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Regulator of nonsense transcripts 1 (EC 3.6.4.-) (ATP-dependent helicase RENT1) (Nonsense mRNA reducing factor 1) (NORF1) (Up-frameshift suppressor 1 homolog) (mUpf1)

 RENT1_MOUSE             Reviewed;        1124 AA.
Q9EPU0; Q3UG00; Q6GYP5; Q6PHQ5; Q8K0N4; Q99PR4;
18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
29-MAY-2007, sequence version 2.
12-SEP-2018, entry version 157.
RecName: Full=Regulator of nonsense transcripts 1;
EC=3.6.4.-;
AltName: Full=ATP-dependent helicase RENT1;
AltName: Full=Nonsense mRNA reducing factor 1;
Short=NORF1;
AltName: Full=Up-frameshift suppressor 1 homolog;
Short=mUpf1;
Name=Upf1; Synonyms=Rent1;
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 [MRNA] (ISOFORM 2), AND DISRUPTION PHENOTYPE.
STRAIN=129/Sv;
PubMed=11152657; DOI=10.1093/hmg/10.2.99;
Medghalchi S.M., Frischmeyer P.A., Mendell J.T., Kelly A.G.,
Lawler A.M., Dietz H.C.;
"Rent1, a trans-effector of nonsense-mediated mRNA decay, is essential
for mammalian embryonic viability.";
Hum. Mol. Genet. 10:99-105(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Selg M., Strande J., Beck-Engeser G.B.J., Liehr T., Winkler T.,
Jack H.-M.;
"Genomic structure, chromosomal localization and expression of murine
nonsense mRNA reducing factor 1 (mNORF1).";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
STRAIN=129/SvJ;
Selg M., Strande J.L., Liehr T., Roth E., Beck-Engeser G.B.,
Winkler T.H., Jack H.-M.;
"Cloning, genomic structure, chromosomal localization and expression
of mHUPF1, the murine homolog of the yeast nonsense mRNA reducing
factor UPF1.";
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Brain, Embryo, and Eye;
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 73-1113 (ISOFORM 2).
STRAIN=129/Sv;
PubMed=8855285; DOI=10.1073/pnas.93.20.10928;
Perlick H.A., Medghalchi S.M., Spencer F.A., Kendzior R.J. Jr.,
Dietz H.C.;
"Mammalian orthologues of a yeast regulator of nonsense transcript
stability.";
Proc. Natl. Acad. Sci. U.S.A. 93:10928-10932(1996).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1102, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1102 AND SER-1105, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, 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).
-!- FUNCTION: RNA-dependent helicase and ATPase required for nonsense-
mediated decay (NMD) of mRNAs containing premature stop codons. Is
recruited to mRNAs upon translation termination and undergoes a
cycle of phosphorylation and dephosphorylation; its
phosphorylation appears to be a key step in NMD. Recruited by
release factors to stalled ribosomes together with the SMG1C
protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1-
eRF3) complex. In EJC-dependent NMD, the SURF complex associates
with the exon junction complex (EJC) (located 50-55 or more
nucleotides downstream from the termination codon) through UPF2
and allows the formation of an UPF1-UPF2-UPF3 surveillance complex
which is believed to activate NMD. Phosphorylated UPF1 is
recognized by EST1B/SMG5, SMG6 and SMG7 which are thought to
provide a link to the mRNA degradation machinery involving
exonucleolytic and endonucleolytic pathways, and to serve as
adapters to protein phosphatase 2A (PP2A), thereby triggering UPF1
dephosphorylation. UPF1 can also activate NMD without UPF2 or
UPF3, and in the absence of the NMD-enhancing downstream EJC
indicative for alternative NMD pathways. Plays a role in
replication-dependent histone mRNA degradation at the end of phase
S; the function is independent of UPF2. For the recognition of
premature termination codons (PTC) and initiation of NMD a
competitive interaction between UPF1 and PABPC1 with the ribosome-
bound release factors is proposed. The ATPase activity of UPF1 is
required for disassembly of mRNPs undergoing NMD (By similarity).
Essential for embryonic viability. {ECO:0000250}.
-!- SUBUNIT: Found in a post-splicing messenger ribonucleoprotein
(mRNP) complex. Associates with the exon junction complex (EJC).
Associates with the SGM1C complex; is phosphorylated by the
complex kinase component SGM1. Interacts with UPF2. Interacts with
UPF3A and UPF3B. Interacts with EST1A. Interacts with SLBP.
Interacts (when hyperphosphorylated) with PNRC2. Interacts with
AGO1 and AGO2. Interacts with GSPT2. Interacts with isoform 1 and
isoform 5 of ADAR/ADAR1. Interacts with SMG7. Interacts with
ZC3H12A; this interaction occurs in a mRNA translationally
active- and termination-dependent manner and is essential for
ZC3H12A-mediated degradation of target mRNAs. Interacts with
CPSF6. {ECO:0000250|UniProtKB:Q92900}.
-!- INTERACTION:
Q7TMF2:Eri1; NbExp=2; IntAct=EBI-6876715, EBI-16026214;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, P-body {ECO:0000250}.
Nucleus {ECO:0000250}. Note=Hyperphosphorylated form is targeted
to the P-body, while unphosphorylated protein is distributed
throughout the cytoplasm. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9EPU0-1; Sequence=Displayed;
Name=2;
IsoId=Q9EPU0-2; Sequence=VSP_025764;
-!- DOMAIN: The [ST]-Q motif constitutes a recognition sequence for
kinases from the PI3/PI4-kinase family. {ECO:0000250}.
-!- PTM: Phosphorylated by SMG1; required for formation of mRNA
surveillance complexes. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Embryos are viable in pre-implantation
period, show complete loss of NMD but are resorbed shortly after
implantation. {ECO:0000269|PubMed:11152657}.
-!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
{ECO:0000305}.
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EMBL; AF322655; AAG42830.1; -; mRNA.
EMBL; AY597039; AAT46119.1; -; Genomic_DNA.
EMBL; AY597038; AAT46119.1; JOINED; Genomic_DNA.
EMBL; AK148196; BAE28409.1; -; mRNA.
EMBL; BC030916; AAH30916.1; -; mRNA.
EMBL; BC052149; AAH52149.1; -; mRNA.
EMBL; BC056442; AAH56442.1; -; mRNA.
EMBL; AF182947; AAK08652.1; -; mRNA.
CCDS; CCDS52572.1; -. [Q9EPU0-1]
RefSeq; NP_001116301.1; NM_001122829.2. [Q9EPU0-1]
RefSeq; NP_109605.2; NM_030680.3. [Q9EPU0-2]
RefSeq; XP_006509667.1; XM_006509604.3. [Q9EPU0-1]
RefSeq; XP_006509668.1; XM_006509605.3. [Q9EPU0-1]
UniGene; Mm.258280; -.
UniGene; Mm.390048; -.
ProteinModelPortal; Q9EPU0; -.
SMR; Q9EPU0; -.
BioGrid; 202860; 7.
DIP; DIP-60114N; -.
IntAct; Q9EPU0; 10.
MINT; Q9EPU0; -.
STRING; 10090.ENSMUSP00000075089; -.
iPTMnet; Q9EPU0; -.
PhosphoSitePlus; Q9EPU0; -.
SwissPalm; Q9EPU0; -.
PaxDb; Q9EPU0; -.
PeptideAtlas; Q9EPU0; -.
PRIDE; Q9EPU0; -.
Ensembl; ENSMUST00000075666; ENSMUSP00000075089; ENSMUSG00000058301. [Q9EPU0-1]
Ensembl; ENSMUST00000215817; ENSMUSP00000148927; ENSMUSG00000058301. [Q9EPU0-2]
GeneID; 19704; -.
KEGG; mmu:19704; -.
UCSC; uc009mab.2; mouse. [Q9EPU0-1]
UCSC; uc012gfa.1; mouse. [Q9EPU0-2]
CTD; 5976; -.
MGI; MGI:107995; Upf1.
eggNOG; KOG1802; Eukaryota.
eggNOG; COG1112; LUCA.
GeneTree; ENSGT00800000124068; -.
HOGENOM; HOG000205990; -.
HOVERGEN; HBG061556; -.
InParanoid; Q9EPU0; -.
KO; K14326; -.
OMA; QPCAAQN; -.
OrthoDB; EOG091G01B6; -.
PhylomeDB; Q9EPU0; -.
TreeFam; TF300554; -.
Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
ChiTaRS; Upf1; mouse.
PRO; PR:Q9EPU0; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000058301; Expressed in 208 organ(s), highest expression level in skin of back.
Genevisible; Q9EPU0; MM.
GO; GO:0000785; C:chromatin; ISS:HGNC.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0035145; C:exon-exon junction complex; ISO:MGI.
GO; GO:0000784; C:nuclear chromosome, telomeric region; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
GO; GO:0044530; C:supraspliceosomal complex; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004004; F:ATP-dependent RNA helicase activity; ISS:UniProtKB.
GO; GO:0003682; F:chromatin binding; ISS:HGNC.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0042162; F:telomeric DNA binding; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISS:UniProtKB.
GO; GO:0044770; P:cell cycle phase transition; ISS:UniProtKB.
GO; GO:0071347; P:cellular response to interleukin-1; ISS:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
GO; GO:0006281; P:DNA repair; ISS:HGNC.
GO; GO:0006260; P:DNA replication; ISS:HGNC.
GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; IMP:MGI.
GO; GO:0071044; P:histone mRNA catabolic process; ISS:UniProtKB.
GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; ISO:MGI.
GO; GO:0000294; P:nuclear-transcribed mRNA catabolic process, endonucleolytic cleavage-dependent decay; ISS:UniProtKB.
GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISO:MGI.
GO; GO:0061014; P:positive regulation of mRNA catabolic process; ISS:UniProtKB.
GO; GO:0032204; P:regulation of telomere maintenance; ISO:MGI.
GO; GO:0006449; P:regulation of translational termination; ISS:HGNC.
GO; GO:0032201; P:telomere maintenance via semi-conservative replication; ISO:MGI.
InterPro; IPR006935; Helicase/UvrB_N.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR018999; RNA-helicase_UPF1_UPF2-interct.
Pfam; PF04851; ResIII; 1.
Pfam; PF09416; UPF1_Zn_bind; 1.
SUPFAM; SSF52540; SSF52540; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome; Cytoplasm;
Helicase; Hydrolase; Metal-binding; Methylation;
Nonsense-mediated mRNA decay; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Repeat; RNA-binding; Zinc;
Zinc-finger.
CHAIN 1 1124 Regulator of nonsense transcripts 1.
/FTId=PRO_0000080717.
ZN_FING 116 267 UPF1-type.
NP_BIND 501 505 ATP. {ECO:0000250}.
REGION 1 410 Sufficient for interaction with RENT2.
{ECO:0000250}.
MOTIF 1084 1085 [ST]-Q motif 1.
MOTIF 1102 1103 [ST]-Q motif 2.
COMPBIAS 47 75 Ala/Gly/Pro-rich.
COMPBIAS 1037 1124 Gln/Ser-rich.
BINDING 481 481 ATP. {ECO:0000250}.
BINDING 671 671 ATP. {ECO:0000250}.
BINDING 708 708 ATP. {ECO:0000250}.
BINDING 839 839 ATP. {ECO:0000250}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000250|UniProtKB:Q92900}.
MOD_RES 31 31 Phosphoserine.
{ECO:0000250|UniProtKB:Q92900}.
MOD_RES 560 560 Phosphoserine.
{ECO:0000250|UniProtKB:Q92900}.
MOD_RES 951 951 Phosphoserine.
{ECO:0000250|UniProtKB:Q92900}.
MOD_RES 1014 1014 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q92900}.
MOD_RES 1084 1084 Phosphoserine.
{ECO:0000250|UniProtKB:Q92900}.
MOD_RES 1102 1102 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 1105 1105 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1122 1122 Phosphoserine.
{ECO:0000250|UniProtKB:Q92900}.
VAR_SEQ 348 358 Missing (in isoform 2).
{ECO:0000303|PubMed:11152657,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8855285,
ECO:0000303|Ref.2}.
/FTId=VSP_025764.
CONFLICT 56 56 G -> S (in Ref. 3; AAT46119).
{ECO:0000305}.
CONFLICT 58 58 G -> A (in Ref. 4; BAE28409).
{ECO:0000305}.
CONFLICT 60 60 A -> P (in Ref. 3; AAT46119).
{ECO:0000305}.
CONFLICT 71 71 A -> S (in Ref. 3; AAT46119).
{ECO:0000305}.
CONFLICT 428 428 R -> K (in Ref. 3; AAT46119).
{ECO:0000305}.
CONFLICT 439 439 D -> E (in Ref. 3; AAT46119).
{ECO:0000305}.
CONFLICT 460 460 V -> F (in Ref. 3; AAT46119).
{ECO:0000305}.
CONFLICT 495 495 L -> F (in Ref. 3; AAT46119).
{ECO:0000305}.
CONFLICT 633 633 K -> E (in Ref. 4; BAE28409).
{ECO:0000305}.
CONFLICT 820 820 H -> Y (in Ref. 4; BAE28409).
{ECO:0000305}.
SEQUENCE 1124 AA; 123967 MW; 5F1B0ED50F63C52E CRC64;
MSVEAYGPSS QTLTFLDTEE AELLGADTQG SEFEFTDFTL PSQTQTPPGG PGGAGGPGGA
GAGGAAGQLD AQVGPEGILQ NGAVDDSVAK TSQLLAELNF EEDEEDTYYT KDLPVHACSY
CGIHDPACVV YCNTSKKWFC NGRGNTSGSH IVNHLVRAKC KEVTLHKDGP LGETVLECYN
CGCRNVFLLG FIPAKADSVV VLLCRQPCAS QSSLKDINWD SSQWQPLIQD RCFLSWLVKI
PSEQEQLRAR QITAQQINKL EELWKENPSA TLEDLEKPGV DEEPQHVLLR YEDAYQYQNI
FGPLVKLEAD YDKKLKESQT QDNITVRWDL GLNKKRIAFF TLPKTDSGNE DLVIIWLRDM
RLMQGDEICL RYKGDLAPLW KGIGHVIKVP DNYGDEIAIE LRSSVGAPVE VTHNFQVDFV
WKSTSFDRMQ SALKTFAVDE TSVSGYIYHK LLGHEVEDVV IKCQLPKRFT AQGLPDLNHS
QVYAVKTVLQ RPLSLIQGPP GTGKTVTSAT IVYHLARQGN GPVLVCAPSN IAVDQLTEKI
HQTGLKVVRL CAKSREAIDS PVSFLALHNQ IRNMDSMPEL QKLQQLKDET GELSSADEKR
YRALKRTAER ELLMNADVIC CTCVGAGDPR LAKMQFRSIL IDESTQATEP ECMVPVVLGA
KQLILVGDHC QLGPVVMCKK AAKAGLSQSL FERLVVLGIR PIRLQVQYRM HPALSAFPSN
IFYEGSLQNG VTAADRVKKG FDFQWPQPDK PMFFYVTQGQ EEIASSGTSY LNRTEAANVE
KITTKLLKAG AKPDQIGIIT PYEGQRSYLV QYMQFSGSLH TKLYQEVEIA SVDAFQGREK
DFIILSCVRA NEHQGIGFLN DPRRLNVALT RARYGVIIVG NPKALSKQPL WNHLLSYYKE
QKALVEGPLN NLRESLMQFS KPRKLVNTVN PGARFMTTAM YDAREAIIPG SVYDRSSQGR
PSNMYFQTHD QISMISAGPS HVAAMNIPIP FNLVMPPMPP PGYFGQANGP AAGRGTPKTK
TGRGGRQKNR FGLPGPSQTT LPNSQASQDV ASQPFSQGAL TQGYVSMSQP SQMSQPGLSQ
PELSQDSYLG DEFKSQIDVA LSQDSTYQGE RAYQHGGVTG LSQY


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E3034h Human Regulator Of Nonsense Transcripts 1 ELISA Ki 96T
WAPL_MOUSE Human ELISA Kit FOR Regulator of nonsense transcripts 3A 96T


 

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