PLPP3_BOVIN
ID PLPP3_BOVIN Reviewed; 311 AA.
AC Q3SZE3;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Phospholipid phosphatase 3 {ECO:0000305};
DE EC=3.1.3.- {ECO:0000250|UniProtKB:O14495};
DE EC=3.1.3.4 {ECO:0000250|UniProtKB:O14495};
DE AltName: Full=Lipid phosphate phosphohydrolase 3;
DE AltName: Full=PAP2-beta;
DE AltName: Full=Phosphatidate phosphohydrolase type 2b;
DE AltName: Full=Phosphatidic acid phosphatase 2b;
DE Short=PAP-2b;
DE Short=PAP2b;
GN Name=PLPP3 {ECO:0000250|UniProtKB:O14495}; Synonyms=PPAP2B;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Magnesium-independent phospholipid phosphatase of the plasma
CC membrane that catalyzes the dephosphorylation of a variety of
CC glycerolipid and sphingolipid phosphate esters including
CC phosphatidate/PA, lysophosphatidate/LPA, diacylglycerol
CC pyrophosphate/DGPP, sphingosine 1-phosphate/S1P and ceramide 1-
CC phosphate/C1P. Also acts on N-oleoyl ethanolamine phosphate/N-(9Z-
CC octadecenoyl)-ethanolamine phosphate, a potential physiological
CC compound. Has both an extracellular and an intracellular phosphatase
CC activity, allowing the hydrolysis and the cellular uptake of these
CC bioactive lipid mediators from the milieu, regulating signal
CC transduction in different cellular processes. Through the
CC dephosphorylation of extracellular sphingosine-1-phosphate and the
CC regulation of its extra- and intracellular availability, plays a role
CC in vascular homeostasis, regulating endothelial cell migration,
CC adhesion, survival, proliferation and the production of pro-
CC inflammatory cytokines (By similarity). By maintaining the appropriate
CC levels of this lipid in the cerebellum, also ensure its proper
CC development and function (By similarity). Through its intracellular
CC lipid phosphatase activity may act in early compartments of the
CC secretory pathway, regulating the formation of Golgi to endoplasmic
CC reticulum retrograde transport carriers (By similarity).
CC {ECO:0000250|UniProtKB:O14495, ECO:0000250|UniProtKB:Q99JY8}.
CC -!- FUNCTION: Independently of this phosphatase activity may also function
CC in the Wnt signaling pathway and the stabilization of beta-
CC catenin/CTNNB1, thereby regulating cell proliferation, migration and
CC differentiation in angiogenesis or yet in tumor growth. Also plays a
CC role in integrin-mediated cell-cell adhesion in angiogenesis.
CC {ECO:0000250|UniProtKB:Q99JY8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-
CC glycerol + phosphate; Xref=Rhea:RHEA:27429, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608; EC=3.1.3.4;
CC Evidence={ECO:0000250|UniProtKB:O14495};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27430;
CC Evidence={ECO:0000250|UniProtKB:O14495};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphate + H2O = 1,2-
CC dihexadecanoyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:43236,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:72859,
CC ChEBI:CHEBI:82929; Evidence={ECO:0000250|UniProtKB:O14495};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43237;
CC Evidence={ECO:0000250|UniProtKB:O14495};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1,2-
CC di-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:43244,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:52333,
CC ChEBI:CHEBI:74546; Evidence={ECO:0000250|UniProtKB:O14495};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43245;
CC Evidence={ECO:0000250|UniProtKB:O14495};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + monoacyl-sn-glycero-3-phosphate = a monoacylglycerol +
CC phosphate; Xref=Rhea:RHEA:46736, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17408, ChEBI:CHEBI:43474, ChEBI:CHEBI:77589;
CC Evidence={ECO:0000250|UniProtKB:O14495};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46737;
CC Evidence={ECO:0000250|UniProtKB:O14495};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-sn-glycero-3-phosphate + H2O = (9Z-
CC octadecenoyl)-glycerol + phosphate; Xref=Rhea:RHEA:50884,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:75937,
CC ChEBI:CHEBI:84973; Evidence={ECO:0000250|UniProtKB:O14495};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50885;
CC Evidence={ECO:0000250|UniProtKB:O14495};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + sphing-4-enine 1-phosphate = phosphate + sphing-4-enine;
CC Xref=Rhea:RHEA:27518, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57756, ChEBI:CHEBI:60119;
CC Evidence={ECO:0000250|UniProtKB:O14495};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27519;
CC Evidence={ECO:0000250|UniProtKB:O14495};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylsphing-4-enine 1-phosphate + H2O = an N-acylsphing-4-
CC enine + phosphate; Xref=Rhea:RHEA:33743, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:52639, ChEBI:CHEBI:57674;
CC Evidence={ECO:0000250|UniProtKB:O14495};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33744;
CC Evidence={ECO:0000250|UniProtKB:O14495};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(octanoyl)-sphing-4-enine-1-phosphate = N-
CC octanoylsphing-4-enine + phosphate; Xref=Rhea:RHEA:62040,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:45815,
CC ChEBI:CHEBI:85376; Evidence={ECO:0000250|UniProtKB:O14495};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62041;
CC Evidence={ECO:0000250|UniProtKB:O14495};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(9Z-octadecenoyl)-ethanolamine phosphate = N-(9Z-
CC octadecenoyl) ethanolamine + phosphate; Xref=Rhea:RHEA:62160,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:71466,
CC ChEBI:CHEBI:145465; Evidence={ECO:0000250|UniProtKB:O14495};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62161;
CC Evidence={ECO:0000250|UniProtKB:O14495};
CC -!- ACTIVITY REGULATION: Magnesium-independent phospholipid phosphatase.
CC Insensitive to N-ethylmaleimide. Inhibited by sphingosine, zinc ions
CC and modestly by propanolol. {ECO:0000250|UniProtKB:O14495}.
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000250|UniProtKB:O14495}.
CC -!- SUBUNIT: Forms functional homodimers and homooligomers that are not
CC required for substrate recognition and catalytic activity. Can also
CC form heterooligomers with other PLPP2 and PLPP3. Interacts with CTNND1;
CC negatively regulates the PLPP3-mediated stabilization of beta-
CC catenin/CTNNB1. {ECO:0000250|UniProtKB:O14495}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O14495};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P97544}. Basolateral
CC cell membrane {ECO:0000250|UniProtKB:O14495}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P97544}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O14495}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P97544}. Endoplasmic reticulum-Golgi
CC intermediate compartment membrane {ECO:0000250|UniProtKB:O14495};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P97544}. Golgi
CC apparatus membrane {ECO:0000250|UniProtKB:O14495}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P97544}. Golgi apparatus, trans-Golgi
CC network membrane {ECO:0000250|UniProtKB:O14495}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P97544}. Membrane raft
CC {ECO:0000250|UniProtKB:O14495}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P97544}. Note=Cycles between the endoplasmic
CC reticulum and the Golgi. {ECO:0000250|UniProtKB:O14495}.
CC -!- DOMAIN: The integrin-binding motif mediates the binding to integrin
CC alpha-5/beta-1 (ITGA5:ITGB1) and integrin alpha-V/beta-3 (ITGAV:ITGB3)
CC and is required for the function in integrin-mediated cell-cell
CC adhesion. {ECO:0000250|UniProtKB:O14495}.
CC -!- DOMAIN: The dityrosine basolateral targeting motif mediates
CC localization to the basolateral membrane in polarized cells.
CC {ECO:0000250|UniProtKB:O14495}.
CC -!- PTM: N-glycosylated. Contains high-mannose oligosaccharides.
CC {ECO:0000250|UniProtKB:O14495}.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000305}.
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DR EMBL; BC102920; AAI02921.1; -; mRNA.
DR RefSeq; NP_001069941.1; NM_001076473.2.
DR AlphaFoldDB; Q3SZE3; -.
DR STRING; 9913.ENSBTAP00000015460; -.
DR PaxDb; Q3SZE3; -.
DR PRIDE; Q3SZE3; -.
DR Ensembl; ENSBTAT00000015460; ENSBTAP00000015460; ENSBTAG00000011640.
DR GeneID; 617707; -.
DR KEGG; bta:617707; -.
DR CTD; 8613; -.
DR VEuPathDB; HostDB:ENSBTAG00000011640; -.
DR VGNC; VGNC:33046; PLPP3.
DR eggNOG; KOG3030; Eukaryota.
DR GeneTree; ENSGT00940000156450; -.
DR HOGENOM; CLU_021458_3_0_1; -.
DR InParanoid; Q3SZE3; -.
DR OMA; FTMLYLV; -.
DR OrthoDB; 1621899at2759; -.
DR TreeFam; TF316040; -.
DR Reactome; R-BTA-1660661; Sphingolipid de novo biosynthesis.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000011640; Expressed in fornix of vagina and 105 other tissues.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0106235; F:ceramide-1-phosphate phosphatase activity; ISS:UniProtKB.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR GO; GO:0042577; F:lipid phosphatase activity; IBA:GO_Central.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; ISS:UniProtKB.
DR GO; GO:0042392; F:sphingosine-1-phosphate phosphatase activity; ISS:UniProtKB.
DR GO; GO:0060020; P:Bergmann glial cell differentiation; IEA:Ensembl.
DR GO; GO:0001568; P:blood vessel development; IEA:Ensembl.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0033631; P:cell-cell adhesion mediated by integrin; ISS:UniProtKB.
DR GO; GO:0006672; P:ceramide metabolic process; ISS:UniProtKB.
DR GO; GO:0001702; P:gastrulation with mouth forming second; IEA:Ensembl.
DR GO; GO:0034109; P:homotypic cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0046839; P:phospholipid dephosphorylation; ISS:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; ISS:UniProtKB.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IEA:Ensembl.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:1902068; P:regulation of sphingolipid mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0030111; P:regulation of Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0006670; P:sphingosine metabolic process; ISS:UniProtKB.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR InterPro; IPR028675; LPP3.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR InterPro; IPR043216; PA_PP_rel.
DR PANTHER; PTHR10165; PTHR10165; 1.
DR PANTHER; PTHR10165:SF79; PTHR10165:SF79; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Hydrolase; Lipid metabolism; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..311
FT /note="Phospholipid phosphatase 3"
FT /id="PRO_0000286942"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..85
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..194
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 227..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..258
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 149..157
FT /note="Phosphatase sequence motif I"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT REGION 197..200
FT /note="Phosphatase sequence motif II"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT REGION 245..256
FT /note="Phosphatase sequence motif III"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT REGION 276..311
FT /note="Mediates interaction with CTNND1"
FT /evidence="ECO:0000250|UniProtKB:O14495"
FT MOTIF 109..110
FT /note="Dityrosine basolateral targeting motif"
FT /evidence="ECO:0000250|UniProtKB:O14495"
FT MOTIF 183..185
FT /note="Integrin-binding motif"
FT /evidence="ECO:0000250|UniProtKB:O14495"
FT ACT_SITE 200
FT /note="Proton donors"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT ACT_SITE 252
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT SITE 256
FT /note="Stabilizes the active site histidine for
FT nucleophilic attack"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14495"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 311 AA; 35033 MW; B365EECCA46CFE97 CRC64;
MQNYKYDKAI VAESKNGGSP ALNNNPRKGG SKRVLLICLD LFCLFMAGLP FIIIETSTIK
PYHRGFYCND ESIKYPQKTG ETINDAVLTA VGIVIAILAI ITGEFYRIYY LKEKSRSTIQ
NPYVAALYKQ VGCFLFGCAI SQSFTDIAKV SIGRLRPHFL NVCNPDFSQI NCSVGYIQNY
RCRGEDSKVQ EARKSFFSGH ASFSMYTMLY LVLYLQARFT WRGARLLRPL LQFTLIMMAF
YTGLSRVSDH KHHPSDVLAG FAQGALVACC IVFFVSDLFK TKTTLSLPPS AIRKDMLSPV
DIDRSNHHNM V
