ID PLPP2_HUMAN Reviewed; 288 AA.
AC O43688; A6NLV0; E9PAY8;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 18-JAN-2017, entry version 134.
DE RecName: Full=Phospholipid phosphatase 2 {ECO:0000312|HGNC:HGNC:9230};
DE EC=3.1.3.4;
DE AltName: Full=Lipid phosphate phosphohydrolase 2;
DE AltName: Full=PAP2-gamma;
DE Short=PAP2-G;
DE AltName: Full=Phosphatidate phosphohydrolase type 2c;
DE AltName: Full=Phosphatidic acid phosphatase 2c;
DE Short=PAP-2c;
DE Short=PAP2c;
GN Name=PLPP2 {ECO:0000312|HGNC:HGNC:9230}; Synonyms=LPP2, PPAP2C;
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] (ISOFORM 1).
RX PubMed=9570154; DOI=10.1089/dna.1998.17.377;
RA Leung D.W., Tompkins C.K., White T.;
RT "Molecular cloning of two alternatively spliced forms of human
RT phosphatidic acid phosphatase cDNAs that are differentially expressed
RT in normal and tumor cells.";
RL DNA Cell Biol. 17:377-385(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] (ISOFORM 1), AND CHARACTERIZATION.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary;
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).
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 PA > C-1-P
CC > LPA > S-1-P.
CC -!- CATALYTIC ACTIVITY: A 1,2-diacylglycerol 3-phosphate + H(2)O = a
CC 1,2-diacyl-sn-glycerol + phosphate.
CC -!- ENZYME REGULATION: Inhibited by sphingosine, zinc ions and
CC propanolol.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- INTERACTION:
CC Q7Z3S9:NOTCH2NL; NbExp=3; IntAct=EBI-722017, EBI-945833;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O43688-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43688-2; Sequence=VSP_037765;
CC Note=No experimental confirmation available.;
CC Name=3;
CC IsoId=O43688-3; Sequence=VSP_047366;
CC Note=Gene prediction based on EST data.;
CC -!- TISSUE SPECIFICITY: Found mainly in brain, pancreas and placenta.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000305}.
DR EMBL; AF035959; AAC15968.1; -; mRNA.
DR EMBL; AF047760; AAC32104.1; -; mRNA.
DR EMBL; AF056083; AAC25666.1; -; mRNA.
DR EMBL; BT007021; AAP35667.1; -; mRNA.
DR EMBL; AC016588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002806; AAH02806.1; -; mRNA.
DR CCDS; CCDS12023.1; -. [O43688-1]
DR CCDS; CCDS12024.1; -. [O43688-2]
DR CCDS; CCDS45889.1; -. [O43688-3]
DR RefSeq; NP_003703.1; NM_003712.3. [O43688-1]
DR RefSeq; NP_803545.1; NM_177526.2. [O43688-3]
DR RefSeq; NP_808211.1; NM_177543.2. [O43688-2]
DR UniGene; Hs.465506; -.
DR ProteinModelPortal; O43688; -.
DR BioGrid; 114170; 8.
DR IntAct; O43688; 6.
DR MINT; MINT-1372912; -.
DR STRING; 9606.ENSP00000329697; -.
DR DEPOD; O43688; -.
DR iPTMnet; O43688; -.
DR PhosphoSitePlus; O43688; -.
DR BioMuta; PPAP2C; -.
DR MaxQB; O43688; -.
DR PaxDb; O43688; -.
DR PeptideAtlas; O43688; -.
DR PRIDE; O43688; -.
DR DNASU; 8612; -.
DR Ensembl; ENST00000269812; ENSP00000269812; ENSG00000141934. [O43688-3]
DR Ensembl; ENST00000327790; ENSP00000329697; ENSG00000141934. [O43688-2]
DR Ensembl; ENST00000434325; ENSP00000388565; ENSG00000141934. [O43688-1]
DR GeneID; 8612; -.
DR KEGG; hsa:8612; -.
DR UCSC; uc002loh.5; human. [O43688-1]
DR CTD; 8612; -.
DR DisGeNET; 8612; -.
DR GeneCards; PPAP2C; -.
DR HGNC; HGNC:9230; PLPP2.
DR HPA; HPA055540; -.
DR MIM; 607126; gene.
DR neXtProt; NX_O43688; -.
DR OpenTargets; ENSG00000141934; -.
DR PharmGKB; PA33554; -.
DR eggNOG; KOG3030; Eukaryota.
DR eggNOG; COG0671; LUCA.
DR GeneTree; ENSGT00620000087654; -.
DR HOGENOM; HOG000041307; -.
DR HOVERGEN; HBG002048; -.
DR InParanoid; O43688; -.
DR KO; K01080; -.
DR OMA; KRGFYCN; -.
DR OrthoDB; EOG091G0K5H; -.
DR PhylomeDB; O43688; -.
DR TreeFam; TF316040; -.
DR BioCyc; ZFISH:HS06877-MONOMER; -.
DR Reactome; R-HSA-1660661; Sphingolipid de novo biosynthesis.
DR GeneWiki; Phosphatidic_acid_phosphatase_2c; -.
DR GenomeRNAi; 8612; -.
DR PRO; PR:O43688; -.
DR Proteomes; UP000005640; Chromosome 19.
DR Bgee; ENSG00000141934; -.
DR CleanEx; HS_PPAP2C; -.
DR ExpressionAtlas; O43688; baseline and differential.
DR Genevisible; O43688; HS.
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:0008195; F:phosphatidate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; TAS:ProtInc.
DR GO; GO:0042392; F:sphingosine-1-phosphate phosphatase activity; TAS:Reactome.
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 GO; GO:0030148; P:sphingolipid biosynthetic process; TAS:Reactome.
DR Gene3D; 1.20.144.10; -; 1.
DR InterPro; IPR028674; LPP2.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR PANTHER; PTHR10165:SF25; PTHR10165:SF25; 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; Complete proteome; Glycoprotein; Hydrolase;
KW Membrane; Polymorphism; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1 288 Phospholipid phosphatase 2.
FT /FTId=PRO_0000220909.
FT TRANSMEM 5 25 Helical. {ECO:0000255}.
FT TRANSMEM 52 72 Helical. {ECO:0000255}.
FT TRANSMEM 88 108 Helical. {ECO:0000255}.
FT TRANSMEM 163 183 Helical. {ECO:0000255}.
FT TRANSMEM 197 217 Helical. {ECO:0000255}.
FT TRANSMEM 227 247 Helical. {ECO:0000255}.
FT CARBOHYD 139 139 N-linked (GlcNAc...). {ECO:0000255}.
FT VAR_SEQ 1 56 Missing (in isoform 3). {ECO:0000305}.
FT /FTId=VSP_047366.
FT VAR_SEQ 1 17 MQRRWVFVLLDVLCLLV -> MGVARGPGSRGQHPPPRQQE
FT VCAEGPRARLHPAPPGLG (in isoform 2).
FT {ECO:0000305}.
FT /FTId=VSP_037765.
FT VARIANT 180 180 A -> V (in dbSNP:rs1138439).
FT /FTId=VAR_061541.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 99 240 ismart:acidPPc [T]
FT MYHIT 101 244 ipfam:PAP2 [T]
SQ SEQUENCE 288 AA; 32574 MW; F7C6A09A28DA9AC8 CRC64;
MQRRWVFVLL DVLCLLVASL PFAILTLVNA PYKRGFYCGD DSIRYPYRPD TITHGLMAGV
TITATVILVS AGEAYLVYTD RLYSRSDFNN YVAAVYKVLG TFLFGAAVSQ SLTDLAKYMI
GRLRPNFLAV CDPDWSRVNC SVYVQLEKVC RGNPADVTEA RLSFYSGHSS FGMYCMVFLA
LYVQARLCWK WARLLRPTVQ FFLVAFALYV GYTRVSDYKH HWSDVLVGLL QGALVAALTV
CYISDFFKAR PPQHCLKEEE LERKPSLSLT LTLGEADHNH YGYPHSSS
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