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N6-adenosine-methyltransferase subunit METTL3 (EC 2.1.1.62) (Methyltransferase-like protein 3) (N6-adenosine-methyltransferase 70 kDa subunit) (MT-A70)

 MTA70_MOUSE             Reviewed;         580 AA.
Q8C3P7; Q9CV54; Q9ERS9; Q9WUI4;
25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
25-JUL-2003, sequence version 2.
30-AUG-2017, entry version 114.
RecName: Full=N6-adenosine-methyltransferase subunit METTL3;
EC=2.1.1.62 {ECO:0000269|PubMed:24394384};
AltName: Full=Methyltransferase-like protein 3;
AltName: Full=N6-adenosine-methyltransferase 70 kDa subunit;
Short=MT-A70;
Name=Mettl3; Synonyms=Mta70;
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 [GENOMIC DNA] (ISOFORM 1).
STRAIN=129/Sv;
PubMed=9409616;
Bokar J.A., Shambaugh M.E., Polayes D., Matera A.G., Rottman F.M.;
"Purification and cDNA cloning of the AdoMet-binding subunit of the
human mRNA (N6-adenosine)-methyltransferase.";
RNA 3:1233-1247(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=C57BL/6 X DBA/2;
PubMed=11389549; DOI=10.1002/mrd.1017;
Hwang S.-Y., Oh B., Knowles B.B., Solter D., Lee J.-S.;
"Expression of genes involved in mammalian meiosis during the
transition from egg to embryo.";
Mol. Reprod. Dev. 59:144-158(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Stomach, and Tongue;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
FUNCTION, AND MUTAGENESIS OF 395-ASP--TRP-398.
PubMed=24209618; DOI=10.1016/j.cell.2013.10.026;
Fustin J.M., Doi M., Yamaguchi Y., Hida H., Nishimura S., Yoshida M.,
Isagawa T., Morioka M.S., Kakeya H., Manabe I., Okamura H.;
"RNA-methylation-dependent RNA processing controls the speed of the
circadian clock.";
Cell 155:793-806(2013).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=25456834; DOI=10.1016/j.stem.2014.09.019;
Batista P.J., Molinie B., Wang J., Qu K., Zhang J., Li L.,
Bouley D.M., Lujan E., Haddad B., Daneshvar K., Carter A.C.,
Flynn R.A., Zhou C., Lim K.S., Dedon P., Wernig M., Mullen A.C.,
Xing Y., Giallourakis C.C., Chang H.Y.;
"m(6)A RNA modification controls cell fate transition in mammalian
embryonic stem cells.";
Cell Stem Cell 15:707-719(2014).
[8]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INTERACTION
WITH METTL14.
PubMed=24394384; DOI=10.1038/ncb2902;
Wang Y., Li Y., Toth J.I., Petroski M.D., Zhang Z., Zhao J.C.;
"N-methyladenosine modification destabilizes developmental regulators
in embryonic stem cells.";
Nat. Cell Biol. 16:191-198(2014).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND ENZYME REGULATION.
PubMed=25683224; DOI=10.1016/j.stem.2015.01.016;
Chen T., Hao Y.J., Zhang Y., Li M.M., Wang M., Han W., Wu Y., Lv Y.,
Hao J., Wang L., Li A., Yang Y., Jin K.X., Zhao X., Li Y., Ping X.L.,
Lai W.Y., Wu L.G., Jiang G., Wang H.L., Sang L., Wang X.J., Yang Y.G.,
Zhou Q.;
"m(6)A RNA methylation is regulated by microRNAs and promotes
reprogramming to pluripotency.";
Cell Stem Cell 16:289-301(2015).
[10]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=25569111; DOI=10.1126/science.1261417;
Geula S., Moshitch-Moshkovitz S., Dominissini D., Mansour A.A.,
Kol N., Salmon-Divon M., Hershkovitz V., Peer E., Mor N., Manor Y.S.,
Ben-Haim M.S., Eyal E., Yunger S., Pinto Y., Jaitin D.A., Viukov S.,
Rais Y., Krupalnik V., Chomsky E., Zerbib M., Maza I., Rechavi Y.,
Massarwa R., Hanna S., Amit I., Levanon E.Y., Amariglio N.,
Stern-Ginossar N., Novershtern N., Rechavi G., Hanna J.H.;
"Stem cells. m6A mRNA methylation facilitates resolution of naive
pluripotency toward differentiation.";
Science 347:1002-1006(2015).
-!- FUNCTION: The METTL3-METTL14 heterodimer forms a N6-
methyltransferase complex that methylates adenosine residues of
some RNAs and regulates the circadian clock, differentiation of
embryonic stem cells and primary miRNA processing
(PubMed:25456834, PubMed:24394384, PubMed:25569111). In the
heterodimer formed with METTL14, METTL3 constitutes the catalytic
core (By similarity). N6-methyladenosine (m6A), which takes place
at the 5'-[AG]GAC-3' consensus sites of some mRNAs, plays a role
in the efficiency of mRNA splicing, processing, translation
efficiency, editing and mRNA stability (By similarity). M6A
regulates the length of the circadian clock: acts as an early
pace-setter in the circadian loop by putting mRNA production on a
fast-track for facilitating nuclear processing, thereby providing
an early point of control in setting the dynamics of the feedback
loop (PubMed:24209618). M6A also acts as a regulator of mRNA
stability: in embryonic stem cells (ESCs), m6A methylation of
mRNAs encoding key naive pluripotency-promoting transcripts
results in transcript destabilization, promoting differentiation
of ESCs (PubMed:25456834, PubMed:24394384, PubMed:25569111). M6A
also takes place in other RNA molecules, such as primary miRNA
(pri-miRNAs) (By similarity). METTL3 also mediates methylation of
pri-miRNAs, marking them for recognition and processing by DGCR8
(By similarity). Acts as a positive regulator of mRNA translation
independently of the methyltransferase activity: promotes
translation by interacting with the translation initiation
machinery in the cytoplasm (By similarity).
{ECO:0000250|UniProtKB:Q86U44, ECO:0000269|PubMed:24209618,
ECO:0000269|PubMed:24394384, ECO:0000269|PubMed:25456834,
ECO:0000269|PubMed:25569111}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + m(7)G(5')pppAm = S-
adenosyl-L-homocysteine + m(7)G(5')pppm(6)Am.
{ECO:0000269|PubMed:24394384}.
-!- ENZYME REGULATION: Methyltransferase activity is regulated by
miRNAs via a sequence pairing mechanism.
{ECO:0000269|PubMed:25683224}.
-!- SUBUNIT: Heterodimer; heterodimerizes with METTL14 to form an
antiparallel heterodimer that constitutes an active
methyltransferase. Component of the WMM complex, a N6-
methyltransferase complex composed of WTAP, METTL3 and METTL14.
Interacts with NCBP1/CBP80. Interacts with EIF4E. Interacts with
EIF3B. {ECO:0000250|UniProtKB:Q86U44}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q86U44}.
Nucleus speckle {ECO:0000269|PubMed:24394384,
ECO:0000269|PubMed:25683224}. Cytoplasm
{ECO:0000250|UniProtKB:Q86U44}. Note=Colocalizes with speckles in
interphase nuclei. Suggesting that it may be associated with
nuclear pre-mRNA splicing components (PubMed:24394384).
{ECO:0000269|PubMed:24394384}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8C3P7-1; Sequence=Displayed;
Name=2;
IsoId=Q8C3P7-2; Sequence=VSP_007867, VSP_007868;
Note=No experimental confirmation available.;
-!- DOMAIN: Gate loop 1 and gate loop 2 regions are adjacent to the S-
adenosyl-L-homocysteine-binding site and display large
conformational changes upon ligand-binding. They may play an
important role in adenosine recognition. The interface loop
contributes to the heterodimer interaction.
{ECO:0000250|UniProtKB:Q86U44}.
-!- DISRUPTION PHENOTYPE: Embryonic lethality (PubMed:25569111).
Blastocysts retain normal morphology and expression of
pluripotency markers and yield embryonic stem cells (ESCs) at the
expected ratio. However, they fail to adequately terminate their
naive state and undergo aberrant and restricted lineage priming at
the postimplantation stage, leading to early embryonic lethality
(PubMed:25456834, PubMed:25569111). mRNAs show a nearly complete
absence of N6-methyladenosine (m6A) methylation (PubMed:25456834,
PubMed:25569111). RNAs show defects in splicing and adenosine to
inosine editing (PubMed:25569111). {ECO:0000269|PubMed:25456834,
ECO:0000269|PubMed:25569111}.
-!- SIMILARITY: Belongs to the MT-A70-like family.
{ECO:0000255|PROSITE-ProRule:PRU00489}.
-!- CAUTION: While different publications agree on the role of N6-
methyladenosine (m6A) on RNA stability and its role in embryonic
stem cells (ESCs) pluripotency, the precise function of Mettl3 in
ESCs self-renewal is unclear. A first paper reported that Mettl3
promotes self-renewal of ESCs by maintaining the groung state of
ESCs (PubMed:24394384). However, opposite conclusions were drawn
by publications fromn other groups (PubMed:25456834,
PubMed:25569111). The differences may be explained by different
experimental conditions (such as cell types or RNAi off-target
effects). {ECO:0000269|PubMed:24394384,
ECO:0000269|PubMed:25456834, ECO:0000269|PubMed:25569111}.
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EMBL; AF283992; AAG13957.1; -; Genomic_DNA.
EMBL; AF135789; AAD33673.1; -; mRNA.
EMBL; AK009492; BAB26322.1; -; mRNA.
EMBL; AK085189; BAC39385.1; -; mRNA.
EMBL; BC012526; AAH12526.1; -; mRNA.
CCDS; CCDS27053.1; -. [Q8C3P7-1]
RefSeq; NP_062695.2; NM_019721.2.
UniGene; Mm.271759; -.
ProteinModelPortal; Q8C3P7; -.
SMR; Q8C3P7; -.
BioGrid; 207910; 1.
DIP; DIP-60724N; -.
IntAct; Q8C3P7; 1.
MINT; MINT-4102524; -.
STRING; 10090.ENSMUSP00000022767; -.
iPTMnet; Q8C3P7; -.
PhosphoSitePlus; Q8C3P7; -.
EPD; Q8C3P7; -.
PaxDb; Q8C3P7; -.
PeptideAtlas; Q8C3P7; -.
PRIDE; Q8C3P7; -.
GeneID; 56335; -.
KEGG; mmu:56335; -.
UCSC; uc007tpc.1; mouse. [Q8C3P7-1]
CTD; 56339; -.
MGI; MGI:1927165; Mettl3.
eggNOG; KOG2098; Eukaryota.
eggNOG; COG4725; LUCA.
HOGENOM; HOG000012669; -.
HOVERGEN; HBG052521; -.
InParanoid; Q8C3P7; -.
KO; K05925; -.
PhylomeDB; Q8C3P7; -.
TreeFam; TF323854; -.
ChiTaRS; Mettl3; mouse.
PRO; PR:Q8C3P7; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_METTL3; -.
GO; GO:0036396; C:MIS complex; ISS:UniProtKB.
GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0016422; F:mRNA (2'-O-methyladenosine-N6-)-methyltransferase activity; IDA:UniProtKB.
GO; GO:0001734; F:mRNA (N6-adenosine)-methyltransferase activity; ISO:MGI.
GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
GO; GO:0008173; F:RNA methyltransferase activity; ISO:MGI.
GO; GO:1904047; F:S-adenosyl-L-methionine binding; ISS:UniProtKB.
GO; GO:0006382; P:adenosine to inosine editing; IMP:UniProtKB.
GO; GO:0007623; P:circadian rhythm; IMP:UniProtKB.
GO; GO:0061157; P:mRNA destabilization; IMP:UniProtKB.
GO; GO:0080009; P:mRNA methylation; IMP:UniProtKB.
GO; GO:0016556; P:mRNA modification; ISO:MGI.
GO; GO:0006397; P:mRNA processing; IMP:UniProtKB.
GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:UniProtKB.
GO; GO:1903679; P:positive regulation of cap-independent translational initiation; ISS:UniProtKB.
GO; GO:1990744; P:primary miRNA methylation; ISS:UniProtKB.
GO; GO:0031053; P:primary miRNA processing; ISS:UniProtKB.
GO; GO:0001510; P:RNA methylation; ISS:UniProtKB.
GO; GO:0019827; P:stem cell population maintenance; IMP:UniProtKB.
InterPro; IPR025848; MT-A70.
InterPro; IPR007757; MT-A70-like.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF05063; MT-A70; 1.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS51143; MT_A70; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Biological rhythms;
Complete proteome; Cytoplasm; Methyltransferase; Nucleus;
Phosphoprotein; Reference proteome; RNA-binding;
S-adenosyl-L-methionine; Transferase.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q86U44}.
CHAIN 2 580 N6-adenosine-methyltransferase subunit
METTL3.
/FTId=PRO_0000207631.
REGION 377 378 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:Q86U44}.
REGION 396 410 Gate loop 1.
{ECO:0000250|UniProtKB:Q86U44}.
REGION 450 454 Interaction with METTL14.
{ECO:0000250|UniProtKB:Q86U44}.
REGION 462 479 Interphase loop.
{ECO:0000250|UniProtKB:Q86U44}.
REGION 464 480 Interaction with METTL14.
{ECO:0000250|UniProtKB:Q86U44}.
REGION 465 478 Positively charged region required for
RNA-binding.
{ECO:0000250|UniProtKB:Q86U44}.
REGION 507 515 Gate loop 2.
{ECO:0000250|UniProtKB:Q86U44}.
REGION 536 539 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:Q86U44}.
REGION 549 550 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:Q86U44}.
BINDING 395 395 S-adenosyl-L-methionine.
{ECO:0000250|UniProtKB:Q86U44}.
BINDING 438 438 Interaction with METTL14.
{ECO:0000250|UniProtKB:Q86U44}.
BINDING 441 441 Interaction with METTL14.
{ECO:0000250|UniProtKB:Q86U44}.
BINDING 513 513 S-adenosyl-L-methionine.
{ECO:0000250|UniProtKB:Q86U44}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:Q86U44}.
MOD_RES 43 43 Phosphoserine.
{ECO:0000250|UniProtKB:Q86U44}.
MOD_RES 219 219 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 243 243 Phosphoserine.
{ECO:0000250|UniProtKB:Q86U44}.
VAR_SEQ 34 106 Missing (in isoform 2).
{ECO:0000303|PubMed:11389549}.
/FTId=VSP_007867.
VAR_SEQ 241 299 Missing (in isoform 2).
{ECO:0000303|PubMed:11389549}.
/FTId=VSP_007868.
MUTAGEN 395 398 DPPW->APPA: Loss of activity.
{ECO:0000269|PubMed:24209618}.
CONFLICT 162 162 D -> E (in Ref. 2; AAD33673 and 3;
BAC39385). {ECO:0000305}.
CONFLICT 471 471 R -> P (in Ref. 3; BAB26322).
{ECO:0000305}.
CONFLICT 475 475 W -> L (in Ref. 3; BAB26322).
{ECO:0000305}.
SEQUENCE 580 AA; 64616 MW; 0DBDA2392A37A018 CRC64;
MSDTWSSIQA HKKQLDSLRE RLQRRRKQDS GHLDLRNPEA ALSPTFRSDS PVPTAPTSSG
PKPSTTSVAP ELATDPELEK KLLHHLSDLA LTLPTDAVSI RLAISTPDAP ATQDGVESLL
QKFAAQELIE VKRGLLQDDA HPTLVTYADH SKLSAMMGAV ADKKGLGEVA GTIAGQKRRA
EQDLTTVTTF ASSLASGLAS SASEPAKEPA KKSRKHAASD VDLEIESLLN QQSTKEQQSK
KVSQEILELL NTTTAKEQSI VEKFRSRGRA QVQEFCDYGT KEECMKASDA DRPCRKLHFR
RIINKHTDES LGDCSFLNTC FHMDTCKYVH YEIDACVDSE SPGSKEHMPS QELALTQSVG
GDSSADRLFP PQWICCDIRY LDVSILGKFA VVMADPPWDI HMELPYGTLT DDEMRRLNIP
VLQDDGFLFL WVTGRAMELG RECLNLWGYE RVDEIIWVKT NQLQRIIRTG RTGHWLNHGK
EHCLVGVKGN PQGFNQGLDC DVIVAEVRST SHKPDEIYGM IERLSPGTRK IELFGRPHNV
QPNWITLGNQ LDGIHLLDPD VVARFKQRYP DGIISKPKNL


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U2223m CLIA Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,Inmt,Mouse,Mus musculus,Temt 96T
E2223Rb ELISA Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,INMT,Oryctolagus cuniculus,Rabb 96T
U2223h CLIA Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Homo sapiens,Human,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,INMT 96T
E2223m ELISA Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,Inmt,Mouse,Mus musculus,Temt 96T


 

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