PLPR3_RAT
ID PLPR3_RAT Reviewed; 716 AA.
AC Q7TMB0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 95.
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|RGD:727823};
GN Synonyms=Lppr3 {ECO:0000250|UniProtKB:Q6T4P5},
GN Prg2 {ECO:0000250|UniProtKB:Q6T4P5};
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].
RC STRAIN=Sprague-Dawley, and Wistar; 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).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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; AY147866; AAN37411.1; -; mRNA.
DR EMBL; AY300027; AAP57099.1; -; mRNA.
DR AlphaFoldDB; Q7TMB0; -.
DR STRING; 10116.ENSRNOP00000029601; -.
DR GlyGen; Q7TMB0; 2 sites.
DR iPTMnet; Q7TMB0; -.
DR PhosphoSitePlus; Q7TMB0; -.
DR SwissPalm; Q7TMB0; -.
DR PaxDb; Q7TMB0; -.
DR PRIDE; Q7TMB0; -.
DR UCSC; RGD:727823; rat.
DR RGD; 727823; Plppr3.
DR eggNOG; KOG3030; Eukaryota.
DR InParanoid; Q7TMB0; -.
DR PhylomeDB; Q7TMB0; -.
DR PRO; PR:Q7TMB0; -.
DR Proteomes; UP000002494; Unplaced.
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 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..716
FT /note="Phospholipid phosphatase-related protein type 3"
FT /id="PRO_0000317531"
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..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..488
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 664..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..461
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:0000250|UniProtKB:Q7TPB0"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TPB0"
FT MOD_RES 374
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7TPB0"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TPB0"
FT MOD_RES 506
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TPB0"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TPB0"
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"
SQ SEQUENCE 716 AA; 76786 MW; 9440C6F2DC76CE36 CRC64;
MIAKKEKNKT PKDSMTLLPC FYFVELPIVA SSVVSLYFLE LTDLFQPAKV GFQCHDRSLS
MPYVETNEEL IPLLMLLSLA FAAPAASIMV GEGMVYCLQS RLWGRGPGGV EGSINAGGCN
FNSFLRRTVR FVGVHVFGLC ATALVTDVIQ LATGYHTPFF LTVCKPNYTL LGTSCEANPY
ITQDICSGHD THAILSARKT FPSQHATLSA FAAVYVSMYF NSVISDATKL LKPILVFAFA
IAAGVCGLTQ ITQYRSHPVD VYAGFLIGAG IAAYLACHAV GNFQAPPAEK VPTPAPAKDA
LRVLTQRGHE SMYQQNKSVS TDELGPPGRL EGVPRPVARE KTSLGSLKRA SVDVDLLAPR
SPMGKEGMVT FSNTLPRVST PSLDDPSRRH MTIHVPLDAS RSRQLISEWK QKSLEGRGLG
LPDEASPAHL RAPAEQVAEE EEEEEEEEEE EEEEEEEEEG PVPPSLYPTV QARPGLGPRV
ILPPRPGPQP LIHIPEEVVQ AGAGLSPKSS ASVRAKWLSM VEKGGGPVAV APPQPRVANP
PRLLQVIAMS KAAGGPKAET ASSSSASSDS SQYRSPSDRD SASIVTIDAH APHHPVVHLS
AGSTPWEWKA KVVEGEGGYE LGDLARGFRS SCKQPGIGPG SPVSDVDQEE PRFGAVATVN
LATGEGLPPP GASEGALGAG SRESTLRRQV GALGEREVEA EAESYYRRMQ ARRYQD
