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Database: UniProt
Entry: PLPP3_HUMAN
LinkDB: PLPP3_HUMAN
Original site: PLPP3_HUMAN 
ID   PLPP3_HUMAN             Reviewed;         311 AA.
AC   O14495; B2R651; D3DQ52; Q5U0F7; Q96GW0; Q99782;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   18-SEP-2019, entry version 166.
DE   RecName: Full=Phospholipid phosphatase 3 {ECO:0000312|HGNC:HGNC:9229};
DE            EC=3.1.3.4;
DE   AltName: Full=Lipid phosphate phosphohydrolase 3;
DE   AltName: Full=PAP2-beta;
DE   AltName: Full=Phosphatidate phosphohydrolase type 2b;
DE   AltName: Full=Phosphatidic acid phosphatase 2b;
DE            Short=PAP-2b;
DE            Short=PAP2b;
DE   AltName: Full=Vascular endothelial growth factor and type I collagen-inducible protein;
DE            Short=VCIP;
GN   Name=PLPP3 {ECO:0000312|HGNC:HGNC:9229}; Synonyms=LPP3, PPAP2B;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND INDUCTION.
RX   PubMed=9305923; DOI=10.1074/jbc.272.39.24572;
RA   Kai M., Wada I., Imai S., Sakane F., Kanoh H.;
RT   "Cloning and characterization of two human isozymes of Mg2+-
RT   independent phosphatidic acid phosphatase.";
RL   J. Biol. Chem. 272:24572-24578(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RX   PubMed=9705349; DOI=10.1074/jbc.273.34.22059;
RA   Roberts R., Sciorra V.A., Morris A.J.;
RT   "Human type 2 phosphatidic acid phosphohydrolases. Substrate
RT   specificity of the type 2a, 2b, and 2c enzymes and cell surface
RT   activity of the 2a isoform.";
RL   J. Biol. Chem. 273:22059-22067(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12660161; DOI=10.1093/emboj/cdg165;
RA   Humtsoe J.O., Feng S., Thakker G.D., Yang J., Hong J., Wary K.K.;
RT   "Regulation of cell-cell interactions by phosphatidic acid phosphatase
RT   2b/VCIP.";
RL   EMBO J. 22:1539-1554(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Leung D.W., Tompkins C.K.;
RT   "Molecular cloning of and expression of an isoform of human
RT   phosphatidic acid phosphatase cDNA.";
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=9110174; DOI=10.1101/gr.7.4.353;
RA   Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA   Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT   "Large-scale concatenation cDNA sequencing.";
RL   Genome Res. 7:353-358(1997).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [10]
RP   SUBUNIT.
RX   PubMed=14725715; DOI=10.1186/1471-2091-5-2;
RA   Burnett C., Makridou P., Hewlett L., Howard K.;
RT   "Lipid phosphate phosphatases dimerise, but this interaction is not
RT   required for in vivo activity.";
RL   BMC Biochem. 5:2-2(2004).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
CC   -!- FUNCTION: Catalyzes the conversion of phosphatidic acid (PA) to
CC       diacylglycerol (DG). In addition it hydrolyzes lysophosphatidic
CC       acid (LPA), ceramide-1-phosphate (C-1-P) and sphingosine-1-
CC       phosphate (S-1-P). The relative catalytic efficiency is LPA = PA >
CC       C-1-P > S-1-P. May be involved in cell adhesion and in cell-cell
CC       interactions.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-
CC         sn-glycerol + phosphate; Xref=Rhea:RHEA:27429,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:17815, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58608; EC=3.1.3.4;
CC   -!- ACTIVITY REGULATION: Inhibited by sphingosine, zinc ions and
CC       propanolol. Not inhibited by N-ethylmaleimide treatment.
CC   -!- SUBUNIT: Homodimer. This complex seems not to be involved in
CC       substrate recognition, it may confer only structural or functional
CC       stability. {ECO:0000269|PubMed:14725715}.
CC   -!- INTERACTION:
CC       O60716:CTNND1; NbExp=9; IntAct=EBI-766232, EBI-701927;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC       membrane; Multi-pass membrane protein. Cell membrane; Multi-pass
CC       membrane protein.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in
CC       heart and placenta.
CC   -!- INDUCTION: By EGF, VEGF, FGF2 and phorbol myristate acetate (PMA).
CC       {ECO:0000269|PubMed:9305923}.
CC   -!- PTM: N-glycosylated. Contains high-mannose oligosaccharides.
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB50222.1; Type=Frameshift; Positions=225; Evidence={ECO:0000305};
DR   EMBL; AB000889; BAA22594.1; -; mRNA.
DR   EMBL; AF017786; AAC63433.1; -; mRNA.
DR   EMBL; AF480883; AAO84481.1; -; mRNA.
DR   EMBL; AF043329; AAD02271.1; -; mRNA.
DR   EMBL; U79294; AAB50222.1; ALT_FRAME; mRNA.
DR   EMBL; AK312439; BAG35348.1; -; mRNA.
DR   EMBL; BT019589; AAV38396.1; -; mRNA.
DR   EMBL; CH471059; EAX06651.1; -; Genomic_DNA.
DR   EMBL; CH471059; EAX06652.1; -; Genomic_DNA.
DR   EMBL; CH471059; EAX06653.1; -; Genomic_DNA.
DR   EMBL; BC009196; AAH09196.1; -; mRNA.
DR   CCDS; CCDS604.1; -.
DR   RefSeq; NP_003704.3; NM_003713.4.
DR   BioGrid; 114171; 11.
DR   CORUM; O14495; -.
DR   IntAct; O14495; 4.
DR   MINT; O14495; -.
DR   STRING; 9606.ENSP00000360296; -.
DR   SwissLipids; SLP:000001642; -.
DR   DEPOD; O14495; -.
DR   iPTMnet; O14495; -.
DR   PhosphoSitePlus; O14495; -.
DR   BioMuta; PLPP3; -.
DR   EPD; O14495; -.
DR   jPOST; O14495; -.
DR   MassIVE; O14495; -.
DR   MaxQB; O14495; -.
DR   PaxDb; O14495; -.
DR   PeptideAtlas; O14495; -.
DR   PRIDE; O14495; -.
DR   ProteomicsDB; 48039; -.
DR   DNASU; 8613; -.
DR   Ensembl; ENST00000371250; ENSP00000360296; ENSG00000162407.
DR   GeneID; 8613; -.
DR   KEGG; hsa:8613; -.
DR   UCSC; uc001cyj.3; human.
DR   CTD; 8613; -.
DR   DisGeNET; 8613; -.
DR   GeneCards; PLPP3; -.
DR   HGNC; HGNC:9229; PLPP3.
DR   HPA; HPA028892; -.
DR   HPA; HPA072751; -.
DR   MIM; 607125; gene.
DR   neXtProt; NX_O14495; -.
DR   OpenTargets; ENSG00000162407; -.
DR   PharmGKB; PA33553; -.
DR   eggNOG; KOG3030; Eukaryota.
DR   eggNOG; COG0671; LUCA.
DR   GeneTree; ENSGT00940000156450; -.
DR   HOGENOM; HOG000041307; -.
DR   InParanoid; O14495; -.
DR   KO; K01080; -.
DR   OMA; YKCRGDD; -.
DR   OrthoDB; 1621899at2759; -.
DR   PhylomeDB; O14495; -.
DR   TreeFam; TF316040; -.
DR   Reactome; R-HSA-1660661; Sphingolipid de novo biosynthesis.
DR   SignaLink; O14495; -.
DR   ChiTaRS; PLPP3; human.
DR   GeneWiki; PPAP2B; -.
DR   GenomeRNAi; 8613; -.
DR   Pharos; O14495; -.
DR   PRO; PR:O14495; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000162407; Expressed in 239 organ(s), highest expression level in metanephric glomerulus.
DR   Genevisible; O14495; HS.
DR   GO; GO:0005912; C:adherens junction; TAS:BHF-UCL.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0042577; F:lipid phosphatase activity; IBA:GO_Central.
DR   GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR   GO; GO:0008195; F:phosphatidate phosphatase activity; IBA:GO_Central.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; TAS:ProtInc.
DR   GO; GO:0042392; F:sphingosine-1-phosphate phosphatase activity; IBA:GO_Central.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0044329; P:canonical Wnt signaling pathway involved in positive regulation of cell-cell adhesion; IMP:BHF-UCL.
DR   GO; GO:0044328; P:canonical Wnt signaling pathway involved in positive regulation of endothelial cell migration; IMP:BHF-UCL.
DR   GO; GO:0044330; P:canonical Wnt signaling pathway involved in positive regulation of wound healing; IMP:BHF-UCL.
DR   GO; GO:0008354; P:germ cell migration; TAS:ProtInc.
DR   GO; GO:0034109; P:homotypic cell-cell adhesion; IDA:BHF-UCL.
DR   GO; GO:0006629; P:lipid metabolic process; NAS:ProtInc.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:BHF-UCL.
DR   GO; GO:0046839; P:phospholipid dephosphorylation; IBA:GO_Central.
DR   GO; GO:0006644; P:phospholipid metabolic process; IBA:GO_Central.
DR   GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR   GO; GO:0050821; P:protein stabilization; IDA:BHF-UCL.
DR   GO; GO:0030111; P:regulation of Wnt signaling pathway; IEA:InterPro.
DR   GO; GO:0030148; P:sphingolipid biosynthetic process; TAS:Reactome.
DR   InterPro; IPR028675; LPP3.
DR   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   PANTHER; PTHR10165:SF79; PTHR10165:SF79; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; SSF48317; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Complete proteome; Glycoprotein; Golgi apparatus;
KW   Hydrolase; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    311       Phospholipid phosphatase 3.
FT                                /FTId=PRO_0000220912.
FT   TOPO_DOM      1     33       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     34     54       Helical. {ECO:0000255}.
FT   TOPO_DOM     55     85       Lumenal. {ECO:0000255}.
FT   TRANSMEM     86    106       Helical. {ECO:0000255}.
FT   TOPO_DOM    107    122       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    123    143       Helical. {ECO:0000255}.
FT   TOPO_DOM    144    193       Lumenal. {ECO:0000255}.
FT   TRANSMEM    194    214       Helical. {ECO:0000255}.
FT   TOPO_DOM    215    227       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    228    248       Helical. {ECO:0000255}.
FT   TOPO_DOM    249    257       Lumenal. {ECO:0000255}.
FT   TRANSMEM    258    278       Helical. {ECO:0000255}.
FT   TOPO_DOM    279    311       Cytoplasmic. {ECO:0000255}.
FT   MOD_RES      19     19       Phosphoserine.
FT                                {ECO:0000244|PubMed:18691976,
FT                                ECO:0000244|PubMed:21406692}.
FT   CARBOHYD    170    170       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CONFLICT     32     32       K -> M (in Ref. 7; AAV38396).
FT                                {ECO:0000305}.
FT   CONFLICT    282    282       T -> M (in Ref. 9; AAH09196).
FT                                {ECO:0000305}.
SQ   SEQUENCE   311 AA;  35116 MW;  CB3F60189044DA31 CRC64;
     MQNYKYDKAI VPESKNGGSP ALNNNPRRSG SKRVLLICLD LFCLFMAGLP FLIIETSTIK
     PYHRGFYCND ESIKYPLKTG ETINDAVLCA VGIVIAILAI ITGEFYRIYY LKKSRSTIQN
     PYVAALYKQV GCFLFGCAIS QSFTDIAKVS IGRLRPHFLS VCNPDFSQIN CSEGYIQNYR
     CRGDDSKVQE ARKSFFSGHA SFSMYTMLYL VLYLQARFTW RGARLLRPLL QFTLIMMAFY
     TGLSRVSDHK HHPSDVLAGF AQGALVACCI VFFVSDLFKT KTTLSLPAPA IRKEILSPVD
     IIDRNNHHNM M
//
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