BANP_MOUSE
ID BANP_MOUSE Reviewed; 548 AA.
AC Q8VBU8; O88973; Q3U4R5; Q91YZ1; Q9ES51;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Protein BANP;
DE AltName: Full=Btg3-associated nuclear protein;
DE AltName: Full=Scaffold/matrix-associated region-1-binding protein;
GN Name=Banp; Synonyms=Smar1;
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 2), TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Embryo;
RX PubMed=10940556; DOI=10.1016/s0378-1119(00)00244-4;
RA Birot A.-M., Duret L., Bartholin L., Santalucia B., Tigaud I.,
RA Magaud J.-P., Rouault J.-P.;
RT "Identification and molecular analysis of BANP.";
RL Gene 253:189-196(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY, AND
RP FUNCTION.
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=10950932; DOI=10.1006/geno.2000.6279;
RA Chattopadhyay S., Kaul R., Charest A., Housman D., Chen J.;
RT "SMAR1, a novel, alternatively spliced gene product, binds the
RT Scaffold/Matrix-associated region at the T cell receptor beta locus.";
RL Genomics 68:93-96(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=NOD; TISSUE=Dendritic cell;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 311-548 (ISOFORM 4).
RC STRAIN=C57BL/6J, Czech II, and FVB/N;
RC TISSUE=Brain, Mammary tumor, and Salivary gland;
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 [5]
RP FUNCTION, INTERACTION WITH TP53, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12494467; DOI=10.1002/ijc.10881;
RA Kaul R., Mukherjee S., Ahmed F., Bhat M.K., Chhipa R., Galande S.,
RA Chattopadhyay S.;
RT "Direct interaction with and activation of p53 by SMAR1 retards cell-cycle
RT progression at G2/M phase and delays tumor growth in mice.";
RL Int. J. Cancer 103:606-615(2003).
RN [6]
RP FUNCTION, INTERACTION WITH CUX1, AND SUBCELLULAR LOCATION.
RX PubMed=15371550; DOI=10.1093/nar/gkh807;
RA Kaul-Ghanekar R., Jalota-Badhwar A., Pavithra L., Tucker P.,
RA Chattopadhyay S.;
RT "SMAR1 and Cux/CDP modulate chromatin and act as negative regulators of the
RT TCRbeta enhancer (Ebeta).";
RL Nucleic Acids Res. 32:4862-4875(2004).
RN [7]
RP FUNCTION.
RX PubMed=15623522; DOI=10.1074/jbc.m412206200;
RA Kaul-Ghanekar R., Majumdar S., Jalota-Badhwar A., Gulati N., Dubey N.,
RA Saha B., Chattopadhyay S.;
RT "Abnormal V(D)J recombination of T cell receptor beta locus in SMAR1
RT transgenic mice.";
RL J. Biol. Chem. 280:9450-9459(2005).
RN [8]
RP RETRACTED PAPER.
RX PubMed=15701641; DOI=10.1074/jbc.m413200200;
RA Jalota-Badhwar A., Singh K., Pavithra L., Kaul-Ghanekar R., Jameel S.,
RA Chattopadhyay S.;
RT "Tumor suppressor SMAR1 activates and stabilizes p53 through its arginine-
RT serine-rich motif.";
RL J. Biol. Chem. 280:16019-16029(2005).
RN [9]
RP RETRACTION NOTICE OF PUBMED:15701641.
RX PubMed=32144153; DOI=10.1074/jbc.w120.012894;
RA Jalota A., Singh K., Pavithra L., Kaul-Ghanekar R., Jameel S.,
RA Chattopadhyay S.;
RL J. Biol. Chem. 295:3390-3390(2020).
RN [10]
RP FUNCTION, INTERACTION WITH HDAC1, IDENTIFICATION IN A COMPLEX WITH HDAC1;
RP SIN3A; SIN3B; RBL1 AND RBL2, AND SUBCELLULAR LOCATION.
RX PubMed=16166625; DOI=10.1128/mcb.25.19.8415-8429.2005;
RA Rampalli S., Pavithra L., Bhatt A., Kundu T.K., Chattopadhyay S.;
RT "Tumor suppressor SMAR1 mediates cyclin D1 repression by recruitment of the
RT SIN3/histone deacetylase 1 complex.";
RL Mol. Cell. Biol. 25:8415-8429(2005).
RN [11]
RP FUNCTION, PHOSPHORYLATION AT SER-347, AND MUTAGENESIS OF SER-347; SER-348;
RP SER-349 AND SER-350.
RX PubMed=17229733; DOI=10.1074/jbc.m608434200;
RA Jalota-Badhwar A., Kaul-Ghanekar R., Mogare D., Boppana R., Paknikar K.M.,
RA Chattopadhyay S.;
RT "SMAR1-derived P44 peptide retains its tumor suppressor function through
RT modulation of p53.";
RL J. Biol. Chem. 282:9902-9913(2007).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-283, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Controls V(D)J recombination during T-cell development by
CC repressing T-cell receptor (TCR) beta enhancer function. Binds to
CC scaffold/matrix attachment region beta (S/MARbeta), an ATC-rich DNA
CC sequence located upstream of the TCR beta enhancer. Represses cyclin D1
CC transcription by recruiting HDAC1 to its promoter, thereby diminishing
CC H3K9ac, H3S10ph and H4K8ac levels. Promotes TP53 activation, which
CC causes cell cycle arrest and inhibits tumor growth (PubMed:12494467).
CC {ECO:0000269|PubMed:10950932, ECO:0000269|PubMed:12494467,
CC ECO:0000269|PubMed:15371550, ECO:0000269|PubMed:15623522,
CC ECO:0000269|PubMed:16166625, ECO:0000269|PubMed:17229733}.
CC -!- SUBUNIT: Interacts with TP53 (PubMed:12494467). Interacts with CUX1/CDP
CC (PubMed:15371550). Interacts with HDAC1 (PubMed:16166625). Part of a
CC corepressor complex containing BANP, HDAC1, SIN3A, SIN3B, RBL1 and RBL2
CC (PubMed:16166625). {ECO:0000269|PubMed:12494467,
CC ECO:0000269|PubMed:15371550, ECO:0000269|PubMed:16166625}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10940556,
CC ECO:0000269|PubMed:12494467, ECO:0000269|PubMed:15371550,
CC ECO:0000269|PubMed:16166625}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Long;
CC IsoId=Q8VBU8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VBU8-2; Sequence=VSP_027403;
CC Name=3; Synonyms=Short;
CC IsoId=Q8VBU8-3; Sequence=VSP_027403, VSP_027404;
CC Name=4;
CC IsoId=Q8VBU8-4; Sequence=VSP_027405;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, spleen, and thymus.
CC Isoform 1 is highly expressed in kidney, brain and testis. Isoform 3 is
CC highly expressed in kidney and lung. {ECO:0000269|PubMed:10940556,
CC ECO:0000269|PubMed:10950932, ECO:0000269|PubMed:12494467}.
CC -!- SIMILARITY: Belongs to the BANP/SMAR1 family. {ECO:0000305}.
CC -!- CAUTION: Interaction with TP35 was reported to promotes TP53 'Ser-15'
CC phosphorylation and nuclear accumulation causing cell cycle arrest and
CC inhibition of tumor growth (PubMed:15701641). However, the publication
CC has been retracted due to image duplication and manipulation.
CC Interaction with TP35 has been confirmed by other studies
CC (PubMed:12494467). The nuclear locatization has been confirmed by other
CC studies (PubMed:10940556, PubMed:12494467, PubMed:15371550,
CC PubMed:16166625). {ECO:0000269|PubMed:10940556,
CC ECO:0000269|PubMed:12494467, ECO:0000269|PubMed:15371550,
CC ECO:0000269|PubMed:15701641, ECO:0000269|PubMed:16166625,
CC ECO:0000305|PubMed:32144153}.
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DR EMBL; AF091234; AAC36358.1; -; mRNA.
DR EMBL; AF235503; AAG16659.1; -; mRNA.
DR EMBL; AK154088; BAE32366.1; -; mRNA.
DR EMBL; BC013339; AAH13339.1; -; mRNA.
DR EMBL; BC021650; AAH21650.1; -; mRNA.
DR EMBL; BC022168; AAH22168.1; -; mRNA.
DR EMBL; BC062641; AAH62641.1; -; mRNA.
DR CCDS; CCDS40502.1; -. [Q8VBU8-1]
DR CCDS; CCDS72176.1; -. [Q8VBU8-2]
DR CCDS; CCDS72177.1; -. [Q8VBU8-3]
DR RefSeq; NP_001103570.1; NM_001110100.2.
DR RefSeq; NP_001272910.1; NM_001285981.1. [Q8VBU8-2]
DR RefSeq; NP_001272912.1; NM_001285983.1. [Q8VBU8-3]
DR RefSeq; NP_058092.2; NM_016812.4. [Q8VBU8-1]
DR RefSeq; XP_011246744.1; XM_011248442.1. [Q8VBU8-4]
DR RefSeq; XP_017168388.1; XM_017312899.1. [Q8VBU8-1]
DR AlphaFoldDB; Q8VBU8; -.
DR SMR; Q8VBU8; -.
DR BioGRID; 207288; 1.
DR IntAct; Q8VBU8; 1.
DR STRING; 10090.ENSMUSP00000132095; -.
DR iPTMnet; Q8VBU8; -.
DR PhosphoSitePlus; Q8VBU8; -.
DR EPD; Q8VBU8; -.
DR MaxQB; Q8VBU8; -.
DR PaxDb; Q8VBU8; -.
DR PeptideAtlas; Q8VBU8; -.
DR PRIDE; Q8VBU8; -.
DR ProteomicsDB; 273537; -. [Q8VBU8-1]
DR ProteomicsDB; 273538; -. [Q8VBU8-2]
DR ProteomicsDB; 273539; -. [Q8VBU8-3]
DR ProteomicsDB; 273540; -. [Q8VBU8-4]
DR Antibodypedia; 30702; 164 antibodies from 31 providers.
DR DNASU; 53325; -.
DR Ensembl; ENSMUST00000026354; ENSMUSP00000026354; ENSMUSG00000025316. [Q8VBU8-2]
DR Ensembl; ENSMUST00000093078; ENSMUSP00000090766; ENSMUSG00000025316. [Q8VBU8-3]
DR Ensembl; ENSMUST00000170857; ENSMUSP00000132095; ENSMUSG00000025316. [Q8VBU8-1]
DR Ensembl; ENSMUST00000173254; ENSMUSP00000133783; ENSMUSG00000025316. [Q8VBU8-4]
DR GeneID; 53325; -.
DR KEGG; mmu:53325; -.
DR UCSC; uc009nsg.3; mouse. [Q8VBU8-1]
DR UCSC; uc009nsh.3; mouse. [Q8VBU8-3]
DR UCSC; uc033jih.1; mouse. [Q8VBU8-2]
DR CTD; 54971; -.
DR MGI; MGI:1889023; Banp.
DR VEuPathDB; HostDB:ENSMUSG00000025316; -.
DR eggNOG; ENOG502QRIF; Eukaryota.
DR GeneTree; ENSGT00390000011116; -.
DR InParanoid; Q8VBU8; -.
DR OMA; VSREHTK; -.
DR OrthoDB; 1401911at2759; -.
DR PhylomeDB; Q8VBU8; -.
DR TreeFam; TF331908; -.
DR Reactome; R-MMU-6804759; Regulation of TP53 Activity through Association with Co-factors.
DR BioGRID-ORCS; 53325; 18 hits in 59 CRISPR screens.
DR ChiTaRS; Banp; mouse.
DR PRO; PR:Q8VBU8; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8VBU8; protein.
DR Bgee; ENSMUSG00000025316; Expressed in embryonic post-anal tail and 184 other tissues.
DR ExpressionAtlas; Q8VBU8; baseline and differential.
DR Genevisible; Q8VBU8; MM.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:CACAO.
DR GO; GO:0034504; P:protein localization to nucleus; IBA:GO_Central.
DR InterPro; IPR042343; BANP.
DR InterPro; IPR018379; BEN_domain.
DR PANTHER; PTHR16243; PTHR16243; 1.
DR Pfam; PF10523; BEN; 1.
DR SMART; SM01025; BEN; 1.
DR PROSITE; PS51457; BEN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Chromatin regulator;
KW Coiled coil; Developmental protein; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..548
FT /note="Protein BANP"
FT /id="PRO_0000297911"
FT DOMAIN 234..330
FT /note="BEN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00784"
FT REGION 160..350
FT /note="Interaction with CUX1 and HDAC1"
FT /evidence="ECO:0000269|PubMed:15371550,
FT ECO:0000269|PubMed:16166625"
FT REGION 174..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..400
FT /note="DNA-binding"
FT COILED 65..98
FT /evidence="ECO:0000255"
FT COMPBIAS 189..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 347
FT /note="Required for TP53 activation"
FT /evidence="ECO:0000269|PubMed:17229733"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N9N5"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N9N5"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N9N5"
FT MOD_RES 283
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:17229733"
FT CROSSLNK 141
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N9N5"
FT VAR_SEQ 122..160
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10940556,
FT ECO:0000303|PubMed:10950932, ECO:0000303|PubMed:16141072"
FT /id="VSP_027403"
FT VAR_SEQ 399..401
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10950932,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_027404"
FT VAR_SEQ 435..476
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027405"
FT MUTAGEN 347
FT /note="S->A: Impairs TP53 activation."
FT /evidence="ECO:0000269|PubMed:17229733"
FT MUTAGEN 348
FT /note="S->A: No effect on TP53 activation."
FT /evidence="ECO:0000269|PubMed:17229733"
FT MUTAGEN 349
FT /note="S->A: No effect on TP53 activation."
FT /evidence="ECO:0000269|PubMed:17229733"
FT MUTAGEN 350
FT /note="S->A: No effect on TP53 activation."
FT /evidence="ECO:0000269|PubMed:17229733"
FT CONFLICT 131
FT /note="N -> I (in Ref. 2; AAG16659)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="S -> I (in Ref. 2; AAG16659)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 548 AA; 59657 MW; 9C48D5E122ECB2D1 CRC64;
MMSEQDLADV VQIAVEDLSP DHPVVLENHV VTDDDEPALK RQRLEINCQD PSIKSFLYSI
NQTICLRLDS IEAKLQALEA TCKSLEEKLD LVTNKQHSPI QVPMVAGSPL GATQTCNKVR
CVVPQTTVIL NNDRQNAIVA KMEDPLSNRA PDSLENIISN AVPGRRQNTI VVKVPGQDDS
HNEDGESGSE ASDSVSNCGQ PGSQNIGSNV TLITLNSEED YPNGTWLGDE NNPEMRVRCA
IIPSDMLHIS TNCRTAEKMA LTLLDYLFHR EVQAVSNLSG QGKHGKKQLD PLTIYGIRCH
LFYKFGITES DWYRIKQSID SKCRTAWRRK QRGQSLAVKS FSRRTPSSSS YSASETMMGT
PPPTSELQQS QPQALHYALA NAQQVQIHQI GEDGQVQVIP QGHLHIAQVP QGEQVQITQD
SEGNLQIHHV GQDGQSWGLC QNPIPVSGDS VAQANPSQLW PLGGDTLDLP AGNEMIQVLQ
GAQLIAVASS DPAATGVDGS PLQGSDIQVQ YVQLAPVSDH TAAAQTAEAL QPTLQPDMQL
EHGAIQIQ
