TPO_HUMAN
ID TPO_HUMAN Reviewed; 353 AA.
AC P40225; A1L3Y0; B7ZLR8; B9EGA8; Q13020; Q15790; Q15791; Q15792;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Thrombopoietin;
DE AltName: Full=C-mpl ligand;
DE Short=ML;
DE AltName: Full=Megakaryocyte colony-stimulating factor;
DE AltName: Full=Megakaryocyte growth and development factor;
DE Short=MGDF;
DE AltName: Full=Myeloproliferative leukemia virus oncogene ligand;
DE Flags: Precursor;
GN Name=THPO; Synonyms=MGDF;
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).
RC TISSUE=Fetal liver;
RX PubMed=8202154; DOI=10.1038/369533a0;
RA de Sauvage F.J., Hass P.E., Spencer S.D., Malloy B.E., Gurney A.L.,
RA Spencer S.A., Darbonne W.C., Henzel W.J., Wong S.C., Kuang W.-J.,
RA Oles K.J., Hultgren B., Solberg L.A. Jr., Goeddel D.V., Eaton D.L.;
RT "Stimulation of megakaryocytopoiesis and thrombopoiesis by the c-Mpl
RT ligand.";
RL Nature 369:533-538(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal liver;
RX PubMed=8020099; DOI=10.1016/0092-8674(94)90450-2;
RA Bartley T.D., Bogenberger J., Hunt P., Li Y.-S., Lu H.S., Martin F.,
RA Chang M.-S., Samal B.B., Nichol J.L., Swift S., Johnson M.J., Hsu R.-Y.,
RA Parker V.P., Suggs S., Skrine J.D., Merewether L.A., Clogson C., Hsu E.,
RA Hokom M.M., Hornkohl A., Choi E., Pangelinan M., Sun Y., Mar V., McNich J.,
RA Simonet L., Jacobsen F., Xie C., Shutter J., Chute H., Basu R.,
RA Selander L., Trollinger D., Sieu L., Padilla D., Trail G., Elliott G.,
RA Izumi R., Covey T., Crouse J., Garcia A., Xu W., del Castillo J., Biron J.,
RA Cole S., Hu M.C.-T., Pacifici R., Ponting I., Saris C., Wen D., Yung Y.P.,
RA Lin H., Bosselman R.A.;
RT "Identification and cloning of a megakaryocyte growth and development
RT factor that is a ligand for the cytokine receptor Mpl.";
RL Cell 77:1117-1124(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=7809166; DOI=10.1073/pnas.91.26.13023;
RA Foster D.C., Sprecher C.A., Grant F.J., Kramer J.M., Kuijper J.L.,
RA Holly R.D., Whitmore T.E., Heipel M.D., Bell L.A.N., Ching A.F.,
RA McGrane V., Hart C., O'Hara P.J., Lok S.;
RT "Human thrombopoietin: gene structure, cDNA sequence, expression, and
RT chromosomal localization.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:13023-13027(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=7926023; DOI=10.1016/0014-5793(94)01008-0;
RA Sohma Y., Akahori H., Seki N., Hori T.-A., Ogami K., Kawamura K.,
RA Miyazaki H.;
RT "Molecular cloning and chromosomal localization of the human thrombopoietin
RT gene.";
RL FEBS Lett. 353:57-61(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RX PubMed=7849319;
RA Gurney A.L., Kuang W.-J., Xie M.-H., Malloy B.E., Eaton D.L.,
RA de Sauvage F.J.;
RT "Genomic structure, chromosomal localization, and conserved alternative
RT splice forms of thrombopoietin.";
RL Blood 85:981-988(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=8537317; DOI=10.1093/oxfordjournals.jbchem.a124883;
RA Kato T., Ogami K., Shimada Y., Iwamatsu A., Sohma Y., Akahori H., Horie K.,
RA Kokubo A., Kudo Y., Maeda E., Kobayashi K., Ohashi H., Ozawa T., Inoue H.,
RA Kawamura K., Miyazaki H.;
RT "Purification and characterization of thrombopoietin.";
RL J. Biochem. 118:229-236(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=7822271; DOI=10.1074/jbc.270.2.685;
RA Chang M., McNinch J., Basu R., Shutter J., Hsu R., Perkins C., Mar V.,
RA Suggs S., Welcher A., Li L., Lu H., Bartley T., Hunt P., Martin F.,
RA Samal B., Bogenberger J.;
RT "Cloning and characterization of the human megakaryocyte growth and
RT development factor (MGDF) gene.";
RL J. Biol. Chem. 270:511-514(1995).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 3).
RA Im S.H., Lee W.S., Chung K.H.;
RT "Cloning and sequencing of human thrombopoietin.";
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Testis;
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 DISEASE.
RX PubMed=9425899; DOI=10.1038/ng0198-49;
RA Wiestner A., Schlemper R.J., van der Maas A.P.C., Skoda R.C.;
RT "An activating splice donor mutation in the thrombopoietin gene causes
RT hereditary thrombocythaemia.";
RL Nat. Genet. 18:49-52(1998).
RN [11]
RP DISULFIDE BONDS, AND GLYCOSYLATION AT SER-22; THR-58; THR-131; THR-179;
RP THR-180; SER-184; ASN-197; ASN-206; THR-213; ASN-234; ASN-255 AND SER-265.
RX PubMed=8942648; DOI=10.1021/bi961075b;
RA Hoffman R.C., Andersen H., Walker K., Krakover J.D., Patel S., Stamm M.R.,
RA Osborn S.G.;
RT "Peptide, disulfide, and glycosylation mapping of recombinant human
RT thrombopoietin from ser1 to Arg246.";
RL Biochemistry 35:14849-14861(1996).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 22-184 IN COMPLEX WITH ANTIBODY,
RP AND DISULFIDE BONDS.
RX PubMed=14769915; DOI=10.1073/pnas.0308530100;
RA Feese M.D., Tamada T., Kato Y., Maeda Y., Hirose M., Matsukura Y.,
RA Shigematsu H., Muto T., Matsumoto A., Watarai H., Ogami K., Tahara T.,
RA Kato T., Miyazaki H., Kuroki R.;
RT "Structure of the receptor-binding domain of human thrombopoietin
RT determined by complexation with a neutralizing antibody fragment.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:1816-1821(2004).
CC -!- FUNCTION: Lineage-specific cytokine affecting the proliferation and
CC maturation of megakaryocytes from their committed progenitor cells. It
CC acts at a late stage of megakaryocyte development. It may be the major
CC physiological regulator of circulating platelets.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P40225-1; Sequence=Displayed;
CC Name=2; Synonyms=TPO-2;
CC IsoId=P40225-2; Sequence=VSP_001450;
CC Name=3; Synonyms=Truncated;
CC IsoId=P40225-3; Sequence=VSP_001451;
CC -!- DOMAIN: Two-domain structure with an erythropoietin-like N-terminal and
CC a Ser/Pro/Thr-rich C-terminal.
CC -!- DISEASE: Thrombocythemia 1 (THCYT1) [MIM:187950]: A myeloproliferative
CC disorder characterized by excessive platelet production, resulting in
CC increased numbers of circulating platelets. It can be associated with
CC spontaneous hemorrhages and thrombotic episodes. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the EPO/TPO family. {ECO:0000305}.
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DR EMBL; L33410; AAA59857.1; -; mRNA.
DR EMBL; U11025; AAA50553.1; -; mRNA.
DR EMBL; L36051; AAC37568.1; -; Genomic_DNA.
DR EMBL; L36052; AAC37566.1; -; mRNA.
DR EMBL; D32046; BAA06807.1; -; Genomic_DNA.
DR EMBL; S76771; AAB33390.1; -; Genomic_DNA.
DR EMBL; D32047; BAA21930.1; -; mRNA.
DR EMBL; U59493; AAB03392.1; -; mRNA.
DR EMBL; U59494; AAB03393.1; -; mRNA.
DR EMBL; U59495; AAB03394.1; -; mRNA.
DR EMBL; U17071; AAA74083.1; -; Genomic_DNA.
DR EMBL; BC130322; AAI30323.1; -; mRNA.
DR EMBL; BC136338; AAI36339.1; -; mRNA.
DR EMBL; BC143982; AAI43983.1; -; mRNA.
DR CCDS; CCDS3265.1; -. [P40225-1]
DR CCDS; CCDS54693.1; -. [P40225-2]
DR PIR; G02729; G02729.
DR PIR; I59281; I80105.
DR RefSeq; NP_000451.1; NM_000460.3. [P40225-1]
DR RefSeq; NP_001171068.1; NM_001177597.2. [P40225-2]
DR RefSeq; NP_001171069.1; NM_001177598.2.
DR RefSeq; NP_001276926.1; NM_001289997.1.
DR RefSeq; NP_001276927.1; NM_001289998.1. [P40225-1]
DR RefSeq; NP_001276932.1; NM_001290003.1.
DR RefSeq; NP_001276951.1; NM_001290022.1. [P40225-2]
DR RefSeq; NP_001276955.1; NM_001290026.1.
DR RefSeq; NP_001276956.1; NM_001290027.1.
DR RefSeq; NP_001276957.1; NM_001290028.1. [P40225-1]
DR PDB; 1V7M; X-ray; 2.51 A; V/X=22-184.
DR PDB; 1V7N; X-ray; 3.30 A; V/X/Y/Z=22-184.
DR PDBsum; 1V7M; -.
DR PDBsum; 1V7N; -.
DR AlphaFoldDB; P40225; -.
DR SMR; P40225; -.
DR BioGRID; 112922; 3.
DR DIP; DIP-5729N; -.
DR ELM; P40225; -.
DR IntAct; P40225; 3.
DR STRING; 9606.ENSP00000204615; -.
DR ChEMBL; CHEMBL1293256; -.
DR GlyConnect; 592; 12 N-Linked glycans, 4 O-Linked glycans.
DR GlyGen; P40225; 15 sites, 25 N-linked glycans (2 sites), 7 O-linked glycans (1 site).
DR iPTMnet; P40225; -.
DR PhosphoSitePlus; P40225; -.
DR BioMuta; THPO; -.
DR DMDM; 730982; -.
DR MassIVE; P40225; -.
DR PaxDb; P40225; -.
DR PeptideAtlas; P40225; -.
DR PRIDE; P40225; -.
DR ProteomicsDB; 55350; -. [P40225-1]
DR ProteomicsDB; 55351; -. [P40225-2]
DR ProteomicsDB; 55352; -. [P40225-3]
DR ABCD; P40225; 1 sequenced antibody.
DR Antibodypedia; 19145; 615 antibodies from 36 providers.
DR DNASU; 7066; -.
DR Ensembl; ENST00000445696.6; ENSP00000410763.2; ENSG00000090534.20. [P40225-2]
DR Ensembl; ENST00000647395.1; ENSP00000494504.1; ENSG00000090534.20. [P40225-1]
DR GeneID; 7066; -.
DR KEGG; hsa:7066; -.
DR MANE-Select; ENST00000647395.1; ENSP00000494504.1; NM_000460.4; NP_000451.1.
DR UCSC; uc003fol.2; human. [P40225-1]
DR CTD; 7066; -.
DR DisGeNET; 7066; -.
DR GeneCards; THPO; -.
DR HGNC; HGNC:11795; THPO.
DR HPA; ENSG00000090534; Tissue enriched (liver).
DR MalaCards; THPO; -.
DR MIM; 187950; phenotype.
DR MIM; 600044; gene.
DR neXtProt; NX_P40225; -.
DR OpenTargets; ENSG00000090534; -.
DR Orphanet; 3319; Congenital amegakaryocytic thrombocytopenia.
DR Orphanet; 71493; Familial thrombocytosis.
DR Orphanet; 397692; Hereditary isolated aplastic anemia.
DR Orphanet; 329319; Thrombocythemia with distal limb defects.
DR PharmGKB; PA36506; -.
DR VEuPathDB; HostDB:ENSG00000090534; -.
DR eggNOG; ENOG502S9T0; Eukaryota.
DR GeneTree; ENSGT00390000006294; -.
DR HOGENOM; CLU_039844_0_0_1; -.
DR InParanoid; P40225; -.
DR OMA; PILCARQ; -.
DR OrthoDB; 906192at2759; -.
DR PhylomeDB; P40225; -.
DR TreeFam; TF338084; -.
DR PathwayCommons; P40225; -.
DR Reactome; R-HSA-76009; Platelet Aggregation (Plug Formation).
DR SignaLink; P40225; -.
DR SIGNOR; P40225; -.
DR BioGRID-ORCS; 7066; 7 hits in 1063 CRISPR screens.
DR ChiTaRS; THPO; human.
DR EvolutionaryTrace; P40225; -.
DR GeneWiki; Thrombopoietin; -.
DR GenomeRNAi; 7066; -.
DR Pharos; P40225; Tbio.
DR PRO; PR:P40225; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P40225; protein.
DR Bgee; ENSG00000090534; Expressed in right lobe of liver and 93 other tissues.
DR ExpressionAtlas; P40225; baseline and differential.
DR Genevisible; P40225; HS.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0008083; F:growth factor activity; TAS:UniProtKB.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0008283; P:cell population proliferation; IEA:InterPro.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0035855; P:megakaryocyte development; IDA:ARUK-UCL.
DR GO; GO:0030219; P:megakaryocyte differentiation; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:ARUK-UCL.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:1902035; P:positive regulation of hematopoietic stem cell proliferation; IDA:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:ARUK-UCL.
DR GO; GO:0045654; P:positive regulation of megakaryocyte differentiation; ISS:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:ARUK-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0097696; P:receptor signaling pathway via STAT; IDA:ARUK-UCL.
DR GO; GO:0038163; P:thrombopoietin-mediated signaling pathway; IDA:ARUK-UCL.
DR Gene3D; 1.20.1250.10; -; 1.
DR InterPro; IPR009079; 4_helix_cytokine-like_core.
DR InterPro; IPR019767; EPO/TPO_CS.
DR InterPro; IPR001323; EPO_TPO.
DR InterPro; IPR003978; Thrombopoietin.
DR PANTHER; PTHR10560; PTHR10560; 1.
DR Pfam; PF00758; EPO_TPO; 1.
DR PRINTS; PR01485; THROMBOPTN.
DR SUPFAM; SSF47266; SSF47266; 1.
DR PROSITE; PS00817; EPO_TPO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytokine; Disulfide bond; Glycoprotein;
KW Hormone; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT CHAIN 22..353
FT /note="Thrombopoietin"
FT /id="PRO_0000008411"
FT REGION 257..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..334
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 22
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:8942648"
FT CARBOHYD 58
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:8942648"
FT CARBOHYD 131
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:8942648"
FT CARBOHYD 179
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:8942648"
FT CARBOHYD 180
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:8942648"
FT CARBOHYD 184
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:8942648"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:8942648"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:8942648"
FT CARBOHYD 213
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:8942648"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:8942648"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:8942648"
FT CARBOHYD 265
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:8942648"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..172
FT DISULFID 50..106
FT VAR_SEQ 133..136
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_001450"
FT VAR_SEQ 160..198
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_001451"
FT VARIANT 14
FT /note="L -> P (in dbSNP:rs1042346)"
FT /id="VAR_011795"
FT VARIANT 116
FT /note="G -> E (in dbSNP:rs1126665)"
FT /id="VAR_011796"
FT CONFLICT 46
FT /note="R -> K (in Ref. 8; AAB03392/AAB03393/AAB03394)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="M -> MSQ (in Ref. 7; AAA74083)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="Q -> E (in Ref. 2; AAA50553)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="T -> P (in Ref. 7; AAA74083)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="G -> E (in Ref. 8; AAB03393/AAB03394)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="S -> C (in Ref. 8; AAB03393/AAB03394)"
FT /evidence="ECO:0000305"
FT HELIX 32..45
FT /evidence="ECO:0007829|PDB:1V7M"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:1V7M"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:1V7M"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:1V7M"
FT HELIX 70..74
FT /evidence="ECO:0007829|PDB:1V7M"
FT HELIX 77..98
FT /evidence="ECO:0007829|PDB:1V7M"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:1V7M"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:1V7M"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:1V7M"
FT HELIX 113..129
FT /evidence="ECO:0007829|PDB:1V7M"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:1V7M"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1V7M"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:1V7M"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:1V7M"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:1V7M"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:1V7N"
SQ SEQUENCE 353 AA; 37823 MW; F0AB5449B72E5526 CRC64;
MELTELLLVV MLLLTARLTL SSPAPPACDL RVLSKLLRDS HVLHSRLSQC PEVHPLPTPV
LLPAVDFSLG EWKTQMEETK AQDILGAVTL LLEGVMAARG QLGPTCLSSL LGQLSGQVRL
LLGALQSLLG TQLPPQGRTT AHKDPNAIFL SFQHLLRGKV RFLMLVGGST LCVRRAPPTT
AVPSRTSLVL TLNELPNRTS GLLETNFTAS ARTTGSGLLK WQQGFRAKIP GLLNQTSRSL
DQIPGYLNRI HELLNGTRGL FPGPSRRTLG APDISSGTSD TGSLPPNLQP GYSPSPTHPP
TGQYTLFPLP PTLPTPVVQL HPLLPDPSAP TPTPTSPLLN TSYTHSQNLS QEG
