NSE1_HUMAN
ID NSE1_HUMAN Reviewed; 266 AA.
AC Q8WV22; D3DWF6; Q9P045; Q9P049;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 5.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Non-structural maintenance of chromosomes element 1 homolog;
DE Short=Non-SMC element 1 homolog;
DE EC=2.3.2.27 {ECO:0000269|PubMed:20864041, ECO:0000269|PubMed:29225034};
GN Name=NSMCE1 {ECO:0000312|HGNC:HGNC:29897}; ORFNames=HSPC333, HSPC337;
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 [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-266, AND VARIANT SER-47.
RC TISSUE=Pancreas;
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 INTERACTION WITH SMC6.
RX PubMed=14701739; DOI=10.1128/mcb.24.2.662-674.2004;
RA Harvey S.H., Sheedy D.M., Cuddihy A.R., O'Connell M.J.;
RT "Coordination of DNA damage responses via the Smc5/Smc6 complex.";
RL Mol. Cell. Biol. 24:662-674(2004).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION, INTERACTION WITH SMC6;
RP NSMCE2; NSMCE4A AND NSMCE3, AND IDENTIFICATION IN THE SMC5-SMC6 COMPLEX.
RX PubMed=18086888; DOI=10.1128/mcb.00767-07;
RA Taylor E.M., Copsey A.C., Hudson J.J., Vidot S., Lehmann A.R.;
RT "Identification of the proteins, including MAGEG1, that make up the human
RT SMC5-6 protein complex.";
RL Mol. Cell. Biol. 28:1197-1206(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP INTERACTION WITH NSMCE3.
RX PubMed=21364888; DOI=10.1371/journal.pone.0017270;
RA Hudson J.J., Bednarova K., Kozakova L., Liao C., Guerineau M., Colnaghi R.,
RA Vidot S., Marek J., Bathula S.R., Lehmann A.R., Palecek J.;
RT "Interactions between the Nse3 and Nse4 components of the SMC5-6 complex
RT identify evolutionarily conserved interactions between MAGE and EID
RT Families.";
RL PLoS ONE 6:E17270-E17270(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [10]
RP INTERACTION WITH NSMCE3.
RX PubMed=27427983; DOI=10.1172/jci82890;
RA van der Crabben S.N., Hennus M.P., McGregor G.A., Ritter D.I.,
RA Nagamani S.C., Wells O.S., Harakalova M., Chinn I.K., Alt A., Vondrova L.,
RA Hochstenbach R., van Montfrans J.M., Terheggen-Lagro S.W., van Lieshout S.,
RA van Roosmalen M.J., Renkens I., Duran K., Nijman I.J., Kloosterman W.P.,
RA Hennekam E., Orange J.S., van Hasselt P.M., Wheeler D.A., Palecek J.J.,
RA Lehmann A.R., Oliver A.W., Pearl L.H., Plon S.E., Murray J.M.,
RA van Haaften G.;
RT "Destabilized SMC5/6 complex leads to chromosome breakage syndrome with
RT severe lung disease.";
RL J. Clin. Invest. 126:2881-2892(2016).
RN [11]
RP FUNCTION, INTERACTION WITH MAGEF1, AND CATALYTIC ACTIVITY.
RX PubMed=29225034; DOI=10.1016/j.molcel.2017.11.010;
RA Weon J.L., Yang S.W., Potts P.R.;
RT "Cytosolic Iron-Sulfur Assembly Is Evolutionarily Tuned by a Cancer-
RT Amplified Ubiquitin Ligase.";
RL Mol. Cell 69:113-125(2018).
RN [12]
RP STRUCTURE BY NMR OF 181-241, AND ZINC-BINDING.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RING domain of the non-SMC element 1 protein.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.92 ANGSTROMS) OF 9-246 IN COMPLEX WITH NSMCE3,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20864041; DOI=10.1016/j.molcel.2010.08.029;
RA Doyle J.M., Gao J., Wang J., Yang M., Potts P.R.;
RT "MAGE-RING protein complexes comprise a family of E3 ubiquitin ligases.";
RL Mol. Cell 39:963-974(2010).
CC -!- FUNCTION: RING-type zinc finger-containing E3 ubiquitin ligase that
CC assembles with melanoma antigen protein (MAGE) to catalyze the direct
CC transfer of ubiquitin from E2 ubiquitin-conjugating enzyme to a
CC specific substrate. Within MAGE-RING ubiquitin ligase complex, MAGE
CC stimulates and specifies ubiquitin ligase activity likely through
CC recruitment and/or stabilization of the E2 ubiquitin-conjugating enzyme
CC at the E3:substrate complex. Involved in maintenance of genome
CC integrity, DNA damage response and DNA repair (PubMed:29225034,
CC PubMed:20864041). NSMCE3/MAGEG1 and NSMCE1 ubiquitin ligase are
CC components of SMC5-SMC6 complex and may positively regulate homologous
CC recombination-mediated DNA repair (PubMed:18086888). MAGEF1-NSMCE1
CC ubiquitin ligase promotes proteasomal degradation of MMS19, a key
CC component of the cytosolic iron-sulfur protein assembly (CIA)
CC machinery. Down-regulation of MMS19 impairs the activity of several DNA
CC repair and metabolism enzymes such as ERCC2/XPD, FANCJ, RTEL1 and POLD1
CC that require iron-sulfur clusters as cofactors (PubMed:29225034).
CC {ECO:0000269|PubMed:18086888, ECO:0000269|PubMed:20864041,
CC ECO:0000269|PubMed:29225034}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:20864041,
CC ECO:0000269|PubMed:29225034};
CC -!- SUBUNIT: Component of the SMC5-SMC6 complex which consists at least of
CC SMC5, SMC6, NSMCE2, NSMCE1, NSMCE4A or EID3 and NSMCE3. NSMCE1, NSMCE4A
CC or EID3 and NSMCE3 probably form a subcomplex that bridges the head
CC domains of the SMC5-SMC6 heterodimer (PubMed:18086888,
CC PubMed:20864041). Interacts with NSMCE3 (PubMed:27427983). Interacts
CC with MAGEF1 (PubMed:29225034). {ECO:0000269|PubMed:18086888,
CC ECO:0000269|PubMed:20864041, ECO:0000269|PubMed:27427983,
CC ECO:0000269|PubMed:29225034}.
CC -!- INTERACTION:
CC Q8WV22; Q96MG7: NSMCE3; NbExp=20; IntAct=EBI-2557372, EBI-2557356;
CC Q8WV22; Q96SB8: SMC6; NbExp=9; IntAct=EBI-2557372, EBI-605415;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18086888}.
CC Chromosome, telomere {ECO:0000305|PubMed:18086888}.
CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:18086888}.
CC -!- SIMILARITY: Belongs to the NSE1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF29011.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF29015.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF161451; AAF29011.1; ALT_SEQ; mRNA.
DR EMBL; AF161455; AAF29015.1; ALT_SEQ; mRNA.
DR EMBL; AC106739; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471145; EAW55756.1; -; Genomic_DNA.
DR EMBL; CH471145; EAW55757.1; -; Genomic_DNA.
DR EMBL; BC018938; AAH18938.4; -; mRNA.
DR CCDS; CCDS10628.2; -.
DR RefSeq; NP_659547.2; NM_145080.3.
DR RefSeq; XP_006721086.1; XM_006721023.3.
DR PDB; 2CT0; NMR; -; A=181-241.
DR PDB; 5HVQ; X-ray; 2.92 A; C=9-246.
DR PDB; 5WY5; X-ray; 2.92 A; A=9-246.
DR PDBsum; 2CT0; -.
DR PDBsum; 5HVQ; -.
DR PDBsum; 5WY5; -.
DR AlphaFoldDB; Q8WV22; -.
DR BMRB; Q8WV22; -.
DR SMR; Q8WV22; -.
DR BioGRID; 128255; 42.
DR ComplexPortal; CPX-5992; SMC5-SMC6 SUMO ligase complex, EID3 variant.
DR ComplexPortal; CPX-6086; SMC5-SMC6 SUMO ligase complex, NSE4EA variant.
DR IntAct; Q8WV22; 20.
DR STRING; 9606.ENSP00000355077; -.
DR iPTMnet; Q8WV22; -.
DR PhosphoSitePlus; Q8WV22; -.
DR BioMuta; NSMCE1; -.
DR DMDM; 209572785; -.
DR EPD; Q8WV22; -.
DR jPOST; Q8WV22; -.
DR MassIVE; Q8WV22; -.
DR MaxQB; Q8WV22; -.
DR PaxDb; Q8WV22; -.
DR PeptideAtlas; Q8WV22; -.
DR PRIDE; Q8WV22; -.
DR ProteomicsDB; 74738; -.
DR Antibodypedia; 26234; 117 antibodies from 19 providers.
DR DNASU; 197370; -.
DR Ensembl; ENST00000361439.9; ENSP00000355077.4; ENSG00000169189.17.
DR GeneID; 197370; -.
DR KEGG; hsa:197370; -.
DR MANE-Select; ENST00000361439.9; ENSP00000355077.4; NM_145080.4; NP_659547.2.
DR UCSC; uc002doi.2; human.
DR CTD; 197370; -.
DR DisGeNET; 197370; -.
DR GeneCards; NSMCE1; -.
DR HGNC; HGNC:29897; NSMCE1.
DR HPA; ENSG00000169189; Low tissue specificity.
DR MIM; 617263; gene.
DR neXtProt; NX_Q8WV22; -.
DR OpenTargets; ENSG00000169189; -.
DR PharmGKB; PA134943761; -.
DR VEuPathDB; HostDB:ENSG00000169189; -.
DR eggNOG; KOG4718; Eukaryota.
DR GeneTree; ENSGT00390000009084; -.
DR HOGENOM; CLU_045153_3_1_1; -.
DR InParanoid; Q8WV22; -.
DR OMA; GRLHDHC; -.
DR OrthoDB; 1159451at2759; -.
DR PhylomeDB; Q8WV22; -.
DR TreeFam; TF314721; -.
DR PathwayCommons; Q8WV22; -.
DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR SignaLink; Q8WV22; -.
DR SIGNOR; Q8WV22; -.
DR BioGRID-ORCS; 197370; 505 hits in 1135 CRISPR screens.
DR ChiTaRS; NSMCE1; human.
DR EvolutionaryTrace; Q8WV22; -.
DR GenomeRNAi; 197370; -.
DR Pharos; Q8WV22; Tdark.
DR PRO; PR:Q8WV22; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q8WV22; protein.
DR Bgee; ENSG00000169189; Expressed in right testis and 182 other tissues.
DR ExpressionAtlas; Q8WV22; baseline and differential.
DR Genevisible; Q8WV22; HS.
DR GO; GO:0000781; C:chromosome, telomeric region; IC:ComplexPortal.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030915; C:Smc5-Smc6 complex; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IDA:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0006301; P:postreplication repair; IBA:GO_Central.
DR GO; GO:0016925; P:protein sumoylation; IC:ComplexPortal.
DR GO; GO:0032204; P:regulation of telomere maintenance; IC:ComplexPortal.
DR CDD; cd16493; RING-CH-C4HC3_NSE1; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011513; Nse1.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR014857; Znf_RING-like.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR20973; PTHR20973; 1.
DR Pfam; PF07574; SMC_Nse1; 1.
DR Pfam; PF08746; zf-RING-like; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; DNA damage; DNA recombination; DNA repair;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Telomere;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..266
FT /note="Non-structural maintenance of chromosomes element 1
FT homolog"
FT /id="PRO_0000270944"
FT ZN_FING 191..232
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..102
FT /note="Interaction with NSMCE3"
FT /evidence="ECO:0000269|PubMed:20864041"
FT REGION 246..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 38
FT /note="T -> R (in dbSNP:rs7195194)"
FT /id="VAR_029822"
FT VARIANT 47
FT /note="N -> S (in dbSNP:rs17856580)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_029823"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:5WY5"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:5WY5"
FT HELIX 30..43
FT /evidence="ECO:0007829|PDB:5WY5"
FT HELIX 53..64
FT /evidence="ECO:0007829|PDB:5WY5"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:5WY5"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:5WY5"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:5WY5"
FT STRAND 82..91
FT /evidence="ECO:0007829|PDB:5WY5"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:5WY5"
FT HELIX 103..118
FT /evidence="ECO:0007829|PDB:5WY5"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:5WY5"
FT HELIX 126..130
FT /evidence="ECO:0007829|PDB:5WY5"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:5WY5"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:5WY5"
FT HELIX 143..155
FT /evidence="ECO:0007829|PDB:5WY5"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:5WY5"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:5WY5"
FT HELIX 170..183
FT /evidence="ECO:0007829|PDB:5WY5"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:5WY5"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:5HVQ"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:5WY5"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:5HVQ"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:5WY5"
FT HELIX 213..219
FT /evidence="ECO:0007829|PDB:5WY5"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:5WY5"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:5WY5"
SQ SEQUENCE 266 AA; 30855 MW; 58A3C2AF70FC8F39 CRC64;
MQGSTRRMGV MTDVHRRFLQ LLMTHGVLEE WDVKRLQTHC YKVHDRNATV DKLEDFINNI
NSVLESLYIE IKRGVTEDDG RPIYALVNLA TTSISKMATD FAENELDLFR KALELIIDSE
TGFASSTNIL NLVDQLKGKK MRKKEAEQVL QKFVQNKWLI EKEGEFTLHG RAILEMEQYI
RETYPDAVKI CNICHSLLIQ GQSCETCGIR MHLPCVAKYF QSNAEPRCPH CNDYWPHEIP
KVFDPEKERE SGVLKSNKKS LRSRQH
