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Superoxide dismutase [Cu-Zn] 2, chloroplastic (EC 1.15.1.1) (Copper/zinc superoxide dismutase 2)

 SODC2_ARATH             Reviewed;         216 AA.
O78310; Q0WUQ0; Q541D5; Q9SUJ7; Q9SUJ8;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
20-JUN-2002, sequence version 2.
16-JAN-2019, entry version 151.
RecName: Full=Superoxide dismutase [Cu-Zn] 2, chloroplastic;
EC=1.15.1.1;
AltName: Full=Copper/zinc superoxide dismutase 2;
Flags: Precursor;
Name=CSD2; Synonyms=KD-SOD, SODCP; OrderedLocusNames=At2g28190;
ORFNames=F24D13.2;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
INDUCTION BY LIGHT; UV-B AND OZONE, AND GENE FAMILY.
STRAIN=cv. Columbia;
PubMed=9765550; DOI=10.1104/pp.118.2.637;
Kliebenstein D.J., Monde R.A., Last R.L.;
"Superoxide dismutase in Arabidopsis: an eclectic enzyme family with
disparate regulation and protein localization.";
Plant Physiol. 118:637-650(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND VARIANTS TYR-23;
SER-39; ALA-101 AND LYS-164.
STRAIN=cv. Cvi-1, and cv. Landsberg erecta;
PubMed=11457901; DOI=10.1093/jexbot/52.360.1417;
Abarca D., Roldan M., Martin M., Sabater B.;
"Arabidopsis thaliana ecotype Cvi shows an increased tolerance to
photo-oxidative stress and contains a new chloroplastic copper/zinc
superoxide dismutase isoenzyme.";
J. Exp. Bot. 52:1417-1425(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12885779; DOI=10.1074/jbc.M304987200;
Rizhsky L., Liang H., Mittler R.;
"The water-water cycle is essential for chloroplast protection in the
absence of stress.";
J. Biol. Chem. 278:38921-38925(2003).
[9]
FUNCTION, INDUCTION BY OXIDATIVE STRESS, AND TISSUE SPECIFICITY.
PubMed=16861386; DOI=10.1105/tpc.106.041673;
Sunkar R., Kapoor A., Zhu J.-K.;
"Posttranscriptional induction of two Cu/Zn superoxide dismutase genes
in Arabidopsis is mediated by downregulation of miR398 and important
for oxidative stress tolerance.";
Plant Cell 18:2051-2065(2006).
[10]
REGULATION BY ACONITASE.
PubMed=17013749; DOI=10.1007/s11103-006-9087-x;
Moeder W., Del Pozo O., Navarre D.A., Martin G.B., Klessig D.F.;
"Aconitase plays a role in regulating resistance to oxidative stress
and cell death in Arabidopsis and Nicotiana benthamiana.";
Plant Mol. Biol. 63:273-287(2007).
[11]
INDUCTION BY SALT.
STRAIN=cv. Columbia;
PubMed=18275461; DOI=10.1111/j.1399-3054.2007.01009.x;
Attia H., Arnaud N., Karray N., Lachaal M.;
"Long-term effects of mild salt stress on growth, ion accumulation and
superoxide dismutase expression of Arabidopsis rosette leaves.";
Physiol. Plantarum 132:293-305(2008).
[12]
INDUCTION BY SUCROSE.
STRAIN=cv. Columbia;
PubMed=18392778; DOI=10.1007/s11103-008-9329-1;
Dugas D.V., Bartel B.;
"Sucrose induction of Arabidopsis miR398 represses two Cu/Zn
superoxide dismutases.";
Plant Mol. Biol. 67:403-417(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
SCALE ANALYSIS].
PubMed=18431481; DOI=10.1371/journal.pone.0001994;
Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O.,
Sun Q., van Wijk K.J.;
"Sorting signals, N-terminal modifications and abundance of the
chloroplast proteome.";
PLoS ONE 3:E1994-E1994(2008).
-!- FUNCTION: Destroys radicals which are normally produced within the
cells and which are toxic to biological systems. Mediates
tolerance to stress, including photo-oxidative stress.
{ECO:0000269|PubMed:11457901, ECO:0000269|PubMed:12885779,
ECO:0000269|PubMed:16861386}.
-!- CATALYTIC ACTIVITY:
Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
ChEBI:CHEBI:18421; EC=1.15.1.1;
-!- COFACTOR:
Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
Note=Binds 1 copper ion per subunit. {ECO:0000250};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBUNIT: Homotetramer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast
{ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:9765550}.
-!- TISSUE SPECIFICITY: Expressed in leaves (at protein level). The
spatial localization is regulated by miR398-mediated silencing.
Mostly present in flowers, old rosette leaves and inflorescence,
and, to a lower extent, in cauline leaves, stems and roots.
{ECO:0000269|PubMed:16861386, ECO:0000269|PubMed:9765550}.
-!- INDUCTION: Upon photosynthetically active radiation (PAR) (e.g.
light fluence) increase and UV-B treatment. Accumulates in
response to ozone fumigation, during recovery. Induced in response
to oxidative stress, via a reduction of miR398-mediated silencing.
Repressed by sucrose in a miR398-mediated silencing-dependent
manner. Repressed by salt stress. Down-regulated by aconitase.
{ECO:0000269|PubMed:16861386, ECO:0000269|PubMed:18275461,
ECO:0000269|PubMed:18392778, ECO:0000269|PubMed:9765550}.
-!- DISRUPTION PHENOTYPE: Growth retardation (e.g. delayed flowering)
and abnormal chloroplasts (e.g. less organized with fewer stacks).
This phenotype is reversed under very low light conditions.
Enhanced tolerance to oxidative stress.
{ECO:0000269|PubMed:12885779}.
-!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
{ECO:0000305}.
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EMBL; AF061519; AAD10208.1; -; mRNA.
EMBL; AJ238521; CAB51839.1; -; Genomic_DNA.
EMBL; AJ238522; CAB51840.1; -; Genomic_DNA.
EMBL; AC005851; AAM15088.1; -; Genomic_DNA.
EMBL; CP002685; AEC08089.1; -; Genomic_DNA.
EMBL; AY064050; AAL36406.1; -; mRNA.
EMBL; AY133756; AAM91690.1; -; mRNA.
EMBL; AK227096; BAE99148.1; -; mRNA.
EMBL; AY087944; AAM65492.1; -; mRNA.
PIR; T51730; T51730.
RefSeq; NP_565666.1; NM_128379.4.
UniGene; At.20409; -.
ProteinModelPortal; O78310; -.
SMR; O78310; -.
BioGrid; 2715; 2.
IntAct; O78310; 1.
STRING; 3702.AT2G28190.1; -.
iPTMnet; O78310; -.
PaxDb; O78310; -.
PRIDE; O78310; -.
EnsemblPlants; AT2G28190.1; AT2G28190.1; AT2G28190.
GeneID; 817365; -.
Gramene; AT2G28190.1; AT2G28190.1; AT2G28190.
KEGG; ath:AT2G28190; -.
Araport; AT2G28190; -.
TAIR; locus:2046168; AT2G28190.
eggNOG; KOG0441; Eukaryota.
eggNOG; COG2032; LUCA.
HOGENOM; HOG000263447; -.
InParanoid; O78310; -.
KO; K04565; -.
OMA; MAKAVCT; -.
OrthoDB; 1574423at2759; -.
PhylomeDB; O78310; -.
Reactome; R-ATH-114608; Platelet degranulation.
Reactome; R-ATH-3299685; Detoxification of Reactive Oxygen Species.
PRO; PR:O78310; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; O78310; baseline and differential.
Genevisible; O78310; AT.
GO; GO:0048046; C:apoplast; IDA:TAIR.
GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0009579; C:thylakoid; IDA:TAIR.
GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
GO; GO:0016532; F:superoxide dismutase copper chaperone activity; IBA:GO_Central.
GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
GO; GO:0071484; P:cellular response to light intensity; IEP:UniProtKB.
GO; GO:0034599; P:cellular response to oxidative stress; IEP:UniProtKB.
GO; GO:0071457; P:cellular response to ozone; IEP:UniProtKB.
GO; GO:0071472; P:cellular response to salt stress; IEP:UniProtKB.
GO; GO:0071329; P:cellular response to sucrose stimulus; IEP:UniProtKB.
GO; GO:0071493; P:cellular response to UV-B; IEP:UniProtKB.
GO; GO:0035195; P:gene silencing by miRNA; IEP:UniProtKB.
GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
GO; GO:0046688; P:response to copper ion; IEP:TAIR.
GO; GO:0010039; P:response to iron ion; IEP:TAIR.
GO; GO:0006979; P:response to oxidative stress; IDA:TAIR.
CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
Gene3D; 2.60.40.200; -; 1.
InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
InterPro; IPR018152; SOD_Cu/Zn_BS.
InterPro; IPR001424; SOD_Cu_Zn_dom.
PANTHER; PTHR10003; PTHR10003; 1.
Pfam; PF00080; Sod_Cu; 1.
PRINTS; PR00068; CUZNDISMTASE.
SUPFAM; SSF49329; SSF49329; 1.
PROSITE; PS00087; SOD_CU_ZN_1; 1.
PROSITE; PS00332; SOD_CU_ZN_2; 1.
1: Evidence at protein level;
Antioxidant; Chloroplast; Complete proteome; Copper; Disulfide bond;
Metal-binding; Oxidoreductase; Plastid; Reference proteome;
Transit peptide; Zinc.
TRANSIT 1 62 Chloroplast.
CHAIN 63 216 Superoxide dismutase [Cu-Zn] 2,
chloroplastic.
/FTId=PRO_0000032844.
METAL 108 108 Copper; catalytic. {ECO:0000250}.
METAL 110 110 Copper; catalytic. {ECO:0000250}.
METAL 125 125 Copper; catalytic. {ECO:0000250}.
METAL 125 125 Zinc; structural. {ECO:0000250}.
METAL 133 133 Zinc; structural. {ECO:0000250}.
METAL 142 142 Zinc; structural. {ECO:0000250}.
METAL 145 145 Zinc; structural. {ECO:0000250}.
METAL 182 182 Copper; catalytic. {ECO:0000250}.
DISULFID 119 208 {ECO:0000250}.
VARIANT 23 23 N -> Y (in strain: cv. Cvi-1; enhanced
stability and better tolerance to photo-
oxidative stress conditions; when
associated with S-39, A-101 and K-164).
{ECO:0000269|PubMed:11457901}.
VARIANT 39 39 N -> S (in strain: cv. Cvi-1; enhanced
stability and better tolerance to photo-
oxidative stress conditions; when
associated with Y-23, A-101 and K-164).
{ECO:0000269|PubMed:11457901}.
VARIANT 101 101 T -> A (in strain: cv. Cvi-1; enhanced
stability and better tolerance to photo-
oxidative stress conditions; when
associated with Y-23, S-39 and K-164).
{ECO:0000269|PubMed:11457901}.
VARIANT 164 164 N -> K (in strain: cv. Cvi-1; enhanced
stability and better tolerance to photo-
oxidative stress conditions; when
associated with Y-23, S-39 and A-101).
{ECO:0000269|PubMed:11457901}.
CONFLICT 32 32 R -> S (in Ref. 1; AAD10208 and 7;
AAM65492). {ECO:0000305}.
SEQUENCE 216 AA; 22244 MW; 5F0E4333E1C1581C CRC64;
MAATNTILAF SSPSRLLIPP SSNPSTLRSS FRGVSLNNNN LHRLQSVSFA VKAPSKALTV
VSAAKKAVAV LKGTSDVEGV VTLTQDDSGP TTVNVRITGL TPGPHGFHLH EFGDTTNGCI
STGPHFNPNN MTHGAPEDEC RHAGDLGNIN ANADGVAETT IVDNQIPLTG PNSVVGRAFV
VHELKDDLGK GGHELSLTTG NAGGRLACGV IGLTPL


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Pathways :
WP100: Glutathione metabolism
WP1039: Glutathione metabolism
WP104: Alanine and aspartate metabolism
WP106: Alanine and aspartate metabolism
WP1126: Tryptophan metabolism
WP1313: Insulin Signaling
WP1321: Myometrial Relaxation and Contraction Pathways
WP1323: EGFR1 Signaling Pathway
WP1329: Alpha6-Beta4 Integrin Signaling Pathway
WP1333: Hypothetical Network for Drug Addiction
WP1344: Wnt Signaling Pathway and Pluripotency
WP1345: T Cell Receptor Signaling Pathway
WP1348: Androgen Receptor Signaling Pathway
WP1354: B Cell Receptor Signaling Pathway
WP1355: One Carbon Metabolism
WP1362: Homologous recombination
WP1363: p38 MAPK Signaling Pathway
WP1365: Calcium Regulation in the Cardiac Cell
WP1370: TGF Beta Signaling Pathway
WP1371: G Protein Signaling Pathways
WP1373: GPCRs, Class C Metabotropic glutamate, pheromone
WP1378: Senescence and Autophagy
WP1379: Diurnally regulated genes with circadian orthologs
WP1380: Regulation of Actin Cytoskeleton
WP1382: Delta-Notch Signaling Pathway

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[FSD2 APG8 At5g51100 MWD22.4] Superoxide dismutase [Fe] 2, chloroplastic (EC 1.15.1.1) (Protein ALBINO OR PALE GREEN 8) (Protein FE SUPEROXIDE DISMUTASE 2)
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[sod1-a] Superoxide dismutase [Cu-Zn] A (XSODA) (EC 1.15.1.1)
[Sod2 Sod-2] Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1)
[SOD2] Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1)
[Sod2] Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1)
[sodB sod sodA Rv3846 MTCY01A6.22c] Superoxide dismutase [Fe] (EC 1.15.1.1)
[sodF1 sodB sodF SCO2633 SC8E4A.03] Superoxide dismutase [Fe-Zn] 1 (EC 1.15.1.1) (FeSOD I) (SOD2)
[sodA sod] Superoxide dismutase [Mn/Fe] (EC 1.15.1.1)
[NECI] Nectarin-1 (EC 1.15.1.1) (Superoxide dismutase [Mn])
[sod1 sod VNG_1190G] Superoxide dismutase [Mn] 1 (EC 1.15.1.1)
[ATP7A MC1 MNK] Copper-transporting ATPase 1 (EC 7.2.2.8) (Copper pump 1) (Menkes disease-associated protein)
[SOD2] Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1) (Mn-SOD)
[Atp7a Mnk] Copper-transporting ATPase 1 (EC 7.2.2.8) (Copper pump 1) (Menkes disease-associated protein homolog)
[SOD2] Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1)
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[fdm] Formaldehyde dismutase (EC 1.2.98.1)
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]

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