PLPR2_HUMAN
ID PLPR2_HUMAN Reviewed; 343 AA.
AC Q96GM1; Q5CZ76; Q8N1U4; Q9H929;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Phospholipid phosphatase-related protein type 2 {ECO:0000305};
DE AltName: Full=Inactive phospholipid phosphatase PLPPR2 {ECO:0000250|UniProtKB:Q6WAY2};
DE AltName: Full=Lipid phosphate phosphatase-related protein type 2 {ECO:0000303|Ref.2};
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|HGNC:HGNC:29566};
GN Synonyms=LPPR2 {ECO:0000303|Ref.2}, PRG4 {ECO:0000250|UniProtKB:Q8VCY8};
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 1).
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 [MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Caudate nucleus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 87-343 (ISOFORM 2).
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP VARIANT [LARGE SCALE ANALYSIS] MET-155.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- INTERACTION:
CC Q96GM1; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-12955265, EBI-11343438;
CC Q96GM1; P11912: CD79A; NbExp=3; IntAct=EBI-12955265, EBI-7797864;
CC Q96GM1; Q9H5X1: CIAO2A; NbExp=3; IntAct=EBI-12955265, EBI-752069;
CC Q96GM1; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-12955265, EBI-1045797;
CC Q96GM1; O00501: CLDN5; NbExp=3; IntAct=EBI-12955265, EBI-18400628;
CC Q96GM1; O95484: CLDN9; NbExp=3; IntAct=EBI-12955265, EBI-18341636;
CC Q96GM1; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-12955265, EBI-6942903;
CC Q96GM1; P04921: GYPC; NbExp=3; IntAct=EBI-12955265, EBI-7797098;
CC Q96GM1; P43628: KIR2DL3; NbExp=3; IntAct=EBI-12955265, EBI-8632435;
CC Q96GM1; Q6UWN5: LYPD5; NbExp=3; IntAct=EBI-12955265, EBI-17200970;
CC Q96GM1; Q9P0N8: MARCHF2; NbExp=3; IntAct=EBI-12955265, EBI-10317612;
CC Q96GM1; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-12955265, EBI-17247926;
CC Q96GM1; Q96PQ1: SIGLEC12; NbExp=3; IntAct=EBI-12955265, EBI-17640454;
CC Q96GM1; Q9BZV2: SLC19A3; NbExp=3; IntAct=EBI-12955265, EBI-3923779;
CC Q96GM1; Q0VAQ4: SMAGP; NbExp=3; IntAct=EBI-12955265, EBI-10226799;
CC Q96GM1; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-12955265, EBI-17280858;
CC Q96GM1; Q86Y82: STX12; NbExp=3; IntAct=EBI-12955265, EBI-2691717;
CC Q96GM1; Q9BVK6: TMED9; NbExp=3; IntAct=EBI-12955265, EBI-1056827;
CC Q96GM1; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-12955265, EBI-10982110;
CC Q96GM1; Q9Y385: UBE2J1; NbExp=3; IntAct=EBI-12955265, EBI-988826;
CC Q96GM1; Q9H7M9: VSIR; NbExp=3; IntAct=EBI-12955265, EBI-744988;
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=Q96GM1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96GM1-2; Sequence=VSP_031010, VSP_031011;
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; AY339628; AAQ73540.1; -; mRNA.
DR EMBL; AY304516; AAP72153.1; -; mRNA.
DR EMBL; AK094869; BAC04443.1; -; mRNA.
DR EMBL; AK023117; BAB14414.1; -; mRNA.
DR EMBL; CH471106; EAW84200.1; -; Genomic_DNA.
DR EMBL; BC009378; AAH09378.1; -; mRNA.
DR EMBL; CR936652; CAI56790.1; -; Transcribed_RNA.
DR CCDS; CCDS12258.1; -. [Q96GM1-1]
DR CCDS; CCDS59352.1; -. [Q96GM1-2]
DR RefSeq; NP_001164106.1; NM_001170635.1. [Q96GM1-2]
DR RefSeq; NP_073574.2; NM_022737.2. [Q96GM1-1]
DR RefSeq; XP_016882637.1; XM_017027148.1. [Q96GM1-2]
DR AlphaFoldDB; Q96GM1; -.
DR BioGRID; 122264; 71.
DR IntAct; Q96GM1; 38.
DR STRING; 9606.ENSP00000466898; -.
DR DEPOD; PLPPR2; -.
DR GlyGen; Q96GM1; 1 site.
DR iPTMnet; Q96GM1; -.
DR PhosphoSitePlus; Q96GM1; -.
DR BioMuta; PLPPR2; -.
DR DMDM; 74760839; -.
DR MassIVE; Q96GM1; -.
DR PaxDb; Q96GM1; -.
DR PeptideAtlas; Q96GM1; -.
DR PRIDE; Q96GM1; -.
DR ProteomicsDB; 76643; -. [Q96GM1-1]
DR ProteomicsDB; 76644; -. [Q96GM1-2]
DR Antibodypedia; 25796; 100 antibodies from 23 providers.
DR DNASU; 64748; -.
DR Ensembl; ENST00000251473.9; ENSP00000251473.4; ENSG00000105520.11. [Q96GM1-1]
DR Ensembl; ENST00000591608.2; ENSP00000466898.1; ENSG00000105520.11. [Q96GM1-2]
DR GeneID; 64748; -.
DR KEGG; hsa:64748; -.
DR UCSC; uc002mre.2; human. [Q96GM1-1]
DR CTD; 64748; -.
DR DisGeNET; 64748; -.
DR GeneCards; PLPPR2; -.
DR HGNC; HGNC:29566; PLPPR2.
DR HPA; ENSG00000105520; Tissue enhanced (brain).
DR MIM; 619591; gene.
DR neXtProt; NX_Q96GM1; -.
DR OpenTargets; ENSG00000105520; -.
DR VEuPathDB; HostDB:ENSG00000105520; -.
DR eggNOG; KOG3030; Eukaryota.
DR GeneTree; ENSGT00940000158145; -.
DR HOGENOM; CLU_021458_1_1_1; -.
DR InParanoid; Q96GM1; -.
DR OMA; NAYIQPF; -.
DR OrthoDB; 1621899at2759; -.
DR PhylomeDB; Q96GM1; -.
DR BRENDA; 3.1.3.4; 2681.
DR PathwayCommons; Q96GM1; -.
DR Reactome; R-HSA-419408; Lysosphingolipid and LPA receptors.
DR SignaLink; Q96GM1; -.
DR BioGRID-ORCS; 64748; 7 hits in 961 CRISPR screens.
DR ChiTaRS; PLPPR2; human.
DR GenomeRNAi; 64748; -.
DR Pharos; Q96GM1; Tdark.
DR PRO; PR:Q96GM1; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q96GM1; protein.
DR Bgee; ENSG00000105520; Expressed in cortical plate and 170 other tissues.
DR ExpressionAtlas; Q96GM1; baseline and differential.
DR Genevisible; Q96GM1; 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; 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_0000317538"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
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 290..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCY8"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCY8"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 23..47
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_031010"
FT VAR_SEQ 317..343
FT /note="NPRSAGRIRHRHGSPHPSRRTAPAVAT -> LSVAQEPEVCRPHSTPARLTP
FT SKSQNCARRGHLIPSCVSSRAPAMCSSPRVPRPRLRSEPTPLPLPLPLPAPTPSQGPSP
FT SSPGPGGPGGGGGRGRKLLLPTPLLRDLYTLSGLYPSPFHRDNFSPYLFASRDHLL
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_031011"
FT VARIANT 155
FT /note="T -> M (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_038546"
FT CONFLICT 42
FT /note="F -> L (in Ref. 3; BAB14414)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="Y -> H (in Ref. 3; BAC04443)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 343 AA; 36880 MW; CB46CE2FA8503E4E CRC64;
MAGGRPHLKR SFSIIPCFVF VESVLLGIVI LLAYRLEFTD TFPVHTQGFF CYDSTYAKPY
PGPEAASRVP PALVYALVTA GPTLTILLGE LARAFFPAPP SAVPVIGEST IVSGACCRFS
PPVRRLVRFL GVYSFGLFTT TIFANAGQVV TGNPTPHFLS VCRPNYTALG CLPPSPDRPG
PDRFVTDQGA CAGSPSLVAA ARRAFPCKDA ALCAYAVTYT AMYVTLVFRV KGSRLVKPSL
CLALLCPAFL VGVVRVAEYR NHWSDVLAGF LTGAAIATFL VTCVVHNFQS RPPSGRRLSP
WEDLGQAPTM DSPLEKNPRS AGRIRHRHGS PHPSRRTAPA VAT