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Endosomal/prevacuolar sodium/hydrogen exchanger (Endosomal/prevacuolar Na( )/H( ) exchanger) (Vacuolar protein sorting-associated protein 44)

 NHX1_YEAST              Reviewed;         633 AA.
Q04121; D6VT80;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
18-JUL-2018, entry version 165.
RecName: Full=Endosomal/prevacuolar sodium/hydrogen exchanger;
AltName: Full=Endosomal/prevacuolar Na(+)/H(+) exchanger;
AltName: Full=Vacuolar protein sorting-associated protein 44;
Flags: Precursor;
Name=NHX1; Synonyms=NHA2, VPL27, VPS44; OrderedLocusNames=YDR456W;
ORFNames=D9461.40;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9507001; DOI=10.1074/jbc.273.12.6951;
Numata M., Petrecca K., Lake N., Orlowski J.;
"Identification of a mitochondrial Na+/H+ exchanger.";
J. Biol. Chem. 273:6951-6959(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
FUNCTION.
PubMed=1493335; DOI=10.1091/mbc.3.12.1389;
Raymond C.K., Howald-Stevenson I., Vater C.A., Stevens T.H.;
"Morphological classification of the yeast vacuolar protein sorting
mutants: evidence for a prevacuolar compartment in class E vps
mutants.";
Mol. Biol. Cell 3:1389-1402(1992).
[5]
FUNCTION.
PubMed=9334180; DOI=10.1074/jbc.272.42.26145;
Nass R., Cunningham K.W., Rao R.;
"Intracellular sequestration of sodium by a novel Na+/H+ exchanger in
yeast is enhanced by mutations in the plasma membrane H+-ATPase.
Insights into mechanisms of sodium tolerance.";
J. Biol. Chem. 272:26145-26152(1997).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=9694857; DOI=10.1074/jbc.273.33.21054;
Nass R., Rao R.;
"Novel localization of a Na+/H+ exchanger in a late endosomal
compartment of yeast. Implications for vacuole biogenesis.";
J. Biol. Chem. 273:21054-21060(1998).
[7]
FUNCTION.
PubMed=10589731;
Nass R., Rao R.;
"The yeast endosomal Na+/H+ exchanger, Nhx1, confers osmotolerance
following acute hypertonic shock.";
Microbiology 145:3221-3228(1999).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=10998367; DOI=10.1042/0264-6021:3510241;
Darley C.P., van Wuytswinkel O.C.M., van der Woude K., Mager W.H.,
de Boer A.H.;
"Arabidopsis thaliana and Saccharomyces cerevisiae NHX1 genes encode
amiloride sensitive electroneutral Na(+)/H(+) exchangers.";
Biochem. J. 351:241-249(2000).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-201; GLU-225
AND ASP-230.
PubMed=11102523; DOI=10.1091/mbc.11.12.4277;
Bowers K., Levi B.P., Patel F.I., Stevens T.H.;
"The sodium/proton exchanger Nhx1p is required for endosomal protein
trafficking in the yeast Saccharomyces cerevisiae.";
Mol. Biol. Cell 11:4277-4294(2000).
[10]
GLYCOSYLATION, AND TOPOLOGY.
PubMed=11036065; DOI=10.1074/jbc.M001688200;
Wells K.M., Rao R.;
"The yeast Na+/H+ exchanger Nhx1 is an N-linked glycoprotein.
Topological implications.";
J. Biol. Chem. 276:3401-3407(2001).
[11]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CYP6.
PubMed=14610088; DOI=10.1074/jbc.M307446200;
Ali R., Brett C.L., Mukherjee S., Rao R.;
"Inhibition of sodium/proton exchange by a Rab-GTPase-activating
protein regulates endosomal traffic in yeast.";
J. Biol. Chem. 279:4498-4506(2004).
[13]
FUNCTION.
PubMed=15635088; DOI=10.1091/mbc.E04-11-0999;
Brett C.L., Tukaye D.N., Mukherjee S., Rao R.;
"The yeast endosomal Na+K+/H+ exchanger Nhx1 regulates cellular pH to
control vesicle trafficking.";
Mol. Biol. Cell 16:1396-1405(2005).
[14]
FUNCTION.
PubMed=15659172; DOI=10.1111/j.1365-2958.2004.04410.x;
Maresova L., Sychrova H.;
"Physiological characterization of Saccharomyces cerevisiae kha1
deletion mutants.";
Mol. Microbiol. 55:588-600(2005).
[15]
FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF GLU-355;
PHE-357; TYR-361; GLU-365; GLU-369 AND PRO-376.
PubMed=16671892; DOI=10.1042/BJ20060388;
Mukherjee S., Kallay L., Brett C.L., Rao R.;
"Mutational analysis of the intramembranous H10 loop of yeast Nhx1
reveals a critical role in ion homoeostasis and vesicle trafficking.";
Biochem. J. 398:97-105(2006).
[16]
SUBCELLULAR LOCATION.
PubMed=17543551; DOI=10.1016/j.cellbi.2007.04.008;
Hedman J.M., Eggleston M.D., Attryde A.L., Marshall P.A.;
"Prevacuolar compartment morphology in vps mutants of Saccharomyces
cerevisiae.";
Cell Biol. Int. 31:1237-1244(2007).
[17]
FUNCTION.
PubMed=17588950; DOI=10.1074/jbc.M703116200;
Cagnac O., Leterrier M., Yeager M., Blumwald E.;
"Identification and characterization of Vnx1p, a novel type of
vacuolar monovalent cation/H+ antiporter of Saccharomyces
cerevisiae.";
J. Biol. Chem. 282:24284-24293(2007).
[18]
FUNCTION.
PubMed=18378800; DOI=10.1085/jgp.200709905;
Jennings M.L., Cui J.;
"Chloride homeostasis in Saccharomyces cerevisiae: high affinity
influx, V-ATPase-dependent sequestration, and identification of a
candidate Cl-sensor.";
J. Gen. Physiol. 131:379-391(2008).
[19]
FUNCTION.
PubMed=18799619; DOI=10.1091/mbc.E08-05-0486;
Chen S., Tarsio M., Kane P.M., Greenberg M.L.;
"Cardiolipin mediates cross-talk between mitochondria and the
vacuole.";
Mol. Biol. Cell 19:5047-5058(2008).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-490; SER-494; THR-498;
SER-499 AND SER-569, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: Endosomal/prevacuolar electroneutral Na(+)/H(+)
exchanger which mediates intracellular sequestration of Na(+)
cations, regulates vacuolar pH and contributes to osmotolerance
following sudden exposure to hyperosmotic media. Contributes also
to the postdiauxic/stationary phase resistance to osmotic stress
and allows for the continued growth of cells until the acquired
osmotolerance response can occur. Involved in hygromycin
resistance probably through its influence on the electrochemical
proton gradient affecting secondarily the entrance of hygromycin.
Mediates pH-dependent vesicle trafficking out of the endosome.
Contributes to K(+) sequestration and homeostasis.
{ECO:0000269|PubMed:10589731, ECO:0000269|PubMed:10998367,
ECO:0000269|PubMed:11102523, ECO:0000269|PubMed:14610088,
ECO:0000269|PubMed:1493335, ECO:0000269|PubMed:15635088,
ECO:0000269|PubMed:15659172, ECO:0000269|PubMed:16671892,
ECO:0000269|PubMed:17588950, ECO:0000269|PubMed:18378800,
ECO:0000269|PubMed:18799619, ECO:0000269|PubMed:9334180,
ECO:0000269|PubMed:9694857}.
-!- SUBUNIT: Interacts with CYP6. {ECO:0000269|PubMed:14610088}.
-!- SUBCELLULAR LOCATION: Endosome membrane; Multi-pass membrane
protein. Prevacuolar compartment membrane; Multi-pass membrane
protein.
-!- MISCELLANEOUS: Present with 521 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1
(CPA1) transporter (TC 2.A.36) family. {ECO:0000305}.
-!- CAUTION: Numerous studies suggest that the C-terminal tail of the
Na(+)/H(+) exchangers assumes a cytosolic orientation and
constitutes a regulatory region. This cytosolic localization is
confirmed by phosphorylation analysis (PubMed:15665377 and
PubMed:18407956). However, residues Asn-515, Asn-550 and Asn-563
have been shown to be glycosylated and localized at the lumenal
side (PubMed:11036065). These contradictory results suggest an
unusual topology of the C-terminal tail which may contain membrane
spans formed by beta-sheets or even may switch from one side to
the other of the membrane. {ECO:0000305|PubMed:11036065}.
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EMBL; U33007; AAB64861.1; -; Genomic_DNA.
EMBL; BK006938; DAA12290.1; -; Genomic_DNA.
PIR; S69734; S69734.
RefSeq; NP_010744.3; NM_001180764.3.
ProteinModelPortal; Q04121; -.
SMR; Q04121; -.
BioGrid; 32510; 284.
DIP; DIP-4145N; -.
IntAct; Q04121; 18.
MINT; Q04121; -.
STRING; 4932.YDR456W; -.
TCDB; 2.A.36.1.12; the monovalent cation:proton antiporter-1 (cpa1) family.
iPTMnet; Q04121; -.
MaxQB; Q04121; -.
PaxDb; Q04121; -.
PRIDE; Q04121; -.
TopDownProteomics; Q04121; -.
EnsemblFungi; YDR456W; YDR456W; YDR456W.
GeneID; 852066; -.
KEGG; sce:YDR456W; -.
EuPathDB; FungiDB:YDR456W; -.
SGD; S000002864; NHX1.
GeneTree; ENSGT00760000119074; -.
HOGENOM; HOG000172307; -.
InParanoid; Q04121; -.
KO; K12041; -.
OMA; IVMFETC; -.
OrthoDB; EOG092C1Y19; -.
BioCyc; YEAST:G3O-29984-MONOMER; -.
Reactome; R-SCE-425986; Sodium/Proton exchangers.
PRO; PR:Q04121; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0005769; C:early endosome; IDA:SGD.
GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005770; C:late endosome; IDA:SGD.
GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005802; C:trans-Golgi network; IDA:SGD.
GO; GO:0015386; F:potassium:proton antiporter activity; IMP:SGD.
GO; GO:0015385; F:sodium:proton antiporter activity; IMP:SGD.
GO; GO:0030004; P:cellular monovalent inorganic cation homeostasis; IMP:SGD.
GO; GO:0071805; P:potassium ion transmembrane transport; IMP:SGD.
GO; GO:0035725; P:sodium ion transmembrane transport; IMP:SGD.
GO; GO:0007035; P:vacuolar acidification; IMP:SGD.
InterPro; IPR006153; Cation/H_exchanger.
InterPro; IPR018422; Cation/H_exchanger_CPA1.
InterPro; IPR004709; NaH_exchanger.
PANTHER; PTHR10110; PTHR10110; 1.
Pfam; PF00999; Na_H_Exchanger; 1.
PRINTS; PR01084; NAHEXCHNGR.
TIGRFAMs; TIGR00840; b_cpa1; 1.
1: Evidence at protein level;
Antiport; Complete proteome; Endosome; Glycoprotein; Ion transport;
Membrane; Phosphoprotein; Potassium; Potassium transport;
Reference proteome; Signal; Sodium; Sodium transport; Transmembrane;
Transmembrane helix; Transport.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 633 Endosomal/prevacuolar sodium/hydrogen
exchanger.
/FTId=PRO_0000052380.
TOPO_DOM 22 61 Lumenal. {ECO:0000255}.
TRANSMEM 62 82 Helical. {ECO:0000255}.
TOPO_DOM 83 85 Cytoplasmic. {ECO:0000255}.
TRANSMEM 86 106 Helical. {ECO:0000255}.
TOPO_DOM 107 117 Lumenal. {ECO:0000255}.
TRANSMEM 118 138 Helical. {ECO:0000255}.
TOPO_DOM 139 152 Cytoplasmic. {ECO:0000255}.
TRANSMEM 153 173 Helical. {ECO:0000255}.
TOPO_DOM 174 189 Lumenal. {ECO:0000255}.
TRANSMEM 190 211 Helical. {ECO:0000255}.
TOPO_DOM 212 217 Cytoplasmic. {ECO:0000255}.
TRANSMEM 218 238 Helical. {ECO:0000255}.
TOPO_DOM 239 258 Lumenal. {ECO:0000255}.
TRANSMEM 259 279 Helical. {ECO:0000255}.
TOPO_DOM 280 288 Cytoplasmic. {ECO:0000255}.
TRANSMEM 289 308 Helical. {ECO:0000255}.
TOPO_DOM 309 313 Lumenal. {ECO:0000255}.
TRANSMEM 314 333 Helical. {ECO:0000255}.
TOPO_DOM 334 344 Cytoplasmic. {ECO:0000255}.
TRANSMEM 345 364 Helical. {ECO:0000255}.
TOPO_DOM 365 376 Cytoplasmic. {ECO:0000255}.
TRANSMEM 377 397 Helical. {ECO:0000255}.
TOPO_DOM 398 431 Lumenal. {ECO:0000255}.
TRANSMEM 432 452 Helical. {ECO:0000255}.
TOPO_DOM 453 457 Cytoplasmic. {ECO:0000255}.
TRANSMEM 458 478 Helical. {ECO:0000255}.
MOTIF 124 133 Amiloride-binding.
COMPBIAS 23 50 Asp-rich.
MOD_RES 490 490 Phosphothreonine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 494 494 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 498 498 Phosphothreonine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 499 499 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 569 569 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
CARBOHYD 420 420 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 515 515 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11036065}.
CARBOHYD 550 550 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11036065}.
CARBOHYD 563 563 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11036065}.
MUTAGEN 201 201 D->N: Impairs protein-trafficking to the
vacuole. {ECO:0000269|PubMed:11102523}.
MUTAGEN 225 225 E->Q: Impairs protein-trafficking to the
vacuole. {ECO:0000269|PubMed:11102523}.
MUTAGEN 230 230 D->N: Impairs protein-trafficking to the
vacuole. {ECO:0000269|PubMed:11102523}.
MUTAGEN 355 355 E->Q: Impairs partially resistance to
osmotic stress and hygromycin.
{ECO:0000269|PubMed:16671892}.
MUTAGEN 357 357 F->A,L,I: Impairs resistance to osmotic
stress and hygromycin, and blocks
protein-trafficking to the vacuole.
{ECO:0000269|PubMed:16671892}.
MUTAGEN 357 357 F->V: Impairs partially resistance to
osmotic stress and hygromycin.
{ECO:0000269|PubMed:16671892}.
MUTAGEN 361 361 Y->A: Impairs resistance to osmotic
stress and hygromycin, and blocks
protein-trafficking to the vacuole.
{ECO:0000269|PubMed:16671892}.
MUTAGEN 365 365 E->A: Impairs resistance to osmotic
stress and hygromycin, and blocks
protein-trafficking to the vacuole.
{ECO:0000269|PubMed:16671892}.
MUTAGEN 369 369 E->A: Impairs partially resistance to
osmotic stress and hygromycin.
{ECO:0000269|PubMed:16671892}.
MUTAGEN 376 376 P->N: Impairs resistance to osmotic
stress and hygromycin.
{ECO:0000269|PubMed:16671892}.
SEQUENCE 633 AA; 70148 MW; 9B771ABDE41CEB0A CRC64;
MLSKVLLNIA FKVLLTTAKR AVDPDDDDEL LPSPDLPGSD DPIAGDPDVD LNPVTEEMFS
SWALFIMLLL LISALWSSYY LTQKRIRAVH ETVLSIFYGM VIGLIIRMSP GHYIQDTVTF
NSSYFFNVLL PPIILNSGYE LNQVNFFNNM LSILIFAIPG TFISAVVIGI ILYIWTFLGL
ESIDISFADA MSVGATLSAT DPVTILSIFN AYKVDPKLYT IIFGESLLND AISIVMFETC
QKFHGQPATF SSVFEGAGLF LMTFSVSLLI GVLIGILVAL LLKHTHIRRY PQIESCLILL
IAYESYFFSN GCHMSGIVSL LFCGITLKHY AYYNMSRRSQ ITIKYIFQLL ARLSENFIFI
YLGLELFTEV ELVYKPLLII VAAISICVAR WCAVFPLSQF VNWIYRVKTI RSMSGITGEN
ISVPDEIPYN YQMMTFWAGL RGAVGVALAL GIQGEYKFTL LATVLVVVVL TVIIFGGTTA
GMLEVLNIKT GCISEEDTSD DEFDIEAPRA INLLNGSSIQ TDLGPYSDNN SPDISIDQFA
VSSNKNLPNN ISTTGGNTFG GLNETENTSP NPARSSMDKR NLRDKLGTIF NSDSQWFQNF
DEQVLKPVFL DNVSPSLQDS ATQSPADFSS QNH


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EIAAB26536 Na(+)_K(+)_Ca(2+)-exchange protein 1,Nckx1,Rat,Rattus norvegicus,Retinal rod Na-Ca+K exchanger,Slc24a1,Sodium_potassium_calcium exchanger 1
EIAAB26539 Bos taurus,Bovine,Na(+)_K(+)_Ca(2+)-exchange protein 1,NCKX1,Retinal rod Na-Ca+K exchanger,SLC24A1,Sodium_potassium_calcium exchanger 1


 

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