PLPR4_RAT
ID PLPR4_RAT Reviewed; 766 AA.
AC Q7TMB7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Phospholipid phosphatase-related protein type 4 {ECO:0000305};
DE AltName: Full=Brain-specific phosphatidic acid phosphatase-like protein 1 {ECO:0000250|UniProtKB:Q7Z2D5};
DE AltName: Full=Inactive 2-lysophosphatidate phosphatase PLPPR4 {ECO:0000305|PubMed:15280885};
DE AltName: Full=Lipid phosphate phosphatase-related protein type 4 {ECO:0000250|UniProtKB:Q7Z2D5};
DE AltName: Full=Plasticity-related gene 1 protein {ECO:0000305|PubMed:12730698};
DE Short=PRG-1 {ECO:0000303|PubMed:12730698};
GN Name=Plppr4 {ECO:0000312|RGD:727806};
GN Synonyms=Lppr4 {ECO:0000250|UniProtKB:Q7Z2D5},
GN Php1 {ECO:0000250|UniProtKB:Q7Z2D5}, Prg1 {ECO:0000303|PubMed:12730698};
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND CAUTION.
RC STRAIN=Sprague-Dawley, and Wistar; TISSUE=Brain, and Testis;
RX PubMed=12730698; DOI=10.1038/nn1052;
RA Braeuer A.U., Savaskan N.E., Kuehn H., Prehn S., Ninnemann O., Nitsch R.;
RT "A new phospholipid phosphatase, PRG-1, is involved in axon growth and
RT regenerative sprouting.";
RL Nat. Neurosci. 6:572-578(2003).
RN [2]
RP CAUTION.
RX PubMed=15280885; DOI=10.1038/nn0804-789a;
RA McDermott M.I., Sigal Y.J., Sciorra V.A., Morris A.J.;
RT "Is PRG-1 a new lipid phosphatase?";
RL Nat. Neurosci. 7:789-789(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347; SER-386 AND SER-474, AND
RP IDENTIFICATION BY 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 -!- FUNCTION: Postsynaptic density membrane protein that indirectly
CC regulates glutamatergic synaptic transmission through lysophosphatidic
CC acid (LPA)-mediated signaling pathways. Binds lysophosphatidic acid
CC (LPA) and mediates its internalization into cells. Could act as
CC receptor or a transporter of this lipid at the post-synaptic membrane
CC (By similarity). Modulates lysophosphatidic acid (LPA) activity in
CC neuron axonal outgrowth during development by attenuating phospholipid-
CC induced axon collapse (PubMed:12730698). {ECO:0000250|UniProtKB:Q7TME0,
CC ECO:0000269|PubMed:12730698}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic density membrane
CC {ECO:0000305|PubMed:12730698}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in neurons (at protein
CC level). {ECO:0000269|PubMed:12730698}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the subventricular zone and
CC specifically in the hippocampal anlage at embryonic day 19 (E19). From
CC postnatal stages on, expressed in the hippocampus and in the entorhinal
CC cortex. In the dentate gyrus weakly expressed in the infrapyramidal
CC blade at P0 and at P5 expressed in the suprapyramidal blade. This
CC expression remains unchanged during maturation. A reduced expression is
CC seen in adult brain. {ECO:0000269|PubMed:12730698}.
CC -!- PTM: O-glycosylated. Probably at Ser-347.
CC {ECO:0000250|UniProtKB:Q7TME0}.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000305}.
CC -!- CAUTION: Originally described as a 2-lysophosphatidate/LPA phosphatase
CC (PubMed:12730698). However, following studies suggested it does not
CC have such activity or only a residual one (PubMed:15280885). This is
CC further supported by the fact that the phosphatase sequence motifs as
CC well as the His residue acting as a nucleophile in active phosphatases
CC of the PA-phosphatase related phosphoesterase family are not conserved
CC (PubMed:15280885). {ECO:0000269|PubMed:12730698,
CC ECO:0000269|PubMed:15280885}.
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DR EMBL; AY266268; AAP41101.1; -; mRNA.
DR EMBL; AF541280; AAP57769.1; -; mRNA.
DR AlphaFoldDB; Q7TMB7; -.
DR STRING; 10116.ENSRNOP00000022625; -.
DR SwissLipids; SLP:000000722; -.
DR GlyGen; Q7TMB7; 6 sites.
DR iPTMnet; Q7TMB7; -.
DR PhosphoSitePlus; Q7TMB7; -.
DR PaxDb; Q7TMB7; -.
DR PRIDE; Q7TMB7; -.
DR UCSC; RGD:727806; rat.
DR RGD; 727806; Plppr4.
DR eggNOG; KOG3030; Eukaryota.
DR InParanoid; Q7TMB7; -.
DR PhylomeDB; Q7TMB7; -.
DR Reactome; R-RNO-419408; Lysosphingolipid and LPA receptors.
DR PRO; PR:Q7TMB7; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:RGD.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:RGD.
DR GO; GO:0098839; C:postsynaptic density membrane; ISS:UniProtKB.
DR GO; GO:0042577; F:lipid phosphatase activity; IDA:RGD.
DR GO; GO:0052642; F:lysophosphatidic acid phosphatase activity; IMP:UniProtKB.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; IBA:GO_Central.
DR GO; GO:0007409; P:axonogenesis; IDA:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0048839; P:inner ear development; ISO:RGD.
DR GO; GO:0140354; P:lipid import into cell; ISS:UniProtKB.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0046839; P:phospholipid dephosphorylation; IDA:RGD.
DR GO; GO:0006644; P:phospholipid metabolic process; IBA:GO_Central.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR InterPro; IPR043216; PA_PP_rel.
DR InterPro; IPR028684; PLPPR4.
DR PANTHER; PTHR10165; PTHR10165; 1.
DR PANTHER; PTHR10165:SF13; PTHR10165:SF13; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Reference proteome; Synapse; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..766
FT /note="Phospholipid phosphatase-related protein type 4"
FT /id="PRO_0000317438"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 454..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TME0"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TME0"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TME0"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TME0"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 766 AA; 83362 MW; 7986E59DD4BC6C62 CRC64;
MQRAGSSGAR GECDISGTGR LRLEQAARLG GRAVHTSPTG GLGARQVAGM SAKERPKGKV
IKDSVTLLPC FYFVELPILA SSVVSLYFLE LTDVFKPVHS GFSCYDRSLS MPYIEPTQEA
IPFLMLLSLA FAGPAITIMV GEGILYCCLS KRRNGAGLEP NINAGGCNFN SFLRRAVRFV
GVHVVGLCST ALITDIIQLA TGYQAPYFLT VCKPMYTSLE GSCKENSYIV EEICSGSDLT
VINNGKKSFP SQHATLAAFA AVYVSMYFNS TLTDSSKLLK PLLVFTFIIC GIICGLTRIT
QYKNHPVDVY CGFLIGGGIA LYLGLYAVGN FLPSEDSMLQ HRDALRSLTD LNQDPSRVLS
AKNGSSGDGI AHTEGILNRN HRDASSLTNL KRANADVEII TPRSPMGKES MVTFSNTLPR
ANTPSVEDPV RRNASIHASM DSARSKQLLT QWKSKNESRK MSLQVMDSEP EGQSPPRSIE
MRSSSEPSRV GVNGDHHVPG NQYLKIQPGT VPGCNNSMPA GPRVSIQSRP GSSQLVHIPE
ETQENISTSP KSSSARAKWL KAAEKTVACN RGNNQPRIMQ VIAMSKQQGV LQSSPKNAEG
STVTCTGSIR YKTLTDHEPS GIVRVEAHPE NNRPIIQIPS STEGEGSGSW KWKAPEKSSL
RQTYELNDLN RDSESCESLK DSFGSGDRKR KHIDSNEHHH HGITTIRVTP VEGSEIGSET
LSVSSSRDST LRRKGNIILI PERSNSPENT RNIFYKGTSP TRPYKD
