ID S23A2_MOUSE Reviewed; 648 AA.
AC Q9EPR4; Q80Y23; Q8C327; Q9JM78;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 27-MAR-2024, entry version 175.
DE RecName: Full=Solute carrier family 23 member 2;
DE AltName: Full=Na(+)/L-ascorbic acid transporter 2;
DE AltName: Full=Sodium-dependent vitamin C transporter 2;
DE Short=SVCT-2;
DE Short=mSVCT2;
DE AltName: Full=Yolk sac permease-like molecule 2;
GN Name=Slc23a2;
GN Synonyms=Kiaa0238 {ECO:0000303|PubMed:12693553}, Svct2, Yspl2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=129/SvEv; TISSUE=Brain;
RX PubMed=11214969; DOI=10.1093/dnares/7.6.339;
RA Gispert S., Dutra A., Lieberman A., Friedlich D., Nussbaum R.L.;
RT "Cloning and genomic organization of the mouse gene slc23a1 encoding a
RT vitamin C transporter.";
RL DNA Res. 7:339-345(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-647 (ISOFORM 1).
RC TISSUE=Brain;
RA Fujita I., Hirano J., Tanaka K.;
RT "Mouse sodium dependent vitamin C transporter 2 (mSVCT2).";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 108-648 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [8]
RP TISSUE SPECIFICITY, AND DISEASE.
RX PubMed=17689499; DOI=10.1016/j.bcp.2007.05.024;
RA Wu X., Iguchi T., Hirano J., Fujita I., Ueda H., Itoh N., Tanaka K.,
RA Nakanishi T.;
RT "Upregulation of sodium-dependent vitamin C transporter 2 expression in
RT adrenals increases norepinephrine production and aggravates hyperlipidemia
RT in mice with streptozotocin-induced diabetes.";
RL Biochem. Pharmacol. 74:1020-1028(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-78; THR-79; SER-81
RP AND THR-647, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Sodium/ascorbate cotransporter. Mediates electrogenic uptake
CC of vitamin C, with a stoichiometry of 2 Na(+) for each ascorbate.
CC {ECO:0000250|UniProtKB:Q9UGH3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-ascorbate(out) + 2 Na(+)(out) = L-ascorbate(in) + 2
CC Na(+)(in); Xref=Rhea:RHEA:69883, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:38290; Evidence={ECO:0000250|UniProtKB:Q9UGH3};
CC -!- SUBUNIT: Interacts with CLSTN3. {ECO:0000250|UniProtKB:Q9UGH3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9UGH3};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9UGH3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9EPR4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9EPR4-2; Sequence=VSP_007367, VSP_007368;
CC -!- TISSUE SPECIFICITY: Expressed in metabolically active and specialized
CC tissues, including high expression in brain and adrenals. Detected in a
CC wide range of tissues. Expression in kidney is almost undetectable.
CC {ECO:0000269|PubMed:17689499}.
CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q9UGH3}.
CC -!- DISEASE: Note=Elevated expression levels in the adrenals of diabetic
CC mice. {ECO:0000269|PubMed:17689499}.
CC -!- SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2) (TC
CC 2.A.40) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG02252.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA90751.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC65509.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY004874; AAG02252.1; ALT_INIT; mRNA.
DR EMBL; AK087175; BAC39819.1; -; mRNA.
DR EMBL; AL831706; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL28341.1; -; Genomic_DNA.
DR EMBL; BC050823; AAH50823.1; -; mRNA.
DR EMBL; AB038145; BAA90751.1; ALT_INIT; mRNA.
DR EMBL; AK122227; BAC65509.1; ALT_SEQ; Transcribed_RNA.
DR CCDS; CCDS16769.1; -. [Q9EPR4-1]
DR RefSeq; NP_061294.2; NM_018824.2. [Q9EPR4-1]
DR RefSeq; XP_006499969.1; XM_006499906.3.
DR RefSeq; XP_006499970.1; XM_006499907.3. [Q9EPR4-1]
DR RefSeq; XP_011238000.1; XM_011239698.2. [Q9EPR4-1]
DR RefSeq; XP_017174620.1; XM_017319131.1.
DR AlphaFoldDB; Q9EPR4; -.
DR SMR; Q9EPR4; -.
DR BioGRID; 207613; 1.
DR STRING; 10090.ENSMUSP00000028815; -.
DR GlyCosmos; Q9EPR4; 2 sites, No reported glycans.
DR GlyGen; Q9EPR4; 2 sites.
DR iPTMnet; Q9EPR4; -.
DR PhosphoSitePlus; Q9EPR4; -.
DR SwissPalm; Q9EPR4; -.
DR EPD; Q9EPR4; -.
DR jPOST; Q9EPR4; -.
DR MaxQB; Q9EPR4; -.
DR PaxDb; 10090-ENSMUSP00000028815; -.
DR PeptideAtlas; Q9EPR4; -.
DR ProteomicsDB; 253366; -. [Q9EPR4-1]
DR ProteomicsDB; 253367; -. [Q9EPR4-2]
DR Pumba; Q9EPR4; -.
DR Antibodypedia; 42663; 143 antibodies from 23 providers.
DR DNASU; 54338; -.
DR Ensembl; ENSMUST00000028815.15; ENSMUSP00000028815.9; ENSMUSG00000027340.16. [Q9EPR4-1]
DR GeneID; 54338; -.
DR KEGG; mmu:54338; -.
DR UCSC; uc008mmi.1; mouse. [Q9EPR4-1]
DR UCSC; uc008mmj.1; mouse. [Q9EPR4-2]
DR AGR; MGI:1859682; -.
DR CTD; 9962; -.
DR MGI; MGI:1859682; Slc23a2.
DR VEuPathDB; HostDB:ENSMUSG00000027340; -.
DR eggNOG; KOG1292; Eukaryota.
DR GeneTree; ENSGT00950000182953; -.
DR HOGENOM; CLU_017959_5_4_1; -.
DR InParanoid; Q9EPR4; -.
DR OMA; NVSAYCR; -.
DR OrthoDB; 911690at2759; -.
DR PhylomeDB; Q9EPR4; -.
DR TreeFam; TF313272; -.
DR Reactome; R-MMU-196836; Vitamin C (ascorbate) metabolism.
DR BioGRID-ORCS; 54338; 2 hits in 79 CRISPR screens.
DR ChiTaRS; Slc23a2; mouse.
DR PRO; PR:Q9EPR4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9EPR4; Protein.
DR Bgee; ENSMUSG00000027340; Expressed in choroid plexus of fourth ventricle and 236 other cell types or tissues.
DR ExpressionAtlas; Q9EPR4; baseline and differential.
DR Genevisible; Q9EPR4; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0009925; C:basal plasma membrane; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0008520; F:L-ascorbate:sodium symporter activity; IMP:MGI.
DR GO; GO:0015229; F:L-ascorbic acid transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0071361; P:cellular response to ethanol; IEA:Ensembl.
DR GO; GO:0019852; P:L-ascorbic acid metabolic process; ISO:MGI.
DR GO; GO:0015882; P:L-ascorbic acid transmembrane transport; IDA:UniProtKB.
DR GO; GO:1903861; P:positive regulation of dendrite extension; ISO:MGI.
DR GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
DR InterPro; IPR006043; NCS2.
DR InterPro; IPR006042; Xan_ur_permease.
DR PANTHER; PTHR11119:SF33; SOLUTE CARRIER FAMILY 23 MEMBER 2; 1.
DR PANTHER; PTHR11119; XANTHINE-URACIL / VITAMIN C PERMEASE FAMILY MEMBER; 1.
DR Pfam; PF00860; Xan_ur_permease; 1.
DR PROSITE; PS01116; XANTH_URACIL_PERMASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell adhesion; Cell membrane; Glycoprotein;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Sodium; Sodium transport; Symport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..648
FT /note="Solute carrier family 23 member 2"
FT /id="PRO_0000165979"
FT TOPO_DOM 9..110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..139
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..216
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..286
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 287..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..307
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..369
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..415
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..459
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 481..483
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 484..504
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 505..514
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 515..535
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 536..545
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 546..566
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 567..648
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 75
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTW8"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 79
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 647
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 162..272
FT /note="LPLFQASAFAFLAPARAILSLDKWKCNTTEITVANGTAELLEHIWHPRIQEI
FT QGAIIMSSLIEVVIGLLGLPGALLRYIGPLTITPTVALIGLSGFQAAGERAGKHWGIAM
FT -> DYSCQWNGRAVGTHLASPNPRDPGGYHHVLTDRSGHWPPWPAWGSAEVYWTLDHHT
FT HRGPHWPLWFPGSRRESRKALGHCHAVSVLRELQGWGTIFTTMWDSLVEYLKQSH (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007367"
FT VAR_SEQ 273..648
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007368"
SQ SEQUENCE 648 AA; 70049 MW; 2590BB11B2A257CB CRC64;
MMGIGKNTAS KSVEAGGSTE GKYEEEAKHS NFFTLPVVIN GGATSSGEQD NEDTELMAIY
TTENGIAEKS SLAETLDSTG SLDPQRSDMI YTIEDVPPWY LCIFLGLQHY LTCFSGTIAV
PFLLADAMCV GDDQWATSQL IGTIFFCVGI TTLLQTTFGC RLPLFQASAF AFLAPARAIL
SLDKWKCNTT EITVANGTAE LLEHIWHPRI QEIQGAIIMS SLIEVVIGLL GLPGALLRYI
GPLTITPTVA LIGLSGFQAA GERAGKHWGI AMLTIFLVLL FSQYARNVKF PLPIYKSKKG
WTAYKFQLFK MFPIILAILV SWLLCFIFTV TDVFPSNSTD YGYYARTDAR KGVLLVAPWF
KVPYPFQWGM PTVSAAGVIG MLSAVVASII ESIGDYYACA RLSCAPPPPI HAINRGIFVE
GLSCVLDGIF GTGNGSTSSS PNIGVLGITK VGSRRVIQYG AALMLGLGMV GKFSALFASL
PDPVLGALFC TLFGMITAVG LSNLQFIDLN SSRNLFVLGF SIFFGLVLPS YLRQNPLVTG
ITGIDQILNV LLTTAMFVGG CVAFILDNTI PGTPEERGIK KWKKGVSKGS KSLDGMESYN
LPFGMNIIKK YRCFSYLPIS PTFAGYTWKG FGKSENSRSS DKDSQATV
//
