PLPR1_RAT
ID PLPR1_RAT Reviewed; 325 AA.
AC Q6WAY2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Phospholipid phosphatase-related protein type 1 {ECO:0000250|UniProtKB:Q8TBJ4};
DE AltName: Full=Inactive 2-lysophosphatidate phosphatase PLPPR1 {ECO:0000305|PubMed:14750979};
DE AltName: Full=Lipid phosphate phosphatase-related protein type 1 {ECO:0000250|UniProtKB:Q8TBJ4};
DE AltName: Full=Plasticity-related gene 3 protein {ECO:0000305|PubMed:14750979};
DE Short=PRG-3 {ECO:0000303|PubMed:14750979};
GN Name=Plppr1 {ECO:0000312|RGD:1303116};
GN Synonyms=Lppr1 {ECO:0000250|UniProtKB:Q8TBJ4}, Prg3;
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, INDUCTION, AND CAUTION.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
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).
CC -!- FUNCTION: May play a role in neurite outgrowth and neurogenesis.
CC {ECO:0000269|PubMed:14750979}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14750979};
CC Multi-pass membrane protein {ECO:0000255}. Cell projection, neuron
CC projection {ECO:0000269|PubMed:14750979}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the brain. Also found in the
CC liver, kidney and testis. In the brain shows a strongest expression in
CC the hippocampus and cerebellum. {ECO:0000269|PubMed:14750979}.
CC -!- DEVELOPMENTAL STAGE: At embryonic day 16 (E16) can be detected in the
CC hippocampal anlage, thalamus, cortex and olfactory bulb. At perinatal
CC stages (E20-postnatal day 1) shows a strong expression in the cortex
CC and hippocampus and subsequently declines at later postnatal stages.
CC {ECO:0000269|PubMed:14750979}.
CC -!- INDUCTION: Shows a transient down-regulation due to overexcitation of
CC neurons induced by kainic acid. {ECO:0000269|PubMed:14750979}.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000305}.
CC -!- CAUTION: Has no 2-lysophosphatidate/LPA phosphatase activity. This is
CC supported by the fact that the phosphatase sequence motifs as well as
CC the His residue acting as a nucleophile in active phosphatases of the
CC PA-phosphatase related phosphoesterase family are not conserved.
CC {ECO:0000305|PubMed:14750979}.
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DR EMBL; AY299399; AAQ72924.1; -; mRNA.
DR RefSeq; NP_958428.1; NM_201271.1.
DR AlphaFoldDB; Q6WAY2; -.
DR STRING; 10116.ENSRNOP00000009987; -.
DR GlyGen; Q6WAY2; 3 sites.
DR PaxDb; Q6WAY2; -.
DR PRIDE; Q6WAY2; -.
DR GeneID; 298062; -.
DR KEGG; rno:298062; -.
DR UCSC; RGD:1303116; rat.
DR CTD; 54886; -.
DR RGD; 1303116; Plppr1.
DR eggNOG; KOG3030; Eukaryota.
DR InParanoid; Q6WAY2; -.
DR OrthoDB; 1621899at2759; -.
DR PhylomeDB; Q6WAY2; -.
DR PRO; PR:Q6WAY2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
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:0007399; P:nervous system development; IMP:RGD.
DR GO; GO:0006644; P:phospholipid metabolic process; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR028678; LPPR1.
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:SF41; PTHR10165:SF41; 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; Cell projection; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..325
FT /note="Phospholipid phosphatase-related protein type 1"
FT /id="PRO_0000317534"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BFZ2"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 325 AA; 35887 MW; 65889682D16D242B CRC64;
MAVENNTQRS YSIIPCFIFV ELVIMAGTVL LAYYFECTDT FQVHIQGFFC QDGDLMKPYP
GTEEESFISP LVLYCVLAAT PTAIIFIGEI SMYFIKSTRE SLIAEEKMIL TGDCCYLSPL
LRRIVRFIGV FAFGLFATDI FVNAGQVVTG HLTPYFLTVC QPNYTSTDCR AHHQFINNGN
ICTGDLEVIE KARRSFPSKH AALSIYSALY ATMYITSTIK TKSSRLAKPV LCLGDLCTAF
LTGLNRVSEY RNHCSDVIAG FILGTAVALF LGMCVVHNFK GTQGSASKPK PEDPRGVPLM
AFPRIESPLE TLSAQNHSAS MTEVT
