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Phospholipid phosphatase 3 (EC 3.1.3.4) (Differentially expressed in rat intestine 42) (Dri42) (Lipid phosphate phosphohydrolase 3) (PAP2-beta) (Phosphatidate phosphohydrolase type 2b) (Phosphatidic acid phosphatase 2b) (PAP-2b) (PAP2b)

 PLPP3_RAT               Reviewed;         312 AA.
P97544;
15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
23-MAY-2018, entry version 110.
RecName: Full=Phospholipid phosphatase 3 {ECO:0000312|RGD:620454};
EC=3.1.3.4;
AltName: Full=Differentially expressed in rat intestine 42;
Short=Dri42;
AltName: Full=Lipid phosphate phosphohydrolase 3;
AltName: Full=PAP2-beta;
AltName: Full=Phosphatidate phosphohydrolase type 2b;
AltName: Full=Phosphatidic acid phosphatase 2b;
Short=PAP-2b;
Short=PAP2b;
Name=Plpp3 {ECO:0000312|RGD:620454}; Synonyms=Lpp3, Ppap2b;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TOPOLOGY, AND GLYCOSYLATION.
STRAIN=Wistar; TISSUE=Small intestine;
PubMed=8939937; DOI=10.1074/jbc.271.47.29928;
Barila D., Plateroti M., Nobili F., Muda A.O., Xie Y., Morimoto T.,
Perozzi G.;
"The Dri 42 gene, whose expression is upregulated during epithelial
differentiation, encodes a novel ER resident transmembrane protein.";
J. Biol. Chem. 271:29928-29936(1996).
[2]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=8055940; DOI=10.1111/j.1432-1033.1994.tb19043.x;
Barila D., Murgia C., Nobili F., Gaetani S., Perozzi G.;
"Subtractive hybridization cloning of novel genes differentially
expressed during intestinal development.";
Eur. J. Biochem. 223:701-709(1994).
[3]
TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley;
PubMed=11704545;
Nanjundan M., Possmayer F.;
"Molecular cloning and expression of pulmonary lipid phosphate
phosphohydrolases.";
Am. J. Physiol. 281:L1484-L1493(2001).
-!- FUNCTION: Catalyzes the conversion of phosphatidic acid (PA) to
diacylglycerol (DG). In addition it hydrolyzes lysophosphatidic
acid (LPA), ceramide-1-phosphate (C-1-P) and sphingosine-1-
phosphate (S-1-P) (By similarity). Involved in the regulation of
epithelial differentiation. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: A 1,2-diacylglycerol 3-phosphate + H(2)O = a
1,2-diacyl-sn-glycerol + phosphate.
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
membrane protein.
-!- TISSUE SPECIFICITY: Detected in epithelial cells of intestinal
mucosa, lung, liver and brain. {ECO:0000269|PubMed:11704545,
ECO:0000269|PubMed:8055940}.
-!- DEVELOPMENTAL STAGE: Expression is increased during epithelial
differentiation in intestinal mucosa as well as in kidney, liver
and lung. {ECO:0000269|PubMed:8055940}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:8939937}.
-!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Y07783; CAA69106.1; -; mRNA.
UniGene; Rn.12038; -.
ProteinModelPortal; P97544; -.
STRING; 10116.ENSRNOP00000011237; -.
PaxDb; P97544; -.
PRIDE; P97544; -.
UCSC; RGD:620454; rat.
RGD; 620454; Plpp3.
eggNOG; ENOG410ITB4; Eukaryota.
eggNOG; ENOG4111NKF; LUCA.
HOGENOM; HOG000041307; -.
HOVERGEN; HBG002048; -.
InParanoid; P97544; -.
PhylomeDB; P97544; -.
PRO; PR:P97544; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:RGD.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0042577; F:lipid phosphatase activity; IBA:GO_Central.
GO; GO:0008195; F:phosphatidate phosphatase activity; IBA:GO_Central.
GO; GO:0042392; F:sphingosine-1-phosphate phosphatase activity; IBA:GO_Central.
GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
GO; GO:0046839; P:phospholipid dephosphorylation; IBA:GO_Central.
GO; GO:0006644; P:phospholipid metabolic process; IBA:GO_Central.
GO; GO:0030111; P:regulation of Wnt signaling pathway; IEA:InterPro.
InterPro; IPR028675; LPP3.
InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
PANTHER; PTHR10165:SF79; PTHR10165:SF79; 1.
Pfam; PF01569; PAP2; 1.
SMART; SM00014; acidPPc; 1.
SUPFAM; SSF48317; SSF48317; 1.
1: Evidence at protein level;
Complete proteome; Endoplasmic reticulum; Glycoprotein; Hydrolase;
Membrane; Phosphoprotein; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 312 Phospholipid phosphatase 3.
/FTId=PRO_0000220914.
TOPO_DOM 1 33 Cytoplasmic. {ECO:0000255}.
TRANSMEM 34 54 Helical. {ECO:0000255}.
TOPO_DOM 55 85 Lumenal. {ECO:0000255}.
TRANSMEM 86 106 Helical. {ECO:0000255}.
TOPO_DOM 107 123 Cytoplasmic. {ECO:0000255}.
TRANSMEM 124 144 Helical. {ECO:0000255}.
TOPO_DOM 145 194 Lumenal. {ECO:0000255}.
TRANSMEM 195 215 Helical. {ECO:0000255}.
TOPO_DOM 216 226 Cytoplasmic. {ECO:0000255}.
TRANSMEM 227 247 Helical. {ECO:0000255}.
TOPO_DOM 248 258 Lumenal. {ECO:0000255}.
TRANSMEM 259 279 Helical. {ECO:0000255}.
TOPO_DOM 280 312 Cytoplasmic. {ECO:0000255}.
MOD_RES 19 19 Phosphoserine.
{ECO:0000250|UniProtKB:O14495}.
CARBOHYD 171 171 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 312 AA; 35318 MW; 9B447FD321DB0419 CRC64;
MQSYKYDKAI VPESKNGGSP ALNNNPRKGG SKRVLLICLD LFCLFMAALP FLIIETSTIK
PYRRGFYCND ESIKYPLKVS ETINDAVLCA VGIVIAILRI ITGEFYRIYY LKEKSRSTIQ
NPYVAALYKQ VGCFLFGCAI SQSFTDIAKV SIGRLRPHFL SVCDPDFSQI NCSEGYIQNY
RCRGEDSKVQ EARKSFFSGH ASFSMFTMLY LVLYLQARFT WRGARLLRPL LQFTLLMMAF
YTGLSRVSDY KHHPSDVLAG FAQGALVACC IVFFVSDLFK TKTTLSLPAP AIRREILSPV
DIMDRSNHHN MV


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