ID   PLPR2_RAT               Reviewed;         343 AA.
AC   Q6W5G4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Phospholipid phosphatase-related protein type 2 {ECO:0000250|UniProtKB:Q96GM1};
DE   AltName: Full=Inactive phospholipid phosphatase PLPPR2 {ECO:0000250|UniProtKB:Q6WAY2};
DE   AltName: Full=Lipid phosphate phosphatase-related protein type 2 {ECO:0000250|UniProtKB:Q96GM1};
DE   AltName: Full=Plasticity-related gene 4 protein {ECO:0000305|PubMed:14750979};
DE            Short=PRG-4 {ECO:0000303|PubMed:14750979};
GN   Name=Plppr2 {ECO:0000312|RGD:1597171};
GN   Synonyms=Lppr2 {ECO:0000250|UniProtKB:Q96GM1},
GN   Prg4 {ECO:0000250|UniProtKB:Q8VCY8};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Hippocampus;
RX   PubMed=14750979; DOI=10.1046/j.1460-9568.2003.03078.x;
RA   Savaskan N.E., Brauer A.U., Nitsch R.;
RT   "Molecular cloning and expression regulation of PRG-3, a new member of the
RT   plasticity-related gene family.";
RL   Eur. J. Neurosci. 19:212-220(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family. {ECO:0000305}.
CC   -!- CAUTION: Has most probably no phospholipid phosphatase activity (By
CC       similarity). This is supported by the fact that the phosphatase
CC       sequence motifs as well as the His residue acting as a nucleophile in
CC       active phosphatases of the PA-phosphatase related phosphoesterase
CC       family are not conserved (By similarity).
CC       {ECO:0000250|UniProtKB:Q6WAY2}.
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DR   EMBL; AY310911; AAQ76703.1; -; mRNA.
DR   AlphaFoldDB; Q6W5G4; -.
DR   STRING; 10116.ENSRNOP00000016790; -.
DR   GlyGen; Q6W5G4; 1 site.
DR   iPTMnet; Q6W5G4; -.
DR   PaxDb; Q6W5G4; -.
DR   PRIDE; Q6W5G4; -.
DR   UCSC; RGD:1597171; rat.
DR   RGD; 1597171; Plppr2.
DR   eggNOG; KOG3030; Eukaryota.
DR   InParanoid; Q6W5G4; -.
DR   PhylomeDB; Q6W5G4; -.
DR   PRO; PR:Q6W5G4; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0042577; F:lipid phosphatase activity; IBA:GO_Central.
DR   GO; GO:0008195; F:phosphatidate phosphatase activity; IBA:GO_Central.
DR   GO; GO:0046839; P:phospholipid dephosphorylation; IBA:GO_Central.
DR   GO; GO:0006644; P:phospholipid metabolic process; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   InterPro; IPR028679; LPPR2.
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:SF15; PTHR10165:SF15; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; SSF48317; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..343
FT                   /note="Phospholipid phosphatase-related protein type 2"
FT                   /id="PRO_0000317540"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        129..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        239..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        266..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          291..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         299
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VCY8"
FT   MOD_RES         312
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CARBOHYD        165
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   343 AA;  36936 MW;  DE2F7F0F0F8215FD CRC64;
     MAGGRPHLKR SFSIIPCFVF VESVLLGIVV LLAYRLEFTD TFPVHTQGFF CYDSAYAKPY
     PGPEAASRAP PALIYALVTA GPTLTILLGE LARAFFPAPP SSSPVSGEST IVSGACCRFS
     PPLRRLVRFL GVYSFGLFTT TIFANAGQVV TGNPTPHFLS VCRPNYTALG CPPPSPDRPG
     PDRFVTDQSA CAGSPSLVAA ARRAFPCKDA ALCAYAVTYT AMYVTLVFRV KGSRLVKPSL
     CLALLCPAFL VGVVRVAEYR NHWSDVLAGF LTGAAIATFL VTCVVHNFQS RPHSGRRLSP
     WEDLSQAPTM DSPLEKNPRP AGRIRHRHGS PHPSRRTVPA VAT