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Guanine nucleotide-binding protein G(t) subunit alpha-3 (Gustducin alpha-3 chain)

 GNAT3_MOUSE             Reviewed;         354 AA.
Q3V3I2;
01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
01-JUL-2008, sequence version 2.
05-DEC-2018, entry version 117.
RecName: Full=Guanine nucleotide-binding protein G(t) subunit alpha-3;
AltName: Full=Gustducin alpha-3 chain;
Name=Gnat3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-310.
STRAIN=C57BL/6J; TISSUE=Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
DISRUPTION PHENOTYPE.
PubMed=8657284; DOI=10.1038/381796a0;
Wong G.T., Gannon K.S., Margolskee R.F.;
"Transduction of bitter and sweet taste by gustducin.";
Nature 381:796-800(1996).
[4]
DISRUPTION PHENOTYPE, AND TRANSGENE.
PubMed=10407021;
Wong G.T., Ruiz-Avila L., Margolskee R.F.;
"Directing gene expression to gustducin-positive taste receptor
cells.";
J. Neurosci. 19:5802-5809(1999).
[5]
FUNCTION, AND SUBUNIT.
PubMed=10570481; DOI=10.1038/15981;
Huang L., Shanker Y.G., Dubauskaite J., Zheng J.Z., Yan W.,
Rosenzweig S., Spielman A.I., Max M., Margolskee R.F.;
"Ggamma13 colocalizes with gustducin in taste receptor cells and
mediates IP3 responses to bitter denatonium.";
Nat. Neurosci. 2:1055-1062(1999).
[6]
FUNCTION.
PubMed=11245589;
Yan W., Sunavala G., Rosenzweig S., Dasso M., Brand J.G.,
Spielman A.I.;
"Bitter taste transduced by PLC-beta(2)-dependent rise in IP(3) and
alpha-gustducin-dependent fall in cyclic nucleotides.";
Am. J. Physiol. 280:C742-C751(2001).
[7]
DISRUPTION PHENOTYPE, AND TRANSGENE.
PubMed=11447270; DOI=10.1073/pnas.151235798;
Ruiz-Avila L., Wong G.T., Damak S., Margolskee R.F.;
"Dominant loss of responsiveness to sweet and bitter compounds caused
by a single mutation in alpha-gustducin.";
Proc. Natl. Acad. Sci. U.S.A. 98:8868-8873(2001).
[8]
TISSUE SPECIFICITY.
PubMed=14637165; DOI=10.1016/j.bbrc.2003.10.137;
Kim M.-R., Kusakabe Y., Miura H., Shindo Y., Ninomiya Y., Hino A.;
"Regional expression patterns of taste receptors and gustducin in the
mouse tongue.";
Biochem. Biophys. Res. Commun. 312:500-506(2003).
[9]
DISRUPTION PHENOTYPE.
PubMed=14586025;
Caicedo A., Pereira E., Margolskee R.F., Roper S.D.;
"Role of the G-protein subunit alpha-gustducin in taste cell responses
to bitter stimuli.";
J. Neurosci. 23:9947-9952(2003).
[10]
DEVELOPMENTAL STAGE.
PubMed=14627646;
Grillet N., Dubreuil V., Dufour H.D., Brunet J.-F.;
"Dynamic expression of RGS4 in the developing nervous system and
regulation by the neural type-specific transcription factor Phox2b.";
J. Neurosci. 23:10613-10621(2003).
[11]
DISRUPTION PHENOTYPE.
PubMed=15342734; DOI=10.1523/JNEUROSCI.2441-04.2004;
He W., Yasumatsu K., Varadarajan V., Yamada A., Lem J., Ninomiya Y.,
Margolskee R.F., Damak S.;
"Umami taste responses are mediated by alpha-transducin and alpha-
gustducin.";
J. Neurosci. 24:7674-7680(2004).
[12]
DEVELOPMENTAL STAGE.
PubMed=16933139; DOI=10.1007/s00429-006-0112-2;
Zhang G.-H., Deng S.-P., Li L.-L., Li H.-T.;
"Developmental change of alpha-gustducin expression in the mouse
fungiform papilla.";
Anat. Embryol. (Berl.) 211:625-630(2006).
[13]
DISRUPTION PHENOTYPE.
PubMed=16740645; DOI=10.1093/chemse/bjj062;
Danilova V., Damak S., Margolskee R.F., Hellekant G.;
"Taste responses to sweet stimuli in alpha-gustducin knockout and
wild-type mice.";
Chem. Senses 31:573-580(2006).
[14]
TISSUE SPECIFICITY.
PubMed=17290008; DOI=10.1152/ajpgi.00504.2006;
Sutherland K., Young R.L., Cooper N.J., Horowitz M., Blackshaw L.A.;
"Phenotypic characterization of taste cells of the mouse small
intestine.";
Am. J. Physiol. 292:G1420-G1428(2007).
[15]
TISSUE SPECIFICITY.
PubMed=17229761; DOI=10.1093/chemse/bjl053;
Stone L.M., Barrows J., Finger T.E., Kinnamon S.C.;
"Expression of T1Rs and gustducin in palatal taste buds of mice.";
Chem. Senses 32:255-262(2007).
[16]
TISSUE SPECIFICITY.
PubMed=17021831; DOI=10.1007/s00359-006-0168-8;
Fehr J., Meyer D., Widmayer P., Borth H.C., Ackermann F., Wilhelm B.,
Gudermann T., Boekhoff I.;
"Expression of the G-protein alpha-subunit gustducin in mammalian
spermatozoa.";
J. Comp. Physiol. A 193:21-34(2007).
[17]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17724330; DOI=10.1073/pnas.0706890104;
Jang H.-J., Kokrashvili Z., Theodorakis M.J., Carlson O.D., Kim B.-J.,
Zhou J., Kim H.H., Xu X., Chan S.L., Juhaszova M., Bernier M.,
Mosinger B., Margolskee R.F., Egan J.M.;
"Gut-expressed gustducin and taste receptors regulate secretion of
glucagon-like peptide-1.";
Proc. Natl. Acad. Sci. U.S.A. 104:15069-15074(2007).
[18]
FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=17724332; DOI=10.1073/pnas.0706678104;
Margolskee R.F., Dyer J., Kokrashvili Z., Salmon K.S., Ilegems E.,
Daly K., Maillet E.L., Ninomiya Y., Mosinger B., Shirazi-Beechey S.P.;
"T1R3 and gustducin in gut sense sugars to regulate expression of Na+-
glucose cotransporter 1.";
Proc. Natl. Acad. Sci. U.S.A. 104:15075-15080(2007).
-!- FUNCTION: Guanine nucleotide-binding protein (G protein) alpha
subunit playing a prominent role in bitter and sweet taste
transduction as well as in umami (monosodium glutamate,
monopotassium glutamate, and inosine monophosphate) taste
transduction. Transduction by this alpha subunit involves coupling
of specific cell-surface receptors with a cGMP-phosphodiesterase;
Activation of phosphodiesterase lowers intracellular levels of
cAMP and cGMP which may open a cyclic nucleotide-suppressible
cation channel leading to influx of calcium, ultimately leading to
release of neurotransmitter. Indeed, denatonium and strychnine
induce transient reduction in cAMP and cGMP in taste tissue,
whereas this decrease is inhibited by GNAT3 antibody. Gustducin
heterotrimer transduces response to bitter and sweet compounds via
regulation of phosphodiesterase for alpha subunit, as well as via
activation of phospholipase C for beta and gamma subunits, with
ultimate increase inositol trisphosphate and increase of
intracellular Calcium. GNAT3 can functionally couple to taste
receptors to transmit intracellular signal: receptor heterodimer
TAS1R2/TAS1R3 senses sweetness and TAS1R1/TAS1R3 transduces umami
taste, whereas the T2R family GPCRs act as bitter sensors.
Functions also as lumenal sugar sensors in the gut to control the
expression of the Na+-glucose transporter SGLT1 in response to
dietaty sugar, as well as the secretion of Glucagon-like peptide-
1, GLP-1 and glucose-dependent insulinotropic polypeptide, GIP.
Thus, may modulate the gut capacity to absorb sugars, with
implications in malabsorption syndromes and diet-related disorders
including diabetes and obesity. {ECO:0000269|PubMed:10570481,
ECO:0000269|PubMed:11245589, ECO:0000269|PubMed:17724330,
ECO:0000269|PubMed:17724332}.
-!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and
gamma, respectively GNAT3, GNB1 and GNG13 for Gustducin
heterotrimer for bitter taste transduction. The alpha chain
contains the guanine nucleotide binding site. Gustducin
heterotrimer may also be composed of GNAT3, GNB3 and GNG13.
{ECO:0000269|PubMed:10570481}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in taste buds (sensory organs of
clustered epithelial cells) of the circumvallate and fungiform
papillae of the tongue as well as in palatal taste buds at protein
level. Expressed in enteroendocrine cells of the gut, such as in
subsets of enteroendocrine cells in the midjejunum and brush
cells. Detected also in spermatozoa. {ECO:0000269|PubMed:14637165,
ECO:0000269|PubMed:17021831, ECO:0000269|PubMed:17229761,
ECO:0000269|PubMed:17290008, ECO:0000269|PubMed:17724332}.
-!- DEVELOPMENTAL STAGE: From week 1 to 7, the number of cells
expressing GNAT3 in single taste buds increases within fungiform
papilla; by week 7, the number reached the value found in adults.
Expressed in cell bodies and axons of facial motor neurons at
E10.5. {ECO:0000269|PubMed:14627646, ECO:0000269|PubMed:16933139}.
-!- PTM: Potential N-myristoylation may anchor alpha-subunit to the
inner surface of plasma membrane. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice are not affected in their tasting
ability for salty (NaCl) and sour (HCl) stimuli, which are known
not to be mediated by G proteins; but, they exhibit a significant
reduction in the ability to taste the bitter compounds denatonium
and quinine as well as the sweet compounds sucrose and SC45647, a
guanidine sweetener. The incidence of cells responding to bitter
stimulus is also reduced by seventy per cent. The residual
behavioral response to bitter and sweet taste in these deficient
mice suggests that there is alternative mechanism to compensate.
However, transgenic expression of Gnat3 in these deficient mice
restores responsiveness to both bitter and sweet compounds,
whereas expression of mutated 'Gly-352' transgene do not.
Furthermore, in wild-type mice, this mutated transgene acts as
dominant-negative by inhibition of endogenous Gnat3 interactions
with taste receptors. Mice show less preference for acesulfame-K,
dulcin, fructose, D-phenylalanine, L-proline, D-tryptophan,
saccharin, sweetener SC45647 and sucrose; Furthermore, in their
gut, sugar or sweeteners do not increase SGLT1 expression and
glucose-absorptive capacity compared to wild-type mice and the
ingestion of glucose reveals deficiencies in secretion of GLP-1
and regulation of plasma insulin and glucose. Mice lacking GNAT3
show less preference for umami compounds such as monosodium
glutamate (MSG) and no preference for inosine monophosphate (IMP)
whereas wild-type mice strongly prefer IMP. The response to umami
signals implicates the anteriorly placed taste buds of the tongue,
and not the posterior part. {ECO:0000269|PubMed:10407021,
ECO:0000269|PubMed:11447270, ECO:0000269|PubMed:14586025,
ECO:0000269|PubMed:15342734, ECO:0000269|PubMed:16740645,
ECO:0000269|PubMed:17724330, ECO:0000269|PubMed:17724332,
ECO:0000269|PubMed:8657284}.
-!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AC129572; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK040065; BAE20568.1; -; mRNA.
CCDS; CCDS39017.1; -.
RefSeq; NP_001074612.1; NM_001081143.1.
UniGene; Mm.332230; -.
ProteinModelPortal; Q3V3I2; -.
SMR; Q3V3I2; -.
STRING; 10090.ENSMUSP00000030561; -.
iPTMnet; Q3V3I2; -.
PhosphoSitePlus; Q3V3I2; -.
MaxQB; Q3V3I2; -.
PaxDb; Q3V3I2; -.
PRIDE; Q3V3I2; -.
Ensembl; ENSMUST00000030561; ENSMUSP00000030561; ENSMUSG00000028777.
GeneID; 242851; -.
KEGG; mmu:242851; -.
UCSC; uc008wnr.1; mouse.
CTD; 346562; -.
MGI; MGI:3588268; Gnat3.
eggNOG; KOG0082; Eukaryota.
eggNOG; ENOG410XNVQ; LUCA.
GeneTree; ENSGT00940000161422; -.
HOGENOM; HOG000038730; -.
HOVERGEN; HBG063184; -.
InParanoid; Q3V3I2; -.
KO; K19729; -.
OMA; HKYFATT; -.
OrthoDB; EOG091G0VUT; -.
PhylomeDB; Q3V3I2; -.
TreeFam; TF300673; -.
Reactome; R-MMU-112043; PLC beta mediated events.
Reactome; R-MMU-170670; Adenylate cyclase inhibitory pathway.
Reactome; R-MMU-202040; G-protein activation.
Reactome; R-MMU-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
Reactome; R-MMU-392170; ADP signalling through P2Y purinoceptor 12.
Reactome; R-MMU-418594; G alpha (i) signalling events.
Reactome; R-MMU-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
PRO; PR:Q3V3I2; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000028777; Expressed in 15 organ(s), highest expression level in vallate papilla.
ExpressionAtlas; Q3V3I2; baseline and differential.
GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
GO; GO:0005930; C:axoneme; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
GO; GO:0001917; C:photoreceptor inner segment; IBA:GO_Central.
GO; GO:0001750; C:photoreceptor outer segment; IBA:GO_Central.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
GO; GO:0005525; F:GTP binding; ISO:MGI.
GO; GO:0003924; F:GTPase activity; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
GO; GO:0001580; P:detection of chemical stimulus involved in sensory perception of bitter taste; IBA:GO_Central.
GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:MGI.
GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
GO; GO:0050913; P:sensory perception of bitter taste; IMP:MGI.
GO; GO:0050916; P:sensory perception of sweet taste; IMP:MGI.
GO; GO:0050909; P:sensory perception of taste; IDA:MGI.
GO; GO:0050917; P:sensory perception of umami taste; IMP:MGI.
CDD; cd00066; G-alpha; 1.
Gene3D; 1.10.400.10; -; 1.
InterPro; IPR001408; Gprotein_alpha_I.
InterPro; IPR001019; Gprotein_alpha_su.
InterPro; IPR011025; GproteinA_insert.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR10218; PTHR10218; 1.
Pfam; PF00503; G-alpha; 1.
PRINTS; PR00318; GPROTEINA.
PRINTS; PR00441; GPROTEINAI.
SMART; SM00275; G_alpha; 1.
SUPFAM; SSF47895; SSF47895; 1.
SUPFAM; SSF52540; SSF52540; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; GTP-binding; Lipoprotein; Magnesium;
Metal-binding; Myristate; Nucleotide-binding; Reference proteome;
Transducer.
INIT_MET 1 1 Removed.
CHAIN 2 354 Guanine nucleotide-binding protein G(t)
subunit alpha-3.
/FTId=PRO_0000342672.
NP_BIND 40 47 GTP. {ECO:0000250}.
NP_BIND 175 181 GTP. {ECO:0000250}.
NP_BIND 200 204 GTP. {ECO:0000250}.
NP_BIND 269 272 GTP. {ECO:0000250}.
METAL 47 47 Magnesium. {ECO:0000250}.
METAL 181 181 Magnesium. {ECO:0000250}.
BINDING 326 326 GTP; via amide nitrogen. {ECO:0000250}.
LIPID 2 2 N-myristoyl glycine. {ECO:0000250}.
SEQUENCE 354 AA; 40316 MW; 05DBC95DAC356CEF CRC64;
MGSGISSESK ESARRSKELE KKLQEDAERD ARTVKLLLLG AGESGKSTIV KQMKIIHKNG
YSKQECMEFK AVIYSNTLQS ILAIVKAMAT LGIDYVNPRS REDQEQLHSM ANTLEDGDMT
PQLAEIIKRL WGDPGIQACF ERASEYQLND SAAYYLNDLD RLTAPGYVPN EQDVLHSRVK
TTGIIETQFS FKDLNFRMFD VGGQRSERKK WIHCFEGVTC IIFCAALSAY DMVLVEDEEV
NRMHESLHLF NSICNHKYFA TTSIVLFLNK KDLFQEKVAK VHLSICFPEY TGPNTFEDAG
NYIKNQFLDL NLKKEDKEIY SHMTCATDTQ NVKFVFDAVT DIIIKENLKD CGLF


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547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
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IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
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ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
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GENTAUR Poland Sp. z o.o.


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