CFI1_ARATH
ID CFI1_ARATH Reviewed; 246 AA.
AC P41088; Q8W532; Q9LE13; Q9LF74; Q9LF75;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Chalcone--flavanone isomerase 1;
DE Short=Chalcone isomerase 1;
DE EC=5.5.1.6;
DE AltName: Full=Protein TRANSPARENT TESTA 5;
GN Name=CHI1; Synonyms=CFI, TT5; OrderedLocusNames=At3g55120;
GN ORFNames=T15C9_120;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=1354004; DOI=10.2307/3869544;
RA Shirley B.W., Hanley S., Goodman H.M.;
RT "Effects of ionizing radiation on a plant genome: analysis of two
RT Arabidopsis transparent testa mutations.";
RL Plant Cell 4:333-347(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Gr-5, cv. Ita-0, cv. Mh-0, cv. Per-1, cv. Rv-1, and cv. Wlp-2;
RX PubMed=10835405; DOI=10.1093/genetics/155.2.863;
RA Kuittinen H., Aguade M.;
RT "Nucleotide variation at the chalcone isomerase locus in Arabidopsis
RT thaliana.";
RL Genetics 155:863-872(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Gran-10, cv. Gran-2, cv. Gran-3, cv. Gran-4, cv. Gran-5,
RC cv. Gran-6, cv. Gran-7, cv. Gran-8, cv. Gran-9, cv. Lu-2, cv. Lu-3,
RC cv. Lu-4, cv. Lu-5, cv. Lu-6, cv. Lu-7, cv. Lu-8, cv. Rv-10, cv. Rv-2,
RC cv. Rv-3, cv. Rv-4, cv. Rv-5, cv. Rv-6, cv. Rv-7, cv. Rv-8, cv. Rv-9,
RC cv. Tv-10, cv. Tv-2, cv. Tv-3, cv. Tv-4, cv. Tv-5, cv. Tv-6, cv. Tv-7,
RC cv. Tv-8, cv. Tv-9, cv. Wlp-10, cv. Wlp-2, cv. Wlp-3, cv. Wlp-4, cv. Wlp-5,
RC cv. Wlp-6, cv. Wlp-7, cv. Wlp-8, and cv. Wlp-9;
RX PubMed=12411612; DOI=10.1093/oxfordjournals.molbev.a004027;
RA Kuittinen H., Salguero D., Aguade M.;
RT "Parallel patterns of sequence variation within and between populations at
RT three loci of Arabidopsis thaliana.";
RL Mol. Biol. Evol. 19:2030-2034(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION BY LIGHT.
RC STRAIN=cv. Columbia;
RX PubMed=15821875; DOI=10.1007/s11103-004-6910-0;
RA Hartmann U., Sagasser M., Mehrtens F., Stracke R., Weisshaar B.;
RT "Differential combinatorial interactions of cis-acting elements recognized
RT by R2R3-MYB, BZIP, and BHLH factors control light-responsive and tissue-
RT specific activation of phenylpropanoid biosynthesis genes.";
RL Plant Mol. Biol. 57:155-171(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=23473981; DOI=10.1016/j.plaphy.2013.02.001;
RA Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M.,
RA Tohge T., Fernie A.R.;
RT "The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic
RT diversity.";
RL Plant Physiol. Biochem. 72:21-34(2013).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
RX PubMed=22622584; DOI=10.1038/nature11009;
RA Ngaki M.N., Louie G.V., Philippe R.N., Manning G., Pojer F., Bowman M.E.,
RA Li L., Larsen E., Wurtele E.S., Noel J.P.;
RT "Evolution of the chalcone-isomerase fold from fatty-acid binding to
RT stereospecific catalysis.";
RL Nature 485:530-533(2012).
CC -!- FUNCTION: Catalyzes the intramolecular cyclization of bicyclic
CC chalcones into tricyclic (S)-flavanones. Responsible for the
CC isomerization of 4,2',4',6'-tetrahydroxychalcone (also termed chalcone)
CC into naringenin. {ECO:0000269|PubMed:1354004}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a chalcone = a flavanone.; EC=5.5.1.6;
CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC -!- INTERACTION:
CC P41088; P13114: CHS; NbExp=4; IntAct=EBI-1546761, EBI-1546775;
CC -!- TISSUE SPECIFICITY: Mostly expressed in siliques and flowers, and, to a
CC lower extent, in leaves. {ECO:0000269|PubMed:15821875}.
CC -!- INDUCTION: By light. {ECO:0000269|PubMed:15821875}.
CC -!- MISCELLANEOUS: Part of the biosynthetic pathway for all classes of
CC flavonoids, a large class of secondary plant metabolites, many of which
CC are brightly colored.
CC -!- SIMILARITY: Belongs to the chalcone isomerase family. {ECO:0000305}.
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DR EMBL; M86358; AAA32766.1; -; Genomic_DNA.
DR EMBL; AJ287299; CAB94969.1; -; Genomic_DNA.
DR EMBL; AJ287300; CAB94970.1; -; Genomic_DNA.
DR EMBL; AJ287301; CAB94971.1; -; Genomic_DNA.
DR EMBL; AJ287302; CAB94972.1; -; Genomic_DNA.
DR EMBL; AJ287303; CAB94973.1; -; Genomic_DNA.
DR EMBL; AJ287304; CAB94974.1; -; Genomic_DNA.
DR EMBL; AJ287305; CAB94975.1; -; Genomic_DNA.
DR EMBL; AJ287306; CAB94976.1; -; Genomic_DNA.
DR EMBL; AJ287307; CAB94977.1; -; Genomic_DNA.
DR EMBL; AJ287308; CAB94978.1; -; Genomic_DNA.
DR EMBL; AJ287309; CAB94979.1; -; Genomic_DNA.
DR EMBL; AJ287310; CAB94980.1; -; Genomic_DNA.
DR EMBL; AJ287311; CAB94981.1; -; Genomic_DNA.
DR EMBL; AJ287312; CAB94982.1; -; Genomic_DNA.
DR EMBL; AJ287313; CAB94983.1; -; Genomic_DNA.
DR EMBL; AJ287314; CAB94984.1; -; Genomic_DNA.
DR EMBL; AJ287315; CAB94985.1; -; Genomic_DNA.
DR EMBL; AJ287316; CAB94986.1; -; Genomic_DNA.
DR EMBL; AJ287317; CAB94987.1; -; Genomic_DNA.
DR EMBL; AJ287318; CAB94988.1; -; Genomic_DNA.
DR EMBL; AJ287319; CAB94989.1; -; Genomic_DNA.
DR EMBL; AJ287320; CAB94990.1; -; Genomic_DNA.
DR EMBL; AJ287321; CAB94991.1; -; Genomic_DNA.
DR EMBL; AJ492461; CAD42187.1; -; Genomic_DNA.
DR EMBL; AJ492462; CAD42188.1; -; Genomic_DNA.
DR EMBL; AJ492463; CAD42189.1; -; Genomic_DNA.
DR EMBL; AJ492464; CAD42190.1; -; Genomic_DNA.
DR EMBL; AJ492465; CAD42191.1; -; Genomic_DNA.
DR EMBL; AJ492466; CAD42192.1; -; Genomic_DNA.
DR EMBL; AJ492467; CAD42193.1; -; Genomic_DNA.
DR EMBL; AJ492468; CAD42194.1; -; Genomic_DNA.
DR EMBL; AJ492469; CAD42195.1; -; Genomic_DNA.
DR EMBL; AJ492470; CAD42196.1; -; Genomic_DNA.
DR EMBL; AJ492471; CAD42197.1; -; Genomic_DNA.
DR EMBL; AJ492472; CAD42198.1; -; Genomic_DNA.
DR EMBL; AJ492473; CAD42199.1; -; Genomic_DNA.
DR EMBL; AJ492474; CAD42200.1; -; Genomic_DNA.
DR EMBL; AJ492475; CAD42201.1; -; Genomic_DNA.
DR EMBL; AJ492476; CAD42202.1; -; Genomic_DNA.
DR EMBL; AJ492477; CAD42203.1; -; Genomic_DNA.
DR EMBL; AJ492478; CAD42204.1; -; Genomic_DNA.
DR EMBL; AJ492479; CAD42205.1; -; Genomic_DNA.
DR EMBL; AJ492480; CAD42206.1; -; Genomic_DNA.
DR EMBL; AJ492481; CAD42207.1; -; Genomic_DNA.
DR EMBL; AJ492482; CAD42208.1; -; Genomic_DNA.
DR EMBL; AJ492483; CAD42209.1; -; Genomic_DNA.
DR EMBL; AJ492484; CAD42210.1; -; Genomic_DNA.
DR EMBL; AJ492485; CAD42211.1; -; Genomic_DNA.
DR EMBL; AJ492486; CAD42212.1; -; Genomic_DNA.
DR EMBL; AJ492487; CAD42213.1; -; Genomic_DNA.
DR EMBL; AJ492488; CAD42214.1; -; Genomic_DNA.
DR EMBL; AJ492489; CAD42215.1; -; Genomic_DNA.
DR EMBL; AJ492490; CAD42216.1; -; Genomic_DNA.
DR EMBL; AJ492491; CAD42217.1; -; Genomic_DNA.
DR EMBL; AJ492492; CAD42218.1; -; Genomic_DNA.
DR EMBL; AJ492493; CAD42219.1; -; Genomic_DNA.
DR EMBL; AJ492494; CAD42220.1; -; Genomic_DNA.
DR EMBL; AJ492495; CAD42221.1; -; Genomic_DNA.
DR EMBL; AJ492496; CAD42222.1; -; Genomic_DNA.
DR EMBL; AJ492497; CAD42223.1; -; Genomic_DNA.
DR EMBL; AJ492498; CAD42224.1; -; Genomic_DNA.
DR EMBL; AJ492499; CAD42225.1; -; Genomic_DNA.
DR EMBL; AJ492500; CAD42226.1; -; Genomic_DNA.
DR EMBL; AJ492501; CAD42227.1; -; Genomic_DNA.
DR EMBL; AJ492502; CAD42228.1; -; Genomic_DNA.
DR EMBL; AJ492503; CAD42229.1; -; Genomic_DNA.
DR EMBL; AJ418046; CAD10782.1; -; mRNA.
DR EMBL; AF439537; AAL35225.1; -; Genomic_DNA.
DR EMBL; AL132970; CAB82707.2; -; Genomic_DNA.
DR EMBL; CP002686; AEE79342.1; -; Genomic_DNA.
DR EMBL; BT004265; AAO42267.1; -; mRNA.
DR EMBL; BT005528; AAO63948.1; -; mRNA.
DR EMBL; AY086088; AAM63295.1; -; mRNA.
DR PIR; JQ1687; JQ1687.
DR PIR; T47651; T47651.
DR RefSeq; NP_191072.1; NM_115370.4.
DR PDB; 4DOI; X-ray; 1.55 A; A/B=1-246.
DR PDBsum; 4DOI; -.
DR AlphaFoldDB; P41088; -.
DR SMR; P41088; -.
DR BioGRID; 9994; 3.
DR IntAct; P41088; 3.
DR STRING; 3702.AT3G55120.1; -.
DR iPTMnet; P41088; -.
DR PaxDb; P41088; -.
DR PRIDE; P41088; -.
DR ProteomicsDB; 224457; -.
DR EnsemblPlants; AT3G55120.1; AT3G55120.1; AT3G55120.
DR GeneID; 824678; -.
DR Gramene; AT3G55120.1; AT3G55120.1; AT3G55120.
DR KEGG; ath:AT3G55120; -.
DR Araport; AT3G55120; -.
DR TAIR; locus:2097228; AT3G55120.
DR eggNOG; ENOG502QR5P; Eukaryota.
DR HOGENOM; CLU_074682_0_0_1; -.
DR InParanoid; P41088; -.
DR OMA; WKGKTAQ; -.
DR OrthoDB; 1158490at2759; -.
DR PhylomeDB; P41088; -.
DR BioCyc; ARA:AT3G55120-MON; -.
DR UniPathway; UPA00154; -.
DR PRO; PR:P41088; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P41088; baseline and differential.
DR Genevisible; P41088; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0042406; C:extrinsic component of endoplasmic reticulum membrane; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR GO; GO:0045430; F:chalcone isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0009813; P:flavonoid biosynthetic process; IMP:TAIR.
DR GO; GO:0009733; P:response to auxin; IEP:TAIR.
DR GO; GO:0009411; P:response to UV; IMP:TAIR.
DR GO; GO:0010224; P:response to UV-B; IMP:TAIR.
DR Gene3D; 1.10.890.20; -; 1.
DR Gene3D; 3.50.70.10; -; 2.
DR InterPro; IPR044164; CFI.
DR InterPro; IPR016087; Chalcone_isomerase.
DR InterPro; IPR016088; Chalcone_isomerase_3-sand.
DR InterPro; IPR016089; Chalcone_isomerase_bundle_sf.
DR InterPro; IPR036298; Chalcone_isomerase_sf.
DR PANTHER; PTHR28039; PTHR28039; 1.
DR Pfam; PF02431; Chalcone; 1.
DR SUPFAM; SSF54626; SSF54626; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Flavonoid biosynthesis; Isomerase; Reference proteome.
FT CHAIN 1..246
FT /note="Chalcone--flavanone isomerase 1"
FT /id="PRO_0000166428"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 117
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT VARIANT 202
FT /note="I -> V (in strain: cv. Cha-0)"
FT VARIANT 238
FT /note="V -> L (in strain: cv. Gr-5, cv. Gran-2, cv. Gran-3,
FT cv. Gran-5, cv. Gran-7, cv. Gran-8, cv. Gran-10, cv. Ita-0,
FT cv. Ler, cv. Mh-0, cv. Per-1, cv. Rv-1, cv. Rv-3, cv. Rv-4,
FT cv. Rv-5, cv. Rv-8, cv. Wlp-1, cv. Wlp-2, cv. Wlp-3, cv.
FT Wlp-4, cv. Wlp-5, cv. Wlp-6, cv. Wlp-7, cv. Wlp-8, cv. Wlp-
FT 9 and cv. Wlp-10)"
FT VARIANT 246
FT /note="N -> NRE (in strain: cv. Rv-2, cv. Rv-9, cv. Rv-10,
FT cv. Tv-1, cv. Tv-2, cv. TV-6, cv. Tv-7, cv. Tv-8, cv. Tv-9
FT and cv. Tv-10)"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:4DOI"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:4DOI"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:4DOI"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:4DOI"
FT STRAND 38..51
FT /evidence="ECO:0007829|PDB:4DOI"
FT STRAND 54..65
FT /evidence="ECO:0007829|PDB:4DOI"
FT HELIX 69..77
FT /evidence="ECO:0007829|PDB:4DOI"
FT HELIX 82..87
FT /evidence="ECO:0007829|PDB:4DOI"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:4DOI"
FT STRAND 102..110
FT /evidence="ECO:0007829|PDB:4DOI"
FT HELIX 114..121
FT /evidence="ECO:0007829|PDB:4DOI"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:4DOI"
FT HELIX 125..131
FT /evidence="ECO:0007829|PDB:4DOI"
FT HELIX 137..150
FT /evidence="ECO:0007829|PDB:4DOI"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:4DOI"
FT STRAND 169..179
FT /evidence="ECO:0007829|PDB:4DOI"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:4DOI"
FT HELIX 192..203
FT /evidence="ECO:0007829|PDB:4DOI"
FT HELIX 210..224
FT /evidence="ECO:0007829|PDB:4DOI"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:4DOI"
SQ SEQUENCE 246 AA; 26596 MW; 2EB68BF68D576B98 CRC64;
MSSSNACASP SPFPAVTKLH VDSVTFVPSV KSPASSNPLF LGGAGVRGLD IQGKFVIFTV
IGVYLEGNAV PSLSVKWKGK TTEELTESIP FFREIVTGAF EKFIKVTMKL PLTGQQYSEK
VTENCVAIWK QLGLYTDCEA KAVEKFLEIF KEETFPPGSS ILFALSPTGS LTVAFSKDDS
IPETGIAVIE NKLLAEAVLE SIIGKNGVSP GTRLSVAERL SQLMMKNKDE KEVSDHSVEE
KLAKEN
