PLPR1_MOUSE
ID PLPR1_MOUSE Reviewed; 325 AA.
AC Q8BFZ2; Q4V9R3; Q5DTF2; Q8BID2; Q8BIQ1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Phospholipid phosphatase-related protein type 1 {ECO:0000250|UniProtKB:Q8TBJ4};
DE AltName: Full=Inactive 2-lysophosphatidate phosphatase PLPPR1 {ECO:0000250|UniProtKB:Q6WAY2};
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|MGI:MGI:2445015};
GN Synonyms=Kiaa4247 {ECO:0000303|Ref.2},
GN Lppr1 {ECO:0000250|UniProtKB:Q8TBJ4}, Prg3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Brain cortex, Corpus striatum, Diencephalon, and Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=CD-1; TISSUE=Neural stem cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May play a role in neurite outgrowth and neurogenesis.
CC {ECO:0000250|UniProtKB:Q6WAY2}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6WAY2};
CC Multi-pass membrane protein {ECO:0000255}. Cell projection, neuron
CC projection {ECO:0000250|UniProtKB:Q6WAY2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BFZ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BFZ2-2; Sequence=VSP_031009;
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:0000250|UniProtKB:Q6WAY2}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90332.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY345342; AAR09144.1; -; mRNA.
DR EMBL; AK220568; BAD90332.1; ALT_INIT; mRNA.
DR EMBL; AK034251; BAC28649.1; -; mRNA.
DR EMBL; AK043762; BAC31647.1; -; mRNA.
DR EMBL; AK047614; BAC33101.1; -; mRNA.
DR EMBL; AK087439; BAC39874.1; -; mRNA.
DR EMBL; AK087514; BAC39907.1; -; mRNA.
DR EMBL; AK160897; BAE36076.1; -; mRNA.
DR EMBL; AL808138; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL928612; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX537352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC096762; AAH96762.1; -; mRNA.
DR CCDS; CCDS18170.1; -. [Q8BFZ2-1]
DR RefSeq; NP_848871.1; NM_178756.4. [Q8BFZ2-1]
DR RefSeq; XP_006538031.1; XM_006537968.3. [Q8BFZ2-1]
DR RefSeq; XP_011248351.1; XM_011250049.2. [Q8BFZ2-1]
DR RefSeq; XP_017175739.1; XM_017320250.1. [Q8BFZ2-1]
DR AlphaFoldDB; Q8BFZ2; -.
DR STRING; 10090.ENSMUSP00000075966; -.
DR GlyGen; Q8BFZ2; 3 sites.
DR iPTMnet; Q8BFZ2; -.
DR PhosphoSitePlus; Q8BFZ2; -.
DR SwissPalm; Q8BFZ2; -.
DR MaxQB; Q8BFZ2; -.
DR PaxDb; Q8BFZ2; -.
DR PRIDE; Q8BFZ2; -.
DR ProteomicsDB; 288258; -. [Q8BFZ2-1]
DR ProteomicsDB; 288259; -. [Q8BFZ2-2]
DR Antibodypedia; 14633; 46 antibodies from 10 providers.
DR DNASU; 272031; -.
DR Ensembl; ENSMUST00000076670; ENSMUSP00000075966; ENSMUSG00000063446. [Q8BFZ2-1]
DR GeneID; 272031; -.
DR KEGG; mmu:272031; -.
DR UCSC; uc008svp.1; mouse. [Q8BFZ2-1]
DR UCSC; uc012dea.1; mouse. [Q8BFZ2-2]
DR CTD; 54886; -.
DR MGI; MGI:2445015; Plppr1.
DR VEuPathDB; HostDB:ENSMUSG00000063446; -.
DR eggNOG; KOG3030; Eukaryota.
DR GeneTree; ENSGT00940000158875; -.
DR HOGENOM; CLU_021458_1_0_1; -.
DR InParanoid; Q8BFZ2; -.
DR OMA; GEISMYV; -.
DR OrthoDB; 1621899at2759; -.
DR PhylomeDB; Q8BFZ2; -.
DR TreeFam; TF316040; -.
DR BioGRID-ORCS; 272031; 3 hits in 40 CRISPR screens.
DR ChiTaRS; Plppr1; mouse.
DR PRO; PR:Q8BFZ2; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8BFZ2; protein.
DR Bgee; ENSMUSG00000063446; Expressed in layer of neocortex and 83 other tissues.
DR Genevisible; Q8BFZ2; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS: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; ISS:UniProtKB.
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; 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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Glycoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..325
FT /note="Phospholipid phosphatase-related protein type 1"
FT /id="PRO_0000317533"
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..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..247
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:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
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"
FT VAR_SEQ 129..158
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031009"
FT CONFLICT 58
FT /note="P -> L (in Ref. 5; AAH96762)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="E -> G (in Ref. 3; BAC39874)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 325 AA; 35932 MW; DB884AEAFB759094 CRC64;
MAVENNTQRS YSIIPCFIFV ELVIMAGTVL LAYYFECTDT FQVHIQGFFC QDGDLMKPYP
GTEEESFISP LVLYCVLAAT PTAIIFIGEI SMYFIKSTRE SLIAEEKMIL TGDCCYLSPL
LRRIIRFIGV FAFGLFATDI FVNAGQVVTG HLTPYFLTVC QPNYTSTDCR AHQQFINNGN
ICTGDLEVIE KARRSFPSKH AALSIYSALY ATMYITSTIK TKSSRLAKPV LCLGTLCTAF
LTGLNRVSEY RNHCSDVIAG FILGTAVALF LGMCVVHNFR GTQGSPSKPK PEDPRGVPLM
AFPRIESPLE TLSAQNHSAS MTEVT
