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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   03-AUG-2022, entry version 181.
DE   RecName: Full=Phospholipid phosphatase 3 {ECO:0000305};
DE            EC=3.1.3.- {ECO:0000269|PubMed:27694435};
DE            EC=3.1.3.4 {ECO:0000269|PubMed:9607309, ECO:0000269|PubMed:9705349};
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 {ECO:0000303|PubMed:12660161};
DE            Short=VCIP {ECO:0000303|PubMed:12660161};
GN   Name=PLPP3 {ECO:0000312|HGNC:HGNC:9229}; Synonyms=LPP3, PPAP2B;
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], INDUCTION, AND TISSUE SPECIFICITY.
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+-independent
RT   phosphatidic acid phosphatase.";
RL   J. Biol. Chem. 272:24572-24578(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION,
RP   PATHWAY, SUBCELLULAR LOCATION, GLYCOSYLATION, AND MUTAGENESIS OF ASP-184.
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 specificity of
RT   the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a
RT   isoform.";
RL   J. Biol. Chem. 273:22059-22067(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY,
RP   TISSUE SPECIFICITY, AND MOTIF.
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 phosphatidic
RT   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., 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   [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 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., 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 (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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [10]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP   SPECIFICITY, AND PATHWAY.
RX   PubMed=9607309; DOI=10.1016/s0014-5793(98)00421-9;
RA   Hooks S.B., Ragan S.P., Lynch K.R.;
RT   "Identification of a novel human phosphatidic acid phosphatase type 2
RT   isoform.";
RL   FEBS Lett. 427:188-192(1998).
RN   [11]
RP   SUBCELLULAR LOCATION, DOMAIN, AND MOTIF.
RX   PubMed=14527693; DOI=10.1016/s0014-5793(03)00931-1;
RA   Jia Y.J., Kai M., Wada I., Sakane F., Kanoh H.;
RT   "Differential localization of lipid phosphate phosphatases 1 and 3 to cell
RT   surface subdomains in polarized MDCK cells.";
RL   FEBS Lett. 552:240-246(2003).
RN   [12]
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   [13]
RP   FUNCTION, AND MOTIF.
RX   PubMed=16099422; DOI=10.1016/j.bbrc.2005.07.157;
RA   Humtsoe J.O., Bowling R.A. Jr., Feng S., Wary K.K.;
RT   "Murine lipid phosphate phosphohydrolase-3 acts as a cell-associated
RT   integrin ligand.";
RL   Biochem. Biophys. Res. Commun. 335:906-919(2005).
RN   [14]
RP   SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-106; TYR-109 AND TYR-110.
RX   PubMed=17005594; DOI=10.1093/jb/mvj195;
RA   Kai M., Sakane F., Jia Y.J., Imai S., Yasuda S., Kanoh H.;
RT   "Lipid phosphate phosphatases 1 and 3 are localized in distinct lipid
RT   rafts.";
RL   J. Biochem. 140:677-686(2006).
RN   [15]
RP   SUBUNIT.
RX   PubMed=18215144; DOI=10.1042/bj20071607;
RA   Long J.S., Pyne N.J., Pyne S.;
RT   "Lipid phosphate phosphatases form homo- and hetero-oligomers: catalytic
RT   competency, subcellular distribution and function.";
RL   Biochem. J. 411:371-377(2008).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP   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 the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [17]
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   [18]
RP   FUNCTION, INTERACTION WITH CTNND1, SUBCELLULAR LOCATION, AND REGION.
RX   PubMed=20123964; DOI=10.1128/mcb.00038-09;
RA   Humtsoe J.O., Liu M., Malik A.B., Wary K.K.;
RT   "Lipid phosphate phosphatase 3 stabilization of beta-catenin induces
RT   endothelial cell migration and formation of branching point structures.";
RL   Mol. Cell. Biol. 30:1593-1606(2010).
RN   [19]
RP   FUNCTION.
RX   PubMed=21569306; DOI=10.1186/1476-4598-10-51;
RA   Chatterjee I., Humtsoe J.O., Kohler E.E., Sorio C., Wary K.K.;
RT   "Lipid phosphate phosphatase-3 regulates tumor growth via beta-catenin and
RT   CYCLIN-D1 signaling.";
RL   Mol. Cancer 10:51-51(2011).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [21]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=23591818; DOI=10.1242/jcs.117705;
RA   Gutierrez-Martinez E., Fernandez-Ulibarri I., Lazaro-Dieguez F.,
RA   Johannes L., Pyne S., Sarri E., Egea G.;
RT   "Lipid phosphate phosphatase 3 participates in transport carrier formation
RT   and protein trafficking in the early secretory pathway.";
RL   J. Cell Sci. 126:2641-2655(2013).
RN   [22]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=27694435; DOI=10.1093/cvr/cvw217;
RA   Touat-Hamici Z., Weidmann H., Blum Y., Proust C., Durand H., Iannacci F.,
RA   Codoni V., Gaignard P., Therond P., Civelek M., Karabina S.A., Lusis A.J.,
RA   Cambien F., Ninio E.;
RT   "Role of lipid phosphate phosphatase 3 in human aortic endothelial cell
RT   function.";
RL   Cardiovasc. Res. 112:702-713(2016).
CC   -!- FUNCTION: Magnesium-independent phospholipid phosphatase of the plasma
CC       membrane that catalyzes the dephosphorylation of a variety of
CC       glycerolipid and sphingolipid phosphate esters including
CC       phosphatidate/PA, lysophosphatidate/LPA, diacylglycerol
CC       pyrophosphate/DGPP, sphingosine 1-phosphate/S1P and ceramide 1-
CC       phosphate/C1P (PubMed:9705349, PubMed:9607309, PubMed:27694435). Also
CC       acts on N-oleoyl ethanolamine phosphate/N-(9Z-octadecenoyl)-
CC       ethanolamine phosphate, a potential physiological compound
CC       (PubMed:9607309). Has both an extracellular and an intracellular
CC       phosphatase activity, allowing the hydrolysis and the cellular uptake
CC       of these bioactive lipid mediators from the milieu, regulating signal
CC       transduction in different cellular processes (PubMed:9607309,
CC       PubMed:23591818, PubMed:27694435). Through the dephosphorylation of
CC       extracellular sphingosine-1-phosphate and the regulation of its
CC       extra- and intracellular availability, plays a role in vascular
CC       homeostasis, regulating endothelial cell migration, adhesion, survival,
CC       proliferation and the production of pro-inflammatory cytokines
CC       (PubMed:27694435). By maintaining the appropriate levels of this lipid
CC       in the cerebellum, also ensure its proper development and function (By
CC       similarity). Through its intracellular lipid phosphatase activity may
CC       act in early compartments of the secretory pathway, regulating the
CC       formation of Golgi to endoplasmic reticulum retrograde transport
CC       carriers (PubMed:23591818). {ECO:0000250|UniProtKB:Q99JY8,
CC       ECO:0000269|PubMed:23591818, ECO:0000269|PubMed:27694435,
CC       ECO:0000269|PubMed:9607309, ECO:0000269|PubMed:9705349}.
CC   -!- FUNCTION: Independently of this phosphatase activity may also function
CC       in the Wnt signaling pathway and the stabilization of beta-
CC       catenin/CTNNB1, thereby regulating cell proliferation, migration and
CC       differentiation in angiogenesis or yet in tumor growth
CC       (PubMed:20123964, PubMed:21569306). Also plays a role in integrin-
CC       mediated cell-cell adhesion in angiogenesis (PubMed:12660161,
CC       PubMed:16099422). {ECO:0000269|PubMed:12660161,
CC       ECO:0000269|PubMed:16099422, ECO:0000269|PubMed:20123964,
CC       ECO:0000269|PubMed:21569306}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-
CC         glycerol + phosphate; Xref=Rhea:RHEA:27429, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:17815, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608; EC=3.1.3.4;
CC         Evidence={ECO:0000269|PubMed:9607309, ECO:0000269|PubMed:9705349};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27430;
CC         Evidence={ECO:0000305|PubMed:9705349};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphate + H2O = 1,2-
CC         dihexadecanoyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:43236,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:72859,
CC         ChEBI:CHEBI:82929; Evidence={ECO:0000269|PubMed:9705349};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43237;
CC         Evidence={ECO:0000305|PubMed:9705349};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1,2-
CC         di-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:43244,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:52333,
CC         ChEBI:CHEBI:74546; Evidence={ECO:0000269|PubMed:9607309};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43245;
CC         Evidence={ECO:0000305|PubMed:9607309};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + monoacyl-sn-glycero-3-phosphate = a monoacylglycerol +
CC         phosphate; Xref=Rhea:RHEA:46736, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:17408, ChEBI:CHEBI:43474, ChEBI:CHEBI:77589;
CC         Evidence={ECO:0000269|PubMed:9607309, ECO:0000269|PubMed:9705349};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46737;
CC         Evidence={ECO:0000305|PubMed:9705349};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-sn-glycero-3-phosphate + H2O = (9Z-
CC         octadecenoyl)-glycerol + phosphate; Xref=Rhea:RHEA:50884,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:75937,
CC         ChEBI:CHEBI:84973; Evidence={ECO:0000269|PubMed:9607309,
CC         ECO:0000269|PubMed:9705349};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50885;
CC         Evidence={ECO:0000305|PubMed:9705349};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + sphing-4-enine 1-phosphate = phosphate + sphing-4-enine;
CC         Xref=Rhea:RHEA:27518, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57756, ChEBI:CHEBI:60119;
CC         Evidence={ECO:0000269|PubMed:27694435, ECO:0000269|PubMed:9705349};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27519;
CC         Evidence={ECO:0000269|PubMed:27694435};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acylsphing-4-enine 1-phosphate + H2O = an N-acylsphing-4-
CC         enine + phosphate; Xref=Rhea:RHEA:33743, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:52639, ChEBI:CHEBI:57674;
CC         Evidence={ECO:0000269|PubMed:9705349};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33744;
CC         Evidence={ECO:0000305|PubMed:9705349};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-(octanoyl)-sphing-4-enine-1-phosphate = N-
CC         octanoylsphing-4-enine + phosphate; Xref=Rhea:RHEA:62040,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:45815,
CC         ChEBI:CHEBI:85376; Evidence={ECO:0000269|PubMed:9705349};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62041;
CC         Evidence={ECO:0000305|PubMed:9705349};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-(9Z-octadecenoyl)-ethanolamine phosphate = N-(9Z-
CC         octadecenoyl) ethanolamine + phosphate; Xref=Rhea:RHEA:62160,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:71466,
CC         ChEBI:CHEBI:145465; Evidence={ECO:0000269|PubMed:9607309};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62161;
CC         Evidence={ECO:0000305|PubMed:9607309};
CC   -!- ACTIVITY REGULATION: Magnesium-independent phospholipid phosphatase
CC       (PubMed:9705349). Insensitive to N-ethylmaleimide (PubMed:9705349).
CC       Inhibited by sphingosine, zinc ions and modestly by propanolol
CC       (PubMed:9705349). {ECO:0000269|PubMed:9705349}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=100 uM for 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate
CC         {ECO:0000269|PubMed:9607309};
CC         KM=110 uM for (9Z)-octadecenoyl-sn-glycero-3-phosphate
CC         {ECO:0000269|PubMed:9607309};
CC         KM=56 uM for N-oleoyl ethanolamine phosphatidic acid
CC         {ECO:0000269|PubMed:9607309};
CC         Vmax=0.27 nmol/min/mg enzyme with 1,2-dihexadecanoyl-sn-glycero-3-
CC         phosphate as substrate {ECO:0000269|PubMed:9705349};
CC         Vmax=0.46 nmol/min/mg enzyme with (9Z)-octadecenoyl-sn-glycero-3-
CC         phosphate as substrate {ECO:0000269|PubMed:9705349};
CC         Vmax=0.36 nmol/min/mg enzyme with N-(octanoyl)-sphing-4-enine-1-
CC         phosphate as substrate {ECO:0000269|PubMed:9705349};
CC         Vmax=0.24 nmol/min/mg enzyme with sphing-4-enine 1-phosphate as
CC         substrate {ECO:0000269|PubMed:9705349};
CC         Vmax=13 nmol/min/mg enzyme with 1,2-di-(9Z-octadecenoyl)-sn-glycero-
CC         3-phosphate as substrate {ECO:0000269|PubMed:9607309};
CC         Vmax=15 nmol/min/mg enzyme with (9Z)-octadecenoyl-sn-glycero-3-
CC         phosphate as substrate {ECO:0000269|PubMed:9607309};
CC         Vmax=29 nmol/min/mg enzyme with N-(9Z-octadecenoyl)-ethanolamine
CC         phosphate as substrate {ECO:0000269|PubMed:9607309};
CC   -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC       {ECO:0000269|PubMed:27694435, ECO:0000269|PubMed:9607309,
CC       ECO:0000269|PubMed:9705349}.
CC   -!- SUBUNIT: Forms functional homodimers and homooligomers that are not
CC       required for substrate recognition and catalytic activity
CC       (PubMed:14725715). Can also form heterooligomers with other PLPP2 and
CC       PLPP3 (PubMed:18215144). Interacts with CTNND1; negatively regulates
CC       the PLPP3-mediated stabilization of beta-catenin/CTNNB1
CC       (PubMed:20123964). {ECO:0000269|PubMed:14725715,
CC       ECO:0000269|PubMed:18215144, ECO:0000269|PubMed:20123964}.
CC   -!- INTERACTION:
CC       O14495; O60716: CTNND1; NbExp=9; IntAct=EBI-766232, EBI-701927;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12660161,
CC       ECO:0000269|PubMed:20123964, ECO:0000269|PubMed:9705349}; Multi-pass
CC       membrane protein {ECO:0000250|UniProtKB:P97544}. Basolateral cell
CC       membrane {ECO:0000269|PubMed:14527693}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P97544}. Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:23591818}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P97544}. Endoplasmic reticulum-Golgi
CC       intermediate compartment membrane {ECO:0000269|PubMed:23591818}; Multi-
CC       pass membrane protein {ECO:0000250|UniProtKB:P97544}. Golgi apparatus
CC       membrane {ECO:0000269|PubMed:23591818}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P97544}. Golgi apparatus, trans-Golgi network
CC       membrane {ECO:0000269|PubMed:23591818}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P97544}. Membrane raft
CC       {ECO:0000269|PubMed:17005594}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P97544}. Note=Cycles between the endoplasmic
CC       reticulum and the Golgi. {ECO:0000269|PubMed:23591818}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed (PubMed:9305923,
CC       PubMed:12660161). Highly expressed in heart and placenta
CC       (PubMed:9305923). {ECO:0000269|PubMed:12660161,
CC       ECO:0000269|PubMed:9305923}.
CC   -!- INDUCTION: By EGF, VEGF, FGF2 and phorbol myristate acetate (PMA).
CC       {ECO:0000269|PubMed:9305923}.
CC   -!- DOMAIN: The integrin-binding motif mediates the binding to integrin
CC       alpha-5/beta-1 (ITGA5:ITGB1) and integrin alpha-V/beta-3 (ITGAV:ITGB3)
CC       and is required for the function in integrin-mediated cell-cell
CC       adhesion. {ECO:0000269|PubMed:12660161, ECO:0000269|PubMed:16099422}.
CC   -!- DOMAIN: The dityrosine basolateral targeting motif mediates
CC       localization to the basolateral membrane in polarized cells.
CC       {ECO:0000269|PubMed:14527693}.
CC   -!- PTM: N-glycosylated (PubMed:9705349). Contains high-mannose
CC       oligosaccharides (PubMed:9705349). {ECO:0000269|PubMed:9705349}.
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB50222.1; Type=Frameshift; Evidence={ECO:0000305};
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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   AlphaFoldDB; O14495; -.
DR   BioGRID; 114171; 27.
DR   CORUM; O14495; -.
DR   IntAct; O14495; 5.
DR   MINT; O14495; -.
DR   STRING; 9606.ENSP00000360296; -.
DR   SwissLipids; SLP:000001642; -.
DR   DEPOD; PLPP3; -.
DR   GlyGen; O14495; 1 site.
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   Antibodypedia; 33239; 137 antibodies from 26 providers.
DR   DNASU; 8613; -.
DR   Ensembl; ENST00000371250.4; ENSP00000360296.3; ENSG00000162407.9.
DR   GeneID; 8613; -.
DR   KEGG; hsa:8613; -.
DR   MANE-Select; ENST00000371250.4; ENSP00000360296.3; NM_003713.5; NP_003704.3.
DR   UCSC; uc001cyj.3; human.
DR   CTD; 8613; -.
DR   DisGeNET; 8613; -.
DR   GeneCards; PLPP3; -.
DR   HGNC; HGNC:9229; PLPP3.
DR   HPA; ENSG00000162407; Low tissue specificity.
DR   MIM; 607125; gene.
DR   neXtProt; NX_O14495; -.
DR   OpenTargets; ENSG00000162407; -.
DR   PharmGKB; PA33553; -.
DR   VEuPathDB; HostDB:ENSG00000162407; -.
DR   eggNOG; KOG3030; Eukaryota.
DR   GeneTree; ENSGT00940000156450; -.
DR   HOGENOM; CLU_021458_3_0_1; -.
DR   InParanoid; O14495; -.
DR   OMA; KYPANSG; -.
DR   OrthoDB; 1621899at2759; -.
DR   PhylomeDB; O14495; -.
DR   TreeFam; TF316040; -.
DR   BRENDA; 3.1.3.4; 2681.
DR   PathwayCommons; O14495; -.
DR   Reactome; R-HSA-1660661; Sphingolipid de novo biosynthesis.
DR   SignaLink; O14495; -.
DR   UniPathway; UPA00085; -.
DR   BioGRID-ORCS; 8613; 6 hits in 1071 CRISPR screens.
DR   ChiTaRS; PLPP3; human.
DR   GeneWiki; PPAP2B; -.
DR   GenomeRNAi; 8613; -.
DR   Pharos; O14495; Tbio.
DR   PRO; PR:O14495; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; O14495; protein.
DR   Bgee; ENSG00000162407; Expressed in decidua and 204 other tissues.
DR   Genevisible; O14495; HS.
DR   GO; GO:0005912; C:adherens junction; TAS:BHF-UCL.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR   GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR   GO; GO:0106235; F:ceramide-1-phosphate phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
DR   GO; GO:0042577; F:lipid phosphatase activity; IBA:GO_Central.
DR   GO; GO:0008195; F:phosphatidate phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0042392; F:sphingosine-1-phosphate phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0060020; P:Bergmann glial cell differentiation; IEA:Ensembl.
DR   GO; GO:0001568; P:blood vessel development; IEA:Ensembl.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0033631; P:cell-cell adhesion mediated by integrin; IDA:UniProtKB.
DR   GO; GO:0006672; P:ceramide metabolic process; IDA:UniProtKB.
DR   GO; GO:0001702; P:gastrulation with mouth forming second; IEA:Ensembl.
DR   GO; GO:0034109; P:homotypic cell-cell adhesion; IDA:BHF-UCL.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:UniProtKB.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:BHF-UCL.
DR   GO; GO:0046839; P:phospholipid dephosphorylation; IDA:UniProtKB.
DR   GO; GO:0006644; P:phospholipid metabolic process; IDA:UniProtKB.
DR   GO; GO:0022409; P:positive regulation of cell-cell adhesion; IMP:BHF-UCL.
DR   GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR   GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:BHF-UCL.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   GO; GO:0050821; P:protein stabilization; IDA:BHF-UCL.
DR   GO; GO:1902068; P:regulation of sphingolipid mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0030111; P:regulation of Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IMP:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0030148; P:sphingolipid biosynthetic process; TAS:Reactome.
DR   GO; GO:0006670; P:sphingosine metabolic process; IDA:UniProtKB.
DR   GO; GO:0042060; P:wound healing; IMP:BHF-UCL.
DR   InterPro; IPR028675; LPP3.
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: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; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW   Hydrolase; Lipid metabolism; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..311
FT                   /note="Phospholipid phosphatase 3"
FT                   /id="PRO_0000220912"
FT   TOPO_DOM        1..33
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:12660161"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        55..85
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305|PubMed:12660161"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        107..122
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:12660161"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        144..193
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:12660161"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        215..225
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:12660161"
FT   TRANSMEM        226..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        244..257
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305|PubMed:12660161"
FT   TRANSMEM        258..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        279..311
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:12660161"
FT   REGION          148..156
FT                   /note="Phosphatase sequence motif I"
FT                   /evidence="ECO:0000250|UniProtKB:O34349"
FT   REGION          196..199
FT                   /note="Phosphatase sequence motif II"
FT                   /evidence="ECO:0000250|UniProtKB:O34349"
FT   REGION          244..255
FT                   /note="Phosphatase sequence motif III"
FT                   /evidence="ECO:0000250|UniProtKB:O34349"
FT   REGION          275..311
FT                   /note="Mediates interaction with CTNND1"
FT                   /evidence="ECO:0000269|PubMed:20123964"
FT   MOTIF           109..110
FT                   /note="Dityrosine basolateral targeting motif"
FT                   /evidence="ECO:0000269|PubMed:14527693"
FT   MOTIF           182..184
FT                   /note="Integrin-binding motif"
FT                   /evidence="ECO:0000269|PubMed:12660161,
FT                   ECO:0000269|PubMed:16099422"
FT   ACT_SITE        199
FT                   /note="Proton donors"
FT                   /evidence="ECO:0000250|UniProtKB:O34349"
FT   ACT_SITE        251
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O34349"
FT   SITE            255
FT                   /note="Stabilizes the active site histidine for
FT                   nucleophilic attack"
FT                   /evidence="ECO:0000250|UniProtKB:O34349"
FT   MOD_RES         19
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:21406692"
FT   CARBOHYD        170
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         106
FT                   /note="Y->A: No effect on basolateral localization in
FT                   polarized cells."
FT                   /evidence="ECO:0000269|PubMed:17005594"
FT   MUTAGEN         109
FT                   /note="Y->A: Loss of basolateral localization in polarized
FT                   cells."
FT                   /evidence="ECO:0000269|PubMed:17005594"
FT   MUTAGEN         110
FT                   /note="Y->A: Loss of basolateral localization in polarized
FT                   cells."
FT                   /evidence="ECO:0000269|PubMed:17005594"
FT   MUTAGEN         184
FT                   /note="D->E: Loss of binding to integrin. Loss of function
FT                   in integrin-mediated cell-cell interaction."
FT                   /evidence="ECO:0000269|PubMed:9705349"
FT   CONFLICT        32
FT                   /note="K -> M (in Ref. 7; AAV38396)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        282
FT                   /note="T -> M (in Ref. 9; AAH09196)"
FT                   /evidence="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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