PLPR2_MOUSE
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 03-AUG-2022, entry version 129.
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},
GN Prg4 {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_659184.1; NM_144935.1. [Q8VCY8-1]
DR RefSeq; XP_006510250.1; XM_006510187.3. [Q8VCY8-1]
DR AlphaFoldDB; Q8VCY8; -.
DR IntAct; Q8VCY8; 1.
DR MINT; Q8VCY8; -.
DR STRING; 10090.ENSMUSP00000038616; -.
DR GlyGen; Q8VCY8; 1 site.
DR iPTMnet; Q8VCY8; -.
DR PhosphoSitePlus; Q8VCY8; -.
DR SwissPalm; Q8VCY8; -.
DR MaxQB; Q8VCY8; -.
DR PaxDb; Q8VCY8; -.
DR PRIDE; Q8VCY8; -.
DR ProteomicsDB; 288260; -. [Q8VCY8-1]
DR ProteomicsDB; 288261; -. [Q8VCY8-2]
DR Antibodypedia; 25796; 100 antibodies from 23 providers.
DR DNASU; 235044; -.
DR Ensembl; ENSMUST00000046371; ENSMUSP00000038616; ENSMUSG00000040563. [Q8VCY8-2]
DR Ensembl; ENSMUST00000190387; ENSMUSP00000139727; ENSMUSG00000040563. [Q8VCY8-1]
DR GeneID; 235044; -.
DR KEGG; mmu:235044; -.
DR UCSC; uc009ona.2; mouse. [Q8VCY8-2]
DR UCSC; uc009onb.1; mouse. [Q8VCY8-1]
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 OMA; NAYIQPF; -.
DR OrthoDB; 1621899at2759; -.
DR PhylomeDB; Q8VCY8; -.
DR TreeFam; TF316040; -.
DR BioGRID-ORCS; 235044; 5 hits in 56 CRISPR screens.
DR ChiTaRS; Plppr2; mouse.
DR PRO; PR:Q8VCY8; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8VCY8; protein.
DR Bgee; ENSMUSG00000040563; Expressed in subiculum and 179 other tissues.
DR ExpressionAtlas; Q8VCY8; baseline and differential.
DR Genevisible; Q8VCY8; MM.
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 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 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
