ID   PLPR2_MOUSE             Reviewed;         343 AA.
AC   Q8VCY8; Q8BIE4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   04-NOV-2026, entry version 148.
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|MGI:MGI:2384575};
GN   Synonyms=Lppr2 {ECO:0000250|UniProtKB:Q96GM1}, Prg4
GN   {ECO:0000303|PubMed:14750979};
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).
RC   STRAIN=C57BL/6J; 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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Eye;
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299 AND SER-312,
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441 (ISOFORM 2), AND
RP   IDENTIFICATION BY 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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8VCY8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VCY8-2; Sequence=VSP_031012;
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; AY438023; AAR98841.1; -; mRNA.
DR   EMBL; AK082453; BAC38494.1; -; mRNA.
DR   EMBL; BC018242; AAH18242.1; -; mRNA.
DR   EMBL; BC023082; AAH23082.1; -; mRNA.
DR   CCDS; CCDS72203.1; -. [Q8VCY8-2]
DR   CCDS; CCDS80966.1; -. [Q8VCY8-1]
DR   RefSeq; NP_001277228.1; NM_001290299.1. [Q8VCY8-2]
DR   RefSeq; NP_001397526.1; NM_001410597.1. [Q8VCY8-1]
DR   RefSeq; NP_659184.1; NM_144935.1. [Q8VCY8-1]
DR   AlphaFoldDB; Q8VCY8; -.
DR   SMR; Q8VCY8; -.
DR   BioGRID; 231614; 4.
DR   FunCoup; Q8VCY8; 127.
DR   IntAct; Q8VCY8; 1.
DR   STRING; 10090.ENSMUSP00000038616; -.
DR   GlyCosmos; Q8VCY8; 1 site, No reported glycans.
DR   GlyGen; Q8VCY8; 1 site, 1 N-linked glycan (1 site).
DR   iPTMnet; Q8VCY8; -.
DR   PhosphoSitePlus; Q8VCY8; -.
DR   SwissPalm; Q8VCY8; -.
DR   PaxDb; 10090-ENSMUSP00000038616; -.
DR   ProteomicsDB; 288260; -. [Q8VCY8-1]
DR   ProteomicsDB; 288261; -. [Q8VCY8-2]
DR   Antibodypedia; 25796; 99 antibodies from 23 providers.
DR   DNASU; 235044; -.
DR   Ensembl; ENSMPUT00000005573; ENSMPUP00000005481; ENSMPUG00000005523.
DR   Ensembl; ENSMUST00000046371.13; ENSMUSP00000038616.7; ENSMUSG00000040563.14. [Q8VCY8-2]
DR   Ensembl; ENSMUST00000190387.7; ENSMUSP00000139727.2; ENSMUSG00000040563.14. [Q8VCY8-1]
DR   GeneID; 235044; -.
DR   KEGG; mmu:235044; -.
DR   UCSC; uc009ona.2; mouse. [Q8VCY8-2]
DR   UCSC; uc009onb.1; mouse. [Q8VCY8-1]
DR   AGR; MGI:2384575; -.
DR   CTD; 64748; -.
DR   MGI; MGI:2384575; Plppr2.
DR   VEuPathDB; HostDB:ENSMUSG00000040563; -.
DR   eggNOG; KOG3030; Eukaryota.
DR   GeneTree; ENSGT00940000158145; -.
DR   HOGENOM; CLU_021458_1_1_1; -.
DR   InParanoid; Q8VCY8; -.
DR   OrthoDB; 69991at9989; -.
DR   PhylomeDB; Q8VCY8; -.
DR   Reactome; R-MMU-419408; Lysosphingolipid and LPA receptors.
DR   BioGRID-ORCS; 235044; 5 hits in 59 CRISPR screens.
DR   CD-CODE; CE726F99; Postsynaptic density.
DR   PRO; PR:Q8VCY8; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q8VCY8; protein.
DR   Bgee; ENSMUSG00000040563; Expressed in subiculum and 181 other cell types or tissues.
DR   ExpressionAtlas; Q8VCY8; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; 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   CDD; cd03384; PAP2_wunen; 1.
DR   FunFam; 1.20.144.10:FF:000006; Phospholipid phosphatase-related protein type 2 isoform X1; 1.
DR   Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR   InterPro; IPR043216; PAP-like.
DR   InterPro; IPR000326; PAP2/HPO.
DR   InterPro; IPR036938; PAP2/HPO_sf.
DR   PANTHER; PTHR10165; LIPID PHOSPHATE PHOSPHATASE; 1.
DR   PANTHER; PTHR10165:SF15; PHOSPHOLIPID PHOSPHATASE-RELATED PROTEIN TYPE 2; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Glycoprotein; Membrane; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..343
FT                   /note="Phospholipid phosphatase-related protein type 2"
FT                   /id="PRO_0000317539"
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   COMPBIAS        322..335
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         299
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         312
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CARBOHYD        165
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         317..343
FT                   /note="NPRPAGRIRHRHGSPHPSRRTVPAVAT -> LSVAQEPETCRPHSTPARLTP
FT                   SKPQNCARRGHLIPSCVSSRAPAMCSSPRVPRPRLRSEPTPLPLPLPLPAPTPSQGPSP
FT                   SSPGPGGPGGGGGRGRKLLLPTPLLRDLYTLSGLHPSPFHRDNFSPYLFASRDHLL
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_031012"
FT   MOD_RES         Q8VCY8-2:441
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
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
//