ZDHC2_HUMAN
ID ZDHC2_HUMAN Reviewed; 367 AA.
AC Q9UIJ5; D3DSP5;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Palmitoyltransferase ZDHHC2 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000269|PubMed:23793055};
DE AltName: Full=Acyltransferase ZDHHC2 {ECO:0000250|UniProtKB:P59267};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:P59267};
DE AltName: Full=Reduced expression associated with metastasis protein;
DE Short=Ream;
DE AltName: Full=Reduced expression in cancer protein;
DE Short=Rec;
DE AltName: Full=Zinc finger DHHC domain-containing protein 2 {ECO:0000312|HGNC:HGNC:18469};
DE Short=DHHC-2;
DE AltName: Full=Zinc finger protein 372;
GN Name=ZDHHC2 {ECO:0000312|HGNC:HGNC:18469}; Synonyms=REAM, REC, ZNF372;
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], TISSUE SPECIFICITY, AND VARIANTS PHE-306 AND
RP ILE-356.
RX PubMed=10918388;
RX DOI=10.1002/1098-2264(2000)9999:9999<::aid-gcc1001>3.0.co;2-#;
RA Oyama T., Miyoshi Y., Koyama K., Nakagawa H., Yamori T., Ito T.,
RA Matsuda H., Arakawa H., Nakamura Y.;
RT "Isolation of a novel gene on 8p21.3-22 whose expression is reduced
RT significantly in human colorectal cancers with liver metastasis.";
RL Genes Chromosomes Cancer 29:9-15(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Duodenum;
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, PALMITOYLATION, AND MUTAGENESIS OF
RP 154-ASP-HIS-155 AND CYS-157.
RX PubMed=18508921; DOI=10.1091/mbc.e07-11-1164;
RA Sharma C., Yang X.H., Hemler M.E.;
RT "DHHC2 affects palmitoylation, stability, and functions of tetraspanins CD9
RT and CD151.";
RL Mol. Biol. Cell 19:3415-3425(2008).
RN [5]
RP FUNCTION.
RX PubMed=18296695; DOI=10.1074/mcp.m800069-mcp200;
RA Zhang J., Planey S.L., Ceballos C., Stevens S.M. Jr., Keay S.K.,
RA Zacharias D.A.;
RT "Identification of CKAP4/p63 as a major substrate of the palmitoyl
RT acyltransferase DHHC2, a putative tumor suppressor, using a novel
RT proteomics method.";
RL Mol. Cell. Proteomics 7:1378-1388(2008).
RN [6]
RP FUNCTION.
RX PubMed=19144824; DOI=10.1091/mbc.e08-08-0849;
RA Planey S.L., Keay S.K., Zhang C.O., Zacharias D.A.;
RT "Palmitoylation of cytoskeleton associated protein 4 by DHHC2 regulates
RT antiproliferative factor-mediated signaling.";
RL Mol. Biol. Cell 20:1454-1463(2009).
RN [7]
RP FUNCTION.
RX PubMed=21343290; DOI=10.1074/jbc.m110.193763;
RA Jia L., Linder M.E., Blumer K.J.;
RT "Gi/o signaling and the palmitoyltransferase DHHC2 regulate palmitate
RT cycling and shuttling of RGS7 family-binding protein.";
RL J. Biol. Chem. 286:13695-13703(2011).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=21471008; DOI=10.1091/mbc.e10-11-0924;
RA Greaves J., Carmichael J.A., Chamberlain L.H.;
RT "The palmitoyl transferase DHHC2 targets a dynamic membrane cycling
RT pathway: regulation by a C-terminal domain.";
RL Mol. Biol. Cell 22:1887-1895(2011).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, PALMITOYLATION, AND TISSUE SPECIFICITY.
RX PubMed=22034844; DOI=10.3109/09687688.2011.630682;
RA Zeidman R., Buckland G., Cebecauer M., Eissmann P., Davis D.M., Magee A.I.;
RT "DHHC2 is a protein S-acyltransferase for Lck.";
RL Mol. Membr. Biol. 28:473-486(2011).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF CYS-157, AND ACTIVE
RP SITE.
RX PubMed=23793055; DOI=10.1074/jbc.m113.458794;
RA Lai J., Linder M.E.;
RT "Oligomerization of DHHC protein S-acyltransferases.";
RL J. Biol. Chem. 288:22862-22870(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=30404808; DOI=10.1128/jvi.01747-18;
RA Zhang N., Zhao H., Zhang L.;
RT "Fatty acid synthase promotes the palmitoylation of Chikungunya virus
RT nsP1.";
RL J. Virol. 0:0-0(2018).
CC -!- FUNCTION: Palmitoyltransferase that catalyzes the addition of palmitate
CC onto various protein substrates and is involved in a variety of
CC cellular processes (PubMed:18508921, PubMed:18296695, PubMed:19144824,
CC PubMed:21343290, PubMed:22034844, PubMed:23793055). Has no stringent
CC fatty acid selectivity and in addition to palmitate can also transfer
CC onto target proteins myristate from tetradecanoyl-CoA and stearate from
CC octadecanoyl-CoA (By similarity). In the nervous system, plays a role
CC in long term synaptic potentiation by palmitoylating AKAP5 through
CC which it regulates protein trafficking from the dendritic recycling
CC endosomes to the plasma membrane and controls both structural and
CC functional plasticity at excitatory synapses (By similarity). In
CC dendrites, mediates the palmitoylation of DLG4 when synaptic activity
CC decreases and induces synaptic clustering of DLG4 and associated AMPA-
CC type glutamate receptors (By similarity). Also mediates the de novo and
CC turnover palmitoylation of RGS7BP, a shuttle for Gi/o-specific GTPase-
CC activating proteins/GAPs, promoting its localization to the plasma
CC membrane in response to the activation of G protein-coupled receptors.
CC Through the localization of these GTPase-activating proteins/GAPs, it
CC also probably plays a role in G protein-coupled receptors signaling in
CC neurons (By similarity). Also probably plays a role in cell adhesion by
CC palmitoylating CD9 and CD151 to regulate their expression and function
CC (PubMed:18508921). Palmitoylates the endoplasmic reticulum protein
CC CKAP4 and regulates its localization to the plasma membrane
CC (PubMed:18296695, PubMed:19144824). Could also palmitoylate LCK and
CC regulate its localization to the plasma membrane (PubMed:22034844).
CC {ECO:0000250|UniProtKB:P59267, ECO:0000250|UniProtKB:Q9JKR5,
CC ECO:0000269|PubMed:18296695, ECO:0000269|PubMed:18508921,
CC ECO:0000269|PubMed:19144824, ECO:0000269|PubMed:21343290,
CC ECO:0000269|PubMed:22034844, ECO:0000269|PubMed:23793055}.
CC -!- FUNCTION: (Microbial infection) Promotes Chikungunya virus (CHIKV)
CC replication by mediating viral nsp1 palmitoylation.
CC {ECO:0000269|PubMed:30404808}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-
CC hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151;
CC EC=2.3.1.225; Evidence={ECO:0000269|PubMed:23793055};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000305|PubMed:23793055};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteinyl-[protein] + tetradecanoyl-CoA = CoA + S-
CC tetradecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59736, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:15433, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:143199;
CC Evidence={ECO:0000250|UniProtKB:P59267};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59737;
CC Evidence={ECO:0000250|UniProtKB:P59267};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteinyl-[protein] + octadecanoyl-CoA = CoA + S-
CC octadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59740, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:15434, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:143200;
CC Evidence={ECO:0000250|UniProtKB:P59267};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59741;
CC Evidence={ECO:0000250|UniProtKB:P59267};
CC -!- SUBUNIT: Monomer (PubMed:23793055). Homodimer (PubMed:23793055). The
CC monomeric form has a higher catalytic activity (PubMed:23793055).
CC {ECO:0000269|PubMed:23793055}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic density
CC {ECO:0000250|UniProtKB:Q9JKR5}. Postsynaptic recycling endosome
CC membrane {ECO:0000250|UniProtKB:P59267}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:21471008}; Multi-pass
CC membrane protein {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:22034844}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:18508921,
CC ECO:0000269|PubMed:22034844}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Translocates to postsynaptic density when synaptic
CC activity decreases. {ECO:0000250|UniProtKB:Q9JKR5}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed (PubMed:10918388,
CC PubMed:22034844). Reduced expression in colorectal cancers with liver
CC metastasis (PubMed:10918388). {ECO:0000269|PubMed:10918388,
CC ECO:0000269|PubMed:22034844}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- PTM: Autopalmitoylated. {ECO:0000269|PubMed:18508921,
CC ECO:0000269|PubMed:22034844}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AB023584; BAA88923.1; -; mRNA.
DR EMBL; CH471080; EAW63824.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63825.1; -; Genomic_DNA.
DR EMBL; BC039253; AAH39253.1; -; mRNA.
DR EMBL; BC050272; AAH50272.1; -; mRNA.
DR CCDS; CCDS47810.1; -.
DR RefSeq; NP_057437.1; NM_016353.4.
DR AlphaFoldDB; Q9UIJ5; -.
DR SMR; Q9UIJ5; -.
DR BioGRID; 119374; 4.
DR IntAct; Q9UIJ5; 3.
DR STRING; 9606.ENSP00000262096; -.
DR SwissLipids; SLP:000001951; -.
DR iPTMnet; Q9UIJ5; -.
DR PhosphoSitePlus; Q9UIJ5; -.
DR SwissPalm; Q9UIJ5; -.
DR BioMuta; ZDHHC2; -.
DR DMDM; 28202111; -.
DR EPD; Q9UIJ5; -.
DR jPOST; Q9UIJ5; -.
DR MassIVE; Q9UIJ5; -.
DR PaxDb; Q9UIJ5; -.
DR PeptideAtlas; Q9UIJ5; -.
DR PRIDE; Q9UIJ5; -.
DR ProteomicsDB; 84534; -.
DR Antibodypedia; 22244; 128 antibodies from 23 providers.
DR DNASU; 51201; -.
DR Ensembl; ENST00000262096.13; ENSP00000262096.8; ENSG00000104219.13.
DR GeneID; 51201; -.
DR KEGG; hsa:51201; -.
DR MANE-Select; ENST00000262096.13; ENSP00000262096.8; NM_016353.5; NP_057437.1.
DR UCSC; uc003wxe.4; human.
DR CTD; 51201; -.
DR DisGeNET; 51201; -.
DR GeneCards; ZDHHC2; -.
DR HGNC; HGNC:18469; ZDHHC2.
DR HPA; ENSG00000104219; Tissue enhanced (retina).
DR MIM; 618621; gene.
DR neXtProt; NX_Q9UIJ5; -.
DR OpenTargets; ENSG00000104219; -.
DR PharmGKB; PA38336; -.
DR VEuPathDB; HostDB:ENSG00000104219; -.
DR eggNOG; KOG1315; Eukaryota.
DR GeneTree; ENSGT00940000153716; -.
DR HOGENOM; CLU_027721_1_3_1; -.
DR InParanoid; Q9UIJ5; -.
DR OMA; DFPTRSD; -.
DR OrthoDB; 1491968at2759; -.
DR PhylomeDB; Q9UIJ5; -.
DR TreeFam; TF316044; -.
DR BRENDA; 2.3.1.225; 2681.
DR PathwayCommons; Q9UIJ5; -.
DR Reactome; R-HSA-5683826; Surfactant metabolism.
DR Reactome; R-HSA-9694548; Maturation of spike protein.
DR SignaLink; Q9UIJ5; -.
DR SIGNOR; Q9UIJ5; -.
DR BioGRID-ORCS; 51201; 9 hits in 1077 CRISPR screens.
DR ChiTaRS; ZDHHC2; human.
DR GeneWiki; ZDHHC2_(gene); -.
DR GenomeRNAi; 51201; -.
DR Pharos; Q9UIJ5; Tbio.
DR PRO; PR:Q9UIJ5; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9UIJ5; protein.
DR Bgee; ENSG00000104219; Expressed in sperm and 194 other tissues.
DR ExpressionAtlas; Q9UIJ5; baseline and differential.
DR Genevisible; Q9UIJ5; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum 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:0005887; C:integral component of plasma membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0098837; C:postsynaptic recycling endosome; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:Ensembl.
DR GO; GO:0016409; F:palmitoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0019705; F:protein-cysteine S-myristoyltransferase activity; IEA:RHEA.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0140439; F:protein-cysteine S-stearoyltransferase activity; IEA:RHEA.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IDA:UniProtKB.
DR GO; GO:1904719; P:positive regulation of AMPA glutamate receptor clustering; ISS:UniProtKB.
DR GO; GO:1905751; P:positive regulation of endosome to plasma membrane protein transport; ISS:UniProtKB.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:1903539; P:protein localization to postsynaptic membrane; ISS:UniProtKB.
DR GO; GO:0018345; P:protein palmitoylation; IDA:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR GO; GO:0022407; P:regulation of cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; ISS:UniProtKB.
DR GO; GO:0042176; P:regulation of protein catabolic process; IMP:UniProtKB.
DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0016188; P:synaptic vesicle maturation; IBA:GO_Central.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cell membrane; Endoplasmic reticulum; Endosome;
KW Golgi apparatus; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Reference proteome; Synapse; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..367
FT /note="Palmitoyltransferase ZDHHC2"
FT /id="PRO_0000212859"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..54
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..208
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..367
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 127..177
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 299..367
FT /note="Mediates localization to plasma membrane and
FT recycling endosomes"
FT /evidence="ECO:0000250|UniProtKB:P59267"
FT REGION 330..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 335..336
FT /note="Non-canonical dileucine endocytic signal"
FT /evidence="ECO:0000250|UniProtKB:P59267"
FT MOTIF 358..361
FT /note="NPxY-like endocytic signal"
FT /evidence="ECO:0000250|UniProtKB:P59267"
FT COMPBIAS 332..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 157
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000269|PubMed:23793055"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 306
FT /note="S -> F (in a hepatocellular carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:10918388"
FT /id="VAR_015229"
FT VARIANT 356
FT /note="M -> I (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs568589179)"
FT /evidence="ECO:0000269|PubMed:10918388"
FT /id="VAR_015230"
FT MUTAGEN 154..155
FT /note="DH->AA: Loss of protein-cysteine S-
FT palmitoyltransferase activity."
FT /evidence="ECO:0000269|PubMed:18508921"
FT MUTAGEN 157
FT /note="C->S: Loss of protein-cysteine S-
FT palmitoyltransferase activity."
FT /evidence="ECO:0000269|PubMed:18508921,
FT ECO:0000269|PubMed:23793055"
SQ SEQUENCE 367 AA; 42022 MW; B7BFB82837B7EE98 CRC64;
MAPSGPGSSA RRRCRRVLYW IPVVFITLLL GWSYYAYAIQ LCIVSMENTG EQVVCLMAYH
LLFAMFVWSY WKTIFTLPMN PSKEFHLSYA EKDLLEREPR GEAHQEVLRR AAKDLPIYTR
TMSGAIRYCD RCQLIKPDRC HHCSVCDKCI LKMDHHCPWV NNCVGFSNYK FFLLFLAYSL
LYCLFIAATD LQYFIKFWTN GLPDTQAKFH IMFLFFAAAM FSVSLSSLFG YHCWLVSKNK
STLEAFRSPV FRHGTDKNGF SLGFSKNMRQ VFGDEKKYWL LPIFSSLGDG CSFPTCLVNQ
DPEQASTPAG LNSTAKNLEN HQFPAKPLRE SQSHLLTDSQ SWTESSINPG KCKAGMSNPA
LTMENET
