SHSA7_MOUSE
ID SHSA7_MOUSE Reviewed; 558 AA.
AC Q8C3Q5; A0A172Q401; A0A172Q418; Q3UMB3;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Protein shisa-7 {ECO:0000305};
DE AltName: Full=Cystine-knot AMPAR modulating protein of 59 kDa {ECO:0000303|PubMed:26623514, ECO:0000303|PubMed:29199957};
DE Short=CKAMP59 {ECO:0000303|PubMed:26623514, ECO:0000303|PubMed:29199957};
DE AltName: Full=GABA(A) receptor auxiliary subunit Shisa7 {ECO:0000303|PubMed:31601770};
DE AltName: Full=Shisa family member 7 {ECO:0000305};
DE Flags: Precursor;
GN Name=Shisa7 {ECO:0000303|PubMed:29199957, ECO:0000312|MGI:MGI:3605641};
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] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION,
RP IDENTIFICATION (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, INTERACTION WITH
RP GRIA1 AND GRIA2, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6N;
RX PubMed=26623514; DOI=10.7554/elife.09693;
RA Farrow P., Khodosevich K., Sapir Y., Schulmann A., Aslam M., Stern-Bach Y.,
RA Monyer H., von Engelhardt J.;
RT "Auxiliary subunits of the CKAMP family differentially modulate AMPA
RT receptor properties.";
RL Elife 4:E09693-E09693(2015).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-558 (ISOFORM 2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 184-558 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Lung, and Mammary gland;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438 AND THR-532, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY,
RP DISRUPTION PHENOTYPE, IDENTIFICATION IN AMPAR COMPLEX, AND MUTAGENESIS OF
RP 555-GLU--VAL-558.
RX PubMed=29199957; DOI=10.7554/elife.24192;
RA Schmitz L.J.M., Klaassen R.V., Ruiperez-Alonso M., Zamri A.E., Stroeder J.,
RA Rao-Ruiz P., Lodder J.C., van der Loo R.J., Mansvelder H.D., Smit A.B.,
RA Spijker S.;
RT "The AMPA receptor-associated protein Shisa7 regulates hippocampal synaptic
RT function and contextual memory.";
RL Elife 6:0-0(2017).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH GABRA1; GABRA2 AND GABRG2,
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=31601770; DOI=10.1126/science.aax5719;
RA Han W., Li J., Pelkey K.A., Pandey S., Chen X., Wang Y.X., Wu K., Ge L.,
RA Li T., Castellano D., Liu C., Wu L.G., Petralia R.S., Lynch J.W.,
RA McBain C.J., Lu W.;
RT "Shisa7 is a GABAA receptor auxiliary subunit controlling benzodiazepine
RT actions.";
RL Science 366:246-250(2019).
CC -!- FUNCTION: Transmembrane protein that regulates gamma-aminobutyric acid
CC type A receptor (GABA(A)R) trafficking, channel deactivation kinetics
CC and pharmacology, necessary for fast inhibitory transmission in the
CC brain (PubMed:31601770). Enhances the action of benzodiazepine, a
CC primary GABA(A)Rs target drug, in the brain (PubMed:31601770). May
CC affect channel kinetics of AMPA-type glutamate receptors (AMPAR), the
CC brain's main excitatory neurotransmitter, necessary for synaptic
CC hippocampal plasticity, and memory recall (Probable). May regulate the
CC induction and maintenance of long-term potentiation at Schaffer
CC collaterals/CA3-CA1 excitatory synapses (Probable).
CC {ECO:0000269|PubMed:31601770, ECO:0000305|PubMed:26623514,
CC ECO:0000305|PubMed:29199957}.
CC -!- SUBUNIT: Interacts with GABA(A)R (GABA type A receptor) subunits
CC GABRA1, GABRA2 and GABRG2; the interaction is direct (PubMed:31601770).
CC Does not interact with GABRB2 and GABRB3 subunits (PubMed:31601770).
CC Interacts with AMPAR subunits GRIA1, GRIA2 and GRIA3 and AMPAR
CC auxiliary proteins SHISA6 and SHISA7 in heterologous cells
CC (PubMed:26623514, PubMed:29199957). Interacts (via PDZ-binding motif)
CC with DLG4/PSD-95 (via PDZ domain)in heterologous cells; the interaction
CC is direct (PubMed:29199957). {ECO:0000269|PubMed:26623514,
CC ECO:0000269|PubMed:29199957, ECO:0000269|PubMed:31601770}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic density membrane
CC {ECO:0000269|PubMed:29199957, ECO:0000269|PubMed:31601770}; Single-pass
CC type I membrane protein {ECO:0000305|PubMed:29199957}. Note=Localizes
CC at GABAergic inhibitory synapses and colocalizes with gephyrin in
CC hippocampal neurons. {ECO:0000269|PubMed:31601770}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C3Q5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C3Q5-2; Sequence=VSP_034790;
CC -!- TISSUE SPECIFICITY: Mainly expressed in neurons (PubMed:26623514,
CC PubMed:29199957, PubMed:31601770). Highly expressed in brain structures
CC including cortex, striatum, olfactory bulb, amygdala hippocampus CA1-3
CC and dentate gyrus (at protein level) (PubMed:26623514, PubMed:29199957,
CC PubMed:31601770). {ECO:0000269|PubMed:26623514,
CC ECO:0000269|PubMed:29199957, ECO:0000269|PubMed:31601770}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the cerebral cortex on 17 dpc and in
CC olfactory bulb and hippocampus on postnatal day 1 (P1)
CC (PubMed:26623514). Expression in hippocampus increases during postnatal
CC development and reaches a plateau after 3 weeks (PubMed:29199957).
CC Expression is high during prenatal development and decreases in the
CC thalamus and brainstem during postnatal development (PubMed:26623514).
CC {ECO:0000269|PubMed:26623514, ECO:0000269|PubMed:29199957}.
CC -!- DOMAIN: The GRID (GABA(A)R-interacting domain) is critical for its
CC subcellular localization and interaction with GABA(A)R.
CC {ECO:0000269|PubMed:31601770}.
CC -!- DOMAIN: The PDZ-binding motif interacts with PDZ-domain of scaffolding
CC protein DLG4 in heterologous cells. {ECO:0000269|PubMed:29199957}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:29199957}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice show a decrease in miniature
CC inhibitory postsynaptic currents frequency, but not amplitude, in CA1
CC pyramidal neurons (PubMed:31601770). Mice show impaired acquisition of
CC contextual fear memory without affecting auditory fear learning or
CC anxiety (PubMed:29199957). Decreased long-term potentiation of
CC hippocampal glutamatergic synapses (PubMed:29199957).
CC {ECO:0000269|PubMed:29199957, ECO:0000269|PubMed:31601770}.
CC -!- SIMILARITY: Belongs to the shisa family. {ECO:0000305}.
CC -!- CAUTION: SHISA7 has been reported to interact with AMPAR subunit GRIA1
CC in heterologous conditions and in the brain (PubMed:26623514,
CC PubMed:29199957). However, it was later demonstrated that SHISA7 does
CC not colocalize neither interact with AMPAR, but with GABA(A)R
CC (PubMed:31601770). Therefore additional experiments are needed to
CC understand the discrepancy for SHISA7 function.
CC {ECO:0000269|PubMed:26623514, ECO:0000269|PubMed:29199957,
CC ECO:0000269|PubMed:31601770, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC39371.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; KU707906; AND76929.1; -; mRNA.
DR EMBL; KU707907; AND76930.1; -; mRNA.
DR EMBL; AC162034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK085127; BAC39371.1; ALT_INIT; mRNA.
DR EMBL; AK145016; BAE26185.1; -; mRNA.
DR CCDS; CCDS71882.1; -. [Q8C3Q5-2]
DR RefSeq; NP_001277220.1; NM_001290291.1. [Q8C3Q5-2]
DR RefSeq; NP_766325.3; NM_172737.4. [Q8C3Q5-1]
DR RefSeq; XP_006539838.1; XM_006539775.3. [Q8C3Q5-1]
DR RefSeq; XP_011248805.1; XM_011250503.1. [Q8C3Q5-1]
DR RefSeq; XP_017177636.1; XM_017322147.1. [Q8C3Q5-1]
DR AlphaFoldDB; Q8C3Q5; -.
DR SMR; Q8C3Q5; -.
DR BioGRID; 231300; 3.
DR IntAct; Q8C3Q5; 3.
DR MINT; Q8C3Q5; -.
DR STRING; 10090.ENSMUSP00000064886; -.
DR GlyConnect; 2643; 1 N-Linked glycan (1 site).
DR GlyGen; Q8C3Q5; 2 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q8C3Q5; -.
DR PhosphoSitePlus; Q8C3Q5; -.
DR SwissPalm; Q8C3Q5; -.
DR MaxQB; Q8C3Q5; -.
DR PaxDb; Q8C3Q5; -.
DR PeptideAtlas; Q8C3Q5; -.
DR PRIDE; Q8C3Q5; -.
DR ProteomicsDB; 255425; -. [Q8C3Q5-1]
DR ProteomicsDB; 255426; -. [Q8C3Q5-2]
DR Antibodypedia; 52662; 70 antibodies from 18 providers.
DR DNASU; 232813; -.
DR Ensembl; ENSMUST00000066041; ENSMUSP00000064886; ENSMUSG00000053550. [Q8C3Q5-1]
DR Ensembl; ENSMUST00000119433; ENSMUSP00000112423; ENSMUSG00000053550. [Q8C3Q5-2]
DR GeneID; 232813; -.
DR KEGG; mmu:232813; -.
DR UCSC; uc009eyu.2; mouse. [Q8C3Q5-1]
DR UCSC; uc009eyv.3; mouse. [Q8C3Q5-2]
DR CTD; 729956; -.
DR MGI; MGI:3605641; Shisa7.
DR VEuPathDB; HostDB:ENSMUSG00000053550; -.
DR eggNOG; ENOG502QV92; Eukaryota.
DR GeneTree; ENSGT00940000162254; -.
DR InParanoid; Q8C3Q5; -.
DR OMA; HNYIHLN; -.
DR OrthoDB; 475894at2759; -.
DR PhylomeDB; Q8C3Q5; -.
DR TreeFam; TF330800; -.
DR BioGRID-ORCS; 232813; 1 hit in 67 CRISPR screens.
DR PRO; PR:Q8C3Q5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8C3Q5; protein.
DR Bgee; ENSMUSG00000053550; Expressed in superior frontal gyrus and 121 other tissues.
DR ExpressionAtlas; Q8C3Q5; baseline and differential.
DR Genevisible; Q8C3Q5; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098985; C:asymmetric, glutamatergic, excitatory synapse; IDA:UniProtKB.
DR GO; GO:0032591; C:dendritic spine membrane; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; IDA:SynGO.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0050811; F:GABA receptor binding; IDA:UniProtKB.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IDA:UniProtKB.
DR GO; GO:0097112; P:gamma-aminobutyric acid receptor clustering; IDA:UniProtKB.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IDA:UniProtKB.
DR GO; GO:0007613; P:memory; IMP:UniProtKB.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IMP:UniProtKB.
DR GO; GO:1904717; P:regulation of AMPA glutamate receptor clustering; IMP:UniProtKB.
DR GO; GO:0106040; P:regulation of GABA-A receptor activity; IDA:UniProtKB.
DR GO; GO:0098962; P:regulation of postsynaptic neurotransmitter receptor activity; IDA:SynGO.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IBA:GO_Central.
DR InterPro; IPR026910; Shisa.
DR PANTHER; PTHR31774; PTHR31774; 1.
DR Pfam; PF13908; Shisa; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Glycoprotein; Membrane;
KW Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Signal;
KW Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..558
FT /note="Protein shisa-7"
FT /id="PRO_0000344473"
FT TOPO_DOM 23..189
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..558
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 53..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..175
FT /note="GRID"
FT /evidence="ECO:0000269|PubMed:31601770"
FT REGION 236..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 555..558
FT /note="PDZ-binding"
FT /evidence="ECO:0000269|PubMed:29199957"
FT COMPBIAS 57..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 532
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 280..296
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000269|PubMed:26623514"
FT /id="VSP_034790"
FT MUTAGEN 154..175
FT /note="Missing: Abolishes the colocalization with GPHN."
FT /evidence="ECO:0000269|PubMed:31601770"
FT MUTAGEN 555..558
FT /note="Missing: Loss of interaction with PDZ-domain of
FT DLG4."
FT /evidence="ECO:0000269|PubMed:29199957"
FT CONFLICT 202
FT /note="V -> M (in Ref. 3; BAC39371)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 558 AA; 58334 MW; BEDD9B53CE4C8D71 CRC64;
MPALLLLGTV ALLASAAGPA GARPSNDTSS VAPGPLPALL AHLRRLTGAL AGGGSAAGTS
ANATKTSPAS GTGAAARAPP PAELCHGYYD VMGQYDATFN CSTGSYRFCC GTCHYRFCCE
HRHMRLAQAS CSNYDTPRWA TTPPPLAGGA GGAGGAGGGP GPGQAGWLEG GRAGGAGGRG
GEGPGGSTAY VVCGVISFAL AVGVGAKVAF SKASRAPRAH REINVPRALV DILRHQAGPA
TRPDRARSSS LTPGLGGPDS MAPRTPKNLY NTMKPSNLDN LHYNVNSPKH HAATLDWRAM
PPPSPSLHYS TLSCSRSFHN LSHLPPSYEA AVKSELNRYS SLKRLAEKDL DEAYLKRRQL
EMPRGTLPLH ALRRPGTGGG YRMDGWGGPE ELGLAPAPNP RRVMSQEHLL GDGSRASRYE
FTLPRARLVS QEHLLLSSPE ALRQSREHLL SPPRSPALPP DPTTRASLAA SHSNLLLGPG
GPPTPLHGLP PSGLHAHHHH ALHGSPQPAW MSDAGGGGGT LARRPPFQRQ GTLEQLQFIP
GHHLPQHLRT ASKNEVTV
