PLPR3_HUMAN
ID PLPR3_HUMAN Reviewed; 718 AA.
AC Q6T4P5; Q86XQ4; Q96EH1; Q9BQF9; Q9HAJ4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Phospholipid phosphatase-related protein type 3 {ECO:0000305};
DE AltName: Full=Inactive phospholipid phosphatase PLPPR3 {ECO:0000250|UniProtKB:Q6WAY2};
DE AltName: Full=Lipid phosphate phosphatase-related protein type 3 {ECO:0000303|Ref.3};
DE AltName: Full=PAP-2-like protein 2 {ECO:0000303|Ref.2};
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|HGNC:HGNC:23497};
GN Synonyms=LPPR3 {ECO:0000303|Ref.3}, PHP2 {ECO:0000303|Ref.2},
GN PRG2 {ECO:0000312|HGNC:HGNC:23497};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC 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 [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RA Ninnemann O., Braeuer A.U., Savaskan N., Nitsch R.;
RT "A new brain specific member of the PAP-2 family.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Morris A.J., Sigal Y.J., McDermott M., Sciorra V.A.;
RT "Lipid phosphate phosphatase related proteins.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Amygdala;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Embryo;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 116-416 (ISOFORM 1).
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).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=PRG-2a;
CC IsoId=Q6T4P5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6T4P5-2; Sequence=VSP_031005;
CC Name=3; Synonyms=PRG-2b;
CC IsoId=Q6T4P5-3; Sequence=VSP_031006;
CC Name=4;
CC IsoId=Q6T4P5-4; Sequence=VSP_031004;
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; AF541282; AAP57771.1; -; mRNA.
DR EMBL; AY436785; AAR10818.1; -; mRNA.
DR EMBL; AF357888; AAO85401.1; -; mRNA.
DR EMBL; AY304517; AAP72154.1; -; mRNA.
DR EMBL; AL136596; CAB66531.1; -; mRNA.
DR EMBL; AK021597; BAB13851.1; -; mRNA.
DR EMBL; BC012339; AAH12339.1; -; mRNA.
DR CCDS; CCDS12043.1; -. [Q6T4P5-3]
DR CCDS; CCDS58636.1; -. [Q6T4P5-1]
DR RefSeq; NP_001257295.1; NM_001270366.1. [Q6T4P5-1]
DR RefSeq; NP_079164.1; NM_024888.2. [Q6T4P5-3]
DR RefSeq; XP_011526619.1; XM_011528317.2. [Q6T4P5-3]
DR AlphaFoldDB; Q6T4P5; -.
DR BioGRID; 123019; 11.
DR CORUM; Q6T4P5; -.
DR IntAct; Q6T4P5; 9.
DR MINT; Q6T4P5; -.
DR STRING; 9606.ENSP00000352962; -.
DR DEPOD; PLPPR3; -.
DR GlyGen; Q6T4P5; 2 sites.
DR iPTMnet; Q6T4P5; -.
DR PhosphoSitePlus; Q6T4P5; -.
DR BioMuta; PLPPR3; -.
DR DMDM; 74723394; -.
DR EPD; Q6T4P5; -.
DR jPOST; Q6T4P5; -.
DR MassIVE; Q6T4P5; -.
DR PaxDb; Q6T4P5; -.
DR PeptideAtlas; Q6T4P5; -.
DR PRIDE; Q6T4P5; -.
DR ProteomicsDB; 67367; -. [Q6T4P5-1]
DR ProteomicsDB; 67368; -. [Q6T4P5-2]
DR ProteomicsDB; 67369; -. [Q6T4P5-3]
DR ProteomicsDB; 67370; -. [Q6T4P5-4]
DR Antibodypedia; 53515; 103 antibodies from 22 providers.
DR DNASU; 79948; -.
DR Ensembl; ENST00000359894.6; ENSP00000352962.2; ENSG00000129951.19. [Q6T4P5-3]
DR Ensembl; ENST00000520876.8; ENSP00000430297.1; ENSG00000129951.19. [Q6T4P5-1]
DR GeneID; 79948; -.
DR KEGG; hsa:79948; -.
DR MANE-Select; ENST00000520876.8; ENSP00000430297.1; NM_001270366.2; NP_001257295.1.
DR UCSC; uc002lpx.3; human. [Q6T4P5-1]
DR CTD; 79948; -.
DR DisGeNET; 79948; -.
DR GeneCards; PLPPR3; -.
DR HGNC; HGNC:23497; PLPPR3.
DR HPA; ENSG00000129951; Group enriched (bone marrow, brain, fallopian tube).
DR MIM; 610391; gene.
DR neXtProt; NX_Q6T4P5; -.
DR OpenTargets; ENSG00000129951; -.
DR VEuPathDB; HostDB:ENSG00000129951; -.
DR eggNOG; KOG3030; Eukaryota.
DR GeneTree; ENSGT00940000160280; -.
DR HOGENOM; CLU_021458_8_0_1; -.
DR InParanoid; Q6T4P5; -.
DR OMA; GNAPWEW; -.
DR OrthoDB; 1621899at2759; -.
DR PhylomeDB; Q6T4P5; -.
DR BRENDA; 3.1.3.4; 2681.
DR PathwayCommons; Q6T4P5; -.
DR Reactome; R-HSA-419408; Lysosphingolipid and LPA receptors.
DR SignaLink; Q6T4P5; -.
DR BioGRID-ORCS; 79948; 15 hits in 1024 CRISPR screens.
DR ChiTaRS; PLPPR3; human.
DR GenomeRNAi; 79948; -.
DR Pharos; Q6T4P5; Tbio.
DR PRO; PR:Q6T4P5; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q6T4P5; protein.
DR Bgee; ENSG00000129951; Expressed in cortical plate and 108 other tissues.
DR ExpressionAtlas; Q6T4P5; baseline and differential.
DR Genevisible; Q6T4P5; HS.
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 Alternative splicing; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..718
FT /note="Phospholipid phosphatase-related protein type 3"
FT /id="PRO_0000317529"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 313..347
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 545..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..463
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TPB0"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TPB0"
FT MOD_RES 376
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7TPB0"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TPB0"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TPB0"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TPB0"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..392
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_031004"
FT VAR_SEQ 134
FT /note="V -> VG (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_031005"
FT VAR_SEQ 219
FT /note="S -> SVSPAPHCPSQALLLTRGEPSLTPTPMPQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11230166,
FT ECO:0000303|PubMed:12730698, ECO:0000303|Ref.3"
FT /id="VSP_031006"
FT VARIANT 193
FT /note="I -> T (in dbSNP:rs1540615)"
FT /id="VAR_038544"
FT VARIANT 690
FT /note="A -> V (in dbSNP:rs3746136)"
FT /id="VAR_038545"
SQ SEQUENCE 718 AA; 76037 MW; 8F065B5D48D2447D CRC64;
MISTKEKNKI PKDSMTLLPC FYFVELPIVA SSIVSLYFLE LTDLFKPAKV GFQCYDRTLS
MPYVETNEEL IPLLMLLSLA FAAPAASIMV AEGMLYCLQS RLWGRAGGPA GAEGSINAGG
CNFNSFLRRT VRFVGVHVFG LCATALVTDV IQLATGYHTP FFLTVCKPNY TLLGTSCEVN
PYITQDICSG HDIHAILSAR KTFPSQHATL SAFAAVYVSM YFNSVISDTT KLLKPILVFA
FAIAAGVCGL TQITQYRSHP VDVYAGFLIG AGIAAYLACH AVGNFQAPPA EKPAAPAPAK
DALRALTQRG HDSVYQQNKS VSTDELGPPG RLEGAPRPVA REKTSLGSLK RASVDVDLLA
PRSPMAKENM VTFSHTLPRA SAPSLDDPAR RHMTIHVPLD ASRSKQLISE WKQKSLEGRG
LGLPDDASPG HLRAPAEPMA EEEEEEEDEE EEEEEEEEED EGPAPPSLYP TVQARPGLGP
RVILPPRAGP PPLVHIPEEG AQTGAGLSPK SGAGVRAKWL MMAEKSGAAV ANPPRLLQVI
AMSKAPGAPG PKAAETASSS SASSDSSQYR SPSDRDSASI VTIDAHAPHH PVVHLSAGGA
PWEWKAAGGG AKAEADGGYE LGDLARGFRG GAKPPGVSPG SSVSDVDQEE PRFGAVATVN
LATGEGLPPL GAADGALGPG SRESTLRRHA GGLGLAEREA EAEAEGYFRK MQARRFPD
