycerol 3-phosphate + H(2)O = a
CC       1,2-diacyl-sn-glycerol + phosphate.
CC   -!- SUBUNIT: Homodimer. This complex seems not to be involved in
CC       substrate recognition, it may confer only structural or functional
CC       stability. {ECO:0000269|PubMed:14725715}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Note=Found predominantly in plasma membrane.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q61469-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q61469-2; Sequence=VSP_009652;
CC   -!- TISSUE SPECIFICITY: Highly expressed in kidney and lung. Almost
CC       undetectable in brain, heart, bone, muscle or spleen.
CC   -!- INDUCTION: Moderately, by hydrogen peroxide, calcium ionophore and
CC       dexamethasone. {ECO:0000269|PubMed:7556647}.
CC   -!- PTM: N-glycosylated. Contains high-mannose oligosaccharide.
CC   -!- MISCELLANEOUS: Overexpression elicited a number of phenotypic
CC       alteration without affecting several aspects of LPA signaling.
CC       Phenotypic abnormalities affect primarily three organs: the liver,
CC       the skin, and the reproductive organs. There is a reduction on
CC       body size, birth weight, abnormalities in fur growth, and a
CC       severely impaired spermatogenesis.
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA85353.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
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DR   EMBL; L43371; AAA85353.1; ALT_SEQ; mRNA.
DR   EMBL; D84376; BAA12335.1; -; mRNA.
DR   EMBL; AY247795; AAP04434.1; -; mRNA.
DR   EMBL; AY247796; AAP04435.1; -; mRNA.
DR   EMBL; AK077275; BAC36724.1; -; mRNA.
DR   EMBL; BC061161; AAH61161.1; -; mRNA.
DR   CCDS; CCDS26776.1; -. [Q61469-2]
DR   CCDS; CCDS26777.1; -. [Q61469-1]
DR   PIR; S66668; S66668.
DR   RefSeq; NP_032273.1; NM_008247.3. [Q61469-2]
DR   RefSeq; NP_032929.1; NM_008903.2. [Q61469-1]
DR   UniGene; Mm.291029; -.
DR   UniGene; Mm.317186; -.
DR   ProteinModelPortal; Q61469; -.
DR   IntAct; Q61469; 1.
DR   iPTMnet; Q61469; -.
DR   PhosphoSitePlus; Q61469; -.
DR   PeptideAtlas; Q61469; -.
DR   PRIDE; Q61469; -.
DR   Ensembl; ENSMUST00000016144; ENSMUSP00000016144; ENSMUSG00000021759. [Q61469-2]
DR   Ensembl; ENSMUST00000070951; ENSMUSP00000064423; ENSMUSG00000021759. [Q61469-1]
DR   GeneID; 19012; -.
DR   KEGG; mmu:19012; -.
DR   UCSC; uc007rwq.2; mouse. [Q61469-1]
DR   UCSC; uc007rwr.2; mouse. [Q61469-2]
DR   CTD; 8611; -.
DR   MGI; MGI:108412; Plpp1.
DR   GeneTree; ENSGT00620000087654; -.
DR   HOGENOM; HOG000041307; -.
DR   HOVERGEN; HBG002048; -.
DR   InParanoid; Q61469; -.
DR   KO; K01080; -.
DR   OMA; IMKSENS; -.
DR   OrthoDB; EOG091G0K5H; -.
DR   PhylomeDB; Q61469; -.
DR   TreeFam; TF316040; -.
DR   BRENDA; 3.1.3.81; 3474.
DR   Reactome; R-MMU-1660661; Sphingolipid de novo biosynthesis.
DR   ChiTaRS; Ppap2a; mouse.
DR   PRO; PR:Q61469; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   Bgee; ENSMUSG00000021759; -.
DR   CleanEx; MM_PPAP2A; -.
DR   Genevisible; Q61469; MM.
DR   GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR   GO; GO:0005887; C:integral component of plasma membrane; TAS:MGI.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:MGI.
DR   GO; GO:0042577; F:lipid phosphatase activity; IBA:GO_Central.
DR   GO; GO:0008195; F:phosphatidate phosphatase activity; IDA:MGI.
DR   GO; GO:0006672; P:ceramide metabolic process; TAS:MGI.
DR   GO; GO:0006651; P:diacylglycerol biosynthetic process; TAS:MGI.
DR   GO; GO:0046839; P:phospholipid dephosphorylation; IBA:GO_Central.
DR   GO; GO:0006644; P:phospholipid metabolic process; IBA:GO_Central.
DR   GO; GO:0006470; P:protein dephosphorylation; IDA:MGI.
DR   GO; GO:0007165; P:signal transduction; TAS:MGI.
DR   GO; GO:0006670; P:sphingosine metabolic process; TAS:MGI.
DR   Gene3D; 1.20.144.10; -; 1.
DR   InterPro; IPR028670; LPP1.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   PANTHER; PTHR10165:SF112; PTHR10165:SF112; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; SSF48317; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Complete proteome; Glycoprotein;
KW   Hydrolase; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    283       Phospholipid phosphatase 1.
FT                                /FTId=PRO_0000220906.
FT   TOPO_DOM      1      6       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM      7     27       Helical. {ECO:0000255}.
FT   TOPO_DOM     28     53       Extracellular. {ECO:0000255}.
FT   TRANSMEM     54     74       Helical. {ECO:0000255}.
FT   TOPO_DOM     75     88       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     89    109       Helical. {ECO:0000255}.
FT   TOPO_DOM    110    164       Extracellular. {ECO:0000255}.
FT   TRANSMEM    165    185       Helical. {ECO:0000255}.
FT   TOPO_DOM    186    199       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    200    220       Helical. {ECO:0000255}.
FT   TOPO_DOM    221    229       Extracellular. {ECO:0000255}.
FT   TRANSMEM    230    250       Helical. {ECO:0000255}.
FT   TOPO_DOM    251    283       Cytoplasmic. {ECO:0000255}.
FT   CARBOHYD    142    142       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   VAR_SEQ      21     70       GLPFAILTSRHTPFQRGIFCNDDSIKYPYKEDTIPYALLGG
FT                                IVIPFCIIV -> AMPMTILKLGKVYPFQRGFFCTDNSVKY
FT                                PYHDSTIPSRILAILGLGLPIFS (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:16141072,
FT                                ECO:0000303|Ref.3}.
FT                                /FTId=VSP_009652.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       104    248       ipfam:PAP2 [T]
FT   MYHIT       102    243       ismart:acidPPc [T]
SQ   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
//