PLPR3_MOUSE
ID PLPR3_MOUSE Reviewed; 716 AA.
AC Q7TPB0; Q4V781; Q68FN2; Q6NZQ9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Phospholipid phosphatase-related protein type 3 {ECO:0000250|UniProtKB:Q6T4P5};
DE AltName: Full=Inactive phospholipid phosphatase PLPPR3 {ECO:0000250|UniProtKB:Q6WAY2};
DE AltName: Full=Lipid phosphate phosphatase-related protein type 3 {ECO:0000250|UniProtKB:Q6T4P5};
DE AltName: Full=Plasticity-related gene 2 protein {ECO:0000305|PubMed:12730698};
DE Short=PRG-2 {ECO:0000303|PubMed:12730698};
GN Name=Plppr3 {ECO:0000312|MGI:MGI:2388640};
GN Synonyms=Kiaa4076, Lppr3 {ECO:0000250|UniProtKB:Q6T4P5},
GN Prg2 {ECO:0000250|UniProtKB:Q6T4P5};
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=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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320; SER-351; THR-374;
RP SER-426; SER-505 AND SER-641, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7TPB0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TPB0-2; Sequence=VSP_031007, VSP_031008;
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; AF541278; AAP57767.1; -; mRNA.
DR EMBL; BC066006; AAH66006.1; -; mRNA.
DR EMBL; BC079534; AAH79534.1; -; mRNA.
DR EMBL; BC098099; AAH98099.1; -; mRNA.
DR CCDS; CCDS35971.1; -. [Q7TPB0-1]
DR RefSeq; NP_001164406.1; NM_001170935.1.
DR RefSeq; NP_859009.2; NM_181681.2.
DR RefSeq; XP_006513549.1; XM_006513486.3.
DR AlphaFoldDB; Q7TPB0; -.
DR BioGRID; 229708; 5.
DR STRING; 10090.ENSMUSP00000089979; -.
DR GlyGen; Q7TPB0; 2 sites.
DR iPTMnet; Q7TPB0; -.
DR PhosphoSitePlus; Q7TPB0; -.
DR SwissPalm; Q7TPB0; -.
DR MaxQB; Q7TPB0; -.
DR PaxDb; Q7TPB0; -.
DR PeptideAtlas; Q7TPB0; -.
DR PRIDE; Q7TPB0; -.
DR ProteomicsDB; 288262; -. [Q7TPB0-1]
DR ProteomicsDB; 288263; -. [Q7TPB0-2]
DR DNASU; 216152; -.
DR GeneID; 216152; -.
DR KEGG; mmu:216152; -.
DR UCSC; uc007gaf.1; mouse. [Q7TPB0-1]
DR CTD; 79948; -.
DR MGI; MGI:2388640; Plppr3.
DR eggNOG; KOG3030; Eukaryota.
DR InParanoid; Q7TPB0; -.
DR OrthoDB; 1621899at2759; -.
DR PhylomeDB; Q7TPB0; -.
DR TreeFam; TF316040; -.
DR BioGRID-ORCS; 216152; 3 hits in 40 CRISPR screens.
DR ChiTaRS; Plppr3; mouse.
DR PRO; PR:Q7TPB0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q7TPB0; protein.
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; IPR028685; LPPR3.
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:SF14; PTHR10165:SF14; 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..716
FT /note="Phospholipid phosphatase-related protein type 3"
FT /id="PRO_0000317530"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 311..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..460
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 374
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 167
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 408..463
FT /note="EWKQKSLEGRGLGLPDEASPVHLRAPAEQVAEEEEEEEEEEEEEEEEEEEEG
FT PVPP -> SSPAAHHRRRLGNPGNNRKQKNRAVSWQRNSGSGKKKKWEGRGGKKKVAKH
FT RSVNT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031007"
FT VAR_SEQ 464..716
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031008"
FT CONFLICT 520
FT /note="V -> M (in Ref. 2; AAH66006/AAH79534)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 716 AA; 76693 MW; 86605748DED3F5B6 CRC64;
MLAMKEKNKT PKDSMTLLPC FYFVELPIVA SSIVSLYFLE LTDLFKPAKV GFQCYDRALS
MPYVETNEEL IPLLMLLSLA FAAPAASIMV GEGMVYCLQS RLWGRGPGGV EGSINAGGCN
FNSFLRRTVR FVGVHVFGLC ATALVTDVIQ LATGYHTPFF LTVCKPNYTL LGTSCESNPY
ITQDICSGHD THAILSARKT FPSQHATLSA FAAVYVSMYF NAVISDTTKL LKPILVFAFA
IAAGVCGLTQ ITQYRSHPVD VYAGFLIGAG IAAYLACHAV GNFQAPPAEK VPTPAPAKDA
LRALTQRGHE SMYQQNKSVS TDELGPPGRL EGVPRPVARE KTSLGSLKRA SVDVDLLAPR
SPMGKEGMVT FSNTLPRVST PSLDDPARRH MTIHVPLDAS RSRQLIGEWK QKSLEGRGLG
LPDEASPVHL RAPAEQVAEE EEEEEEEEEE EEEEEEEEGP VPPSLYPTVQ ARPGLGPRVI
LPPRPGPQPL VHIPEEGVQA GAGLSPKSSS SSVRAKWLSV AEKGGGPVAV APSQPRVANP
PRLLQVIAMS KAAGGPKAET ASSSSASSDS SQYRSPSDRD SASIVTIDAH APHHPVVHLS
AGSTPWEWKA KVVEGEGSYE LGDLARGFRS SCKQPGMGPG SPVSDVDQEE PRFGAVATVN
LATGEGLPPP GASEGALGAG SRESTLRRQV GGLAEREVEA EAESYYRRMQ ARRYQD
