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DnaJ homolog subfamily C member 3 (Endoplasmic reticulum DNA J domain-containing protein 6) (ER-resident protein ERdj6) (ERdj6) (Interferon-induced, double-stranded RNA-activated protein kinase inhibitor) (Protein kinase inhibitor of 58 kDa) (Protein kinase inhibitor p58)

 DNJC3_HUMAN             Reviewed;         504 AA.
Q13217; Q86WT9; Q8N4N2;
16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 164.
RecName: Full=DnaJ homolog subfamily C member 3;
AltName: Full=Endoplasmic reticulum DNA J domain-containing protein 6;
Short=ER-resident protein ERdj6;
Short=ERdj6;
AltName: Full=Interferon-induced, double-stranded RNA-activated protein kinase inhibitor;
AltName: Full=Protein kinase inhibitor of 58 kDa;
Short=Protein kinase inhibitor p58;
Flags: Precursor;
Name=DNAJC3; Synonyms=P58IPK, PRKRI;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=8666242; DOI=10.1016/0378-1119(95)00883-7;
Korth M.J., Lyons C.N., Wambach M., Katze M.G.;
"Cloning, expression, and cellular localization of the oncogenic 58-
kDa inhibitor of the RNA-activated human and mouse protein kinase.";
Gene 170:181-188(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Leukocyte;
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]
FUNCTION, AND INTERACTION WITH EIF2AK2.
PubMed=8576172; DOI=10.1074/jbc.271.3.1702;
Polyak S.J., Tang N., Wambach M., Barber G.N., Katze M.G.;
"The P58 cellular inhibitor complexes with the interferon-induced,
double-stranded RNA-dependent protein kinase, PKR, to regulate its
autophosphorylation and activity.";
J. Biol. Chem. 271:1702-1707(1996).
[6]
FUNCTION, INTERACTION WITH THAP12, AND INDUCTION.
PubMed=9447982; DOI=10.1128/MCB.18.2.859;
Gale M.J. Jr., Blakely C.M., Hopkins D.A., Melville M.W., Wambach M.,
Romano P.R., Katze M.G.;
"Regulation of interferon-induced protein kinase PKR: modulation of
P58IPK inhibitory function by a novel protein, P52rIPK.";
Mol. Cell. Biol. 18:859-871(1998).
[7]
FUNCTION, INTERACTION WITH DNAJB1 AND HSPA8, AND INDUCTION.
PubMed=9920933; DOI=10.1074/jbc.274.6.3797;
Melville M.W., Tan S.-L., Wambach M., Song J., Morimoto R.I.,
Katze M.G.;
"The cellular inhibitor of the PKR protein kinase, P58(IPK), is an
influenza virus-activated co-chaperone that modulates heat shock
protein 70 activity.";
J. Biol. Chem. 274:3797-3803(1999).
[8]
FUNCTION, AND INDUCTION.
PubMed=12601012; DOI=10.1074/jbc.M212074200;
van Huizen R., Martindale J.L., Gorospe M., Holbrook N.J.;
"P58IPK, a novel endoplasmic reticulum stress-inducible protein and
potential negative regulator of eIF2alpha signaling.";
J. Biol. Chem. 278:15558-15564(2003).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
INVOLVEMENT IN ACPHD.
PubMed=25466870; DOI=10.1016/j.ajhg.2014.10.013;
Synofzik M., Haack T.B., Kopajtich R., Gorza M., Rapaport D.,
Greiner M., Schoenfeld C., Freiberg C., Schorr S., Holl R.W.,
Gonzalez M.A., Fritsche A., Fallier-Becker P., Zimmermann R.,
Strom T.M., Meitinger T., Zuechner S., Schuele R., Schoels L.,
Prokisch H.;
"Absence of BiP co-chaperone DNAJC3 causes diabetes mellitus and
multisystemic neurodegeneration.";
Am. J. Hum. Genet. 95:689-697(2014).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[12]
PHOSPHORYLATION AT SER-274.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[14]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 35-461, AND DISULFIDE BONDS.
PubMed=21799829; DOI=10.1371/journal.pone.0022337;
Svard M., Biterova E.I., Bourhis J.M., Guy J.E.;
"The crystal structure of the human co-chaperone P58(IPK).";
PLoS ONE 6:E22337-E22337(2011).
-!- FUNCTION: Involved in the unfolded protein response (UPR) during
endoplasmic reticulum (ER) stress. Acts as a negative regulator of
the EIF2AK4/GCN2 kinase activity by preventing the phosphorylation
of eIF-2-alpha at 'Ser-52' and hence attenuating general protein
synthesis under ER stress, hypothermic and amino acid starving
stress conditions (By similarity). Co-chaperone of HSPA8/HSC70, it
stimulates its ATPase activity. May inhibit both the
autophosphorylation of EIF2AK2/PKR and the ability of EIF2AK2 to
catalyze phosphorylation of the EIF2A. May inhibit EIF2AK3/PERK
activity. {ECO:0000250|UniProtKB:Q27968,
ECO:0000250|UniProtKB:Q91YW3, ECO:0000269|PubMed:12601012,
ECO:0000269|PubMed:8576172, ECO:0000269|PubMed:9447982,
ECO:0000269|PubMed:9920933}.
-!- SUBUNIT: Interacts with EIF2AK4/GCN2; this interaction occurs
under endoplasmic reticulum (ER) stress, hypothermic and amino
acid starving stress conditions and inhibits EIF2AK4/GCN2 kinase
activity. Interacts with EIF2AK3 (By similarity). Interacts with
EIF2AK2 (PubMed:8576172). Forms a trimeric complex with DNAJB1 and
HSPA8 (PubMed:9920933). Interacts with THAP12 (PubMed:9447982).
{ECO:0000250|UniProtKB:Q91YW3, ECO:0000269|PubMed:8576172,
ECO:0000269|PubMed:9447982, ECO:0000269|PubMed:9920933}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}.
-!- TISSUE SPECIFICITY: Widely expressed with high level in the
pancreas and testis. Also expressed in cell lines with different
levels. {ECO:0000269|PubMed:8666242}.
-!- INDUCTION: Up-regulated during an endoplasmic reticulum stress via
ATF6. Activated in response to infection by influenza virus
through the dissociation of DNAJB1. Down-regulated by DNAJB1 and
THAP12. {ECO:0000269|PubMed:12601012, ECO:0000269|PubMed:9447982,
ECO:0000269|PubMed:9920933}.
-!- DOMAIN: The J domain mediates interaction with HSPA8.
-!- DOMAIN: Binding to misfolded proteins is mediated by a hydrophobic
patch forming a large groove within the first two TPR repeats.
{ECO:0000250}.
-!- DISEASE: Ataxia, combined cerebellar and peripheral, with hearing
loss and diabetes mellitus (ACPHD) [MIM:616192]: A disease
characterized by juvenile-onset diabetes and neurodegeneration,
resulting in ataxia, upper-motor-neuron damage, peripheral
neuropathy, hearing loss, and cerebral atrophy.
{ECO:0000269|PubMed:25466870}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/dnajc3/";
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EMBL; U28424; AAC50502.1; -; mRNA.
EMBL; AY795482; AAV40838.1; -; Genomic_DNA.
EMBL; AL138955; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC047936; AAH47936.2; -; mRNA.
CCDS; CCDS9479.1; -.
PIR; JC4775; JC4775.
RefSeq; NP_006251.1; NM_006260.4.
UniGene; Hs.59214; -.
PDB; 2Y4T; X-ray; 3.00 A; A/B/C=35-461.
PDB; 2Y4U; X-ray; 3.20 A; A=35-461.
PDBsum; 2Y4T; -.
PDBsum; 2Y4U; -.
ProteinModelPortal; Q13217; -.
SMR; Q13217; -.
BioGrid; 111597; 27.
CORUM; Q13217; -.
IntAct; Q13217; 5.
MINT; MINT-1531270; -.
STRING; 9606.ENSP00000365991; -.
iPTMnet; Q13217; -.
PhosphoSitePlus; Q13217; -.
BioMuta; DNAJC3; -.
DMDM; 73620807; -.
EPD; Q13217; -.
MaxQB; Q13217; -.
PaxDb; Q13217; -.
PeptideAtlas; Q13217; -.
PRIDE; Q13217; -.
Ensembl; ENST00000602402; ENSP00000473631; ENSG00000102580.
GeneID; 5611; -.
KEGG; hsa:5611; -.
UCSC; uc001vmq.3; human.
CTD; 5611; -.
DisGeNET; 5611; -.
EuPathDB; HostDB:ENSG00000102580.14; -.
GeneCards; DNAJC3; -.
HGNC; HGNC:9439; DNAJC3.
HPA; HPA039336; -.
HPA; HPA041326; -.
MalaCards; DNAJC3; -.
MIM; 601184; gene.
MIM; 616192; phenotype.
neXtProt; NX_Q13217; -.
OpenTargets; ENSG00000102580; -.
PharmGKB; PA27420; -.
eggNOG; KOG0624; Eukaryota.
eggNOG; COG0484; LUCA.
GeneTree; ENSGT00890000139418; -.
HOGENOM; HOG000193351; -.
HOVERGEN; HBG053820; -.
InParanoid; Q13217; -.
KO; K09523; -.
OMA; GAECGVN; -.
OrthoDB; EOG091G0783; -.
PhylomeDB; Q13217; -.
TreeFam; TF105162; -.
Reactome; R-HSA-192823; Viral mRNA Translation.
Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
SIGNOR; Q13217; -.
ChiTaRS; DNAJC3; human.
GeneWiki; DNAJC3; -.
GenomeRNAi; 5611; -.
PRO; PR:Q13217; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000102580; -.
CleanEx; HS_DNAJC3; -.
ExpressionAtlas; Q13217; baseline and differential.
Genevisible; Q13217; HS.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0031205; C:endoplasmic reticulum Sec complex; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1903561; C:extracellular vesicle; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005790; C:smooth endoplasmic reticulum; IEA:Ensembl.
GO; GO:0051087; F:chaperone binding; IEA:Ensembl.
GO; GO:0051787; F:misfolded protein binding; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
GO; GO:0004860; F:protein kinase inhibitor activity; ISS:UniProtKB.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0070417; P:cellular response to cold; ISS:UniProtKB.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO; GO:0036498; P:IRE1-mediated unfolded protein response; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:ParkinsonsUK-UCL.
GO; GO:1903912; P:negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation; IMP:ParkinsonsUK-UCL.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0036494; P:positive regulation of translation initiation in response to endoplasmic reticulum stress; ISS:UniProtKB.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IEA:Ensembl.
CDD; cd06257; DnaJ; 1.
Gene3D; 1.10.287.110; -; 1.
Gene3D; 1.25.40.10; -; 5.
InterPro; IPR036869; DnaJ_dom_sf.
InterPro; IPR001623; DnaJ_domain.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom.
InterPro; IPR018704; TPR_21.
InterPro; IPR019734; TPR_repeat.
Pfam; PF00226; DnaJ; 1.
Pfam; PF09976; TPR_21; 1.
Pfam; PF13181; TPR_8; 1.
PRINTS; PR00625; JDOMAIN.
SMART; SM00271; DnaJ; 1.
SMART; SM00028; TPR; 7.
SUPFAM; SSF46565; SSF46565; 1.
SUPFAM; SSF48452; SSF48452; 2.
PROSITE; PS50076; DNAJ_2; 1.
PROSITE; PS50005; TPR; 8.
PROSITE; PS50293; TPR_REGION; 1.
1: Evidence at protein level;
3D-structure; Antiviral defense; Chaperone; Complete proteome;
Deafness; Diabetes mellitus; Disulfide bond; Endoplasmic reticulum;
Neurodegeneration; Neuropathy; Phosphoprotein; Reference proteome;
Repeat; Repressor; Signal; Stress response; TPR repeat;
Translation regulation; Unfolded protein response.
SIGNAL 1 31 {ECO:0000255}.
CHAIN 32 504 DnaJ homolog subfamily C member 3.
/FTId=PRO_0000071045.
REPEAT 37 70 TPR 1.
REPEAT 72 104 TPR 2.
REPEAT 105 138 TPR 3.
REPEAT 154 187 TPR 4.
REPEAT 189 221 TPR 5.
REPEAT 222 255 TPR 6.
REPEAT 268 301 TPR 7.
REPEAT 306 339 TPR 8.
REPEAT 340 373 TPR 9.
DOMAIN 394 462 J. {ECO:0000255|PROSITE-
ProRule:PRU00286}.
REGION 375 393 Flexible linker.
MOD_RES 274 274 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
DISULFID 248 258 {ECO:0000269|PubMed:21799829}.
DISULFID 313 329 {ECO:0000269|PubMed:21799829}.
HELIX 35 49 {ECO:0000244|PDB:2Y4T}.
HELIX 53 66 {ECO:0000244|PDB:2Y4T}.
HELIX 71 83 {ECO:0000244|PDB:2Y4T}.
HELIX 87 100 {ECO:0000244|PDB:2Y4T}.
TURN 101 103 {ECO:0000244|PDB:2Y4U}.
HELIX 105 117 {ECO:0000244|PDB:2Y4T}.
HELIX 121 132 {ECO:0000244|PDB:2Y4T}.
HELIX 138 167 {ECO:0000244|PDB:2Y4T}.
HELIX 170 183 {ECO:0000244|PDB:2Y4T}.
HELIX 188 200 {ECO:0000244|PDB:2Y4T}.
HELIX 204 207 {ECO:0000244|PDB:2Y4T}.
HELIX 208 218 {ECO:0000244|PDB:2Y4T}.
HELIX 222 234 {ECO:0000244|PDB:2Y4T}.
HELIX 238 251 {ECO:0000244|PDB:2Y4T}.
HELIX 256 281 {ECO:0000244|PDB:2Y4T}.
HELIX 284 297 {ECO:0000244|PDB:2Y4T}.
HELIX 302 317 {ECO:0000244|PDB:2Y4T}.
TURN 318 320 {ECO:0000244|PDB:2Y4T}.
HELIX 322 335 {ECO:0000244|PDB:2Y4T}.
HELIX 340 352 {ECO:0000244|PDB:2Y4T}.
HELIX 356 367 {ECO:0000244|PDB:2Y4T}.
STRAND 370 372 {ECO:0000244|PDB:2Y4T}.
HELIX 374 391 {ECO:0000244|PDB:2Y4T}.
HELIX 396 398 {ECO:0000244|PDB:2Y4T}.
HELIX 409 420 {ECO:0000244|PDB:2Y4T}.
HELIX 423 425 {ECO:0000244|PDB:2Y4T}.
HELIX 429 448 {ECO:0000244|PDB:2Y4T}.
HELIX 451 454 {ECO:0000244|PDB:2Y4T}.
SEQUENCE 504 AA; 57580 MW; E720A1E7F618B912 CRC64;
MVAPGSVTSR LGSVFPFLLV LVDLQYEGAE CGVNADVEKH LELGKKLLAA GQLADALSQF
HAAVDGDPDN YIAYYRRATV FLAMGKSKAA LPDLTKVIQL KMDFTAARLQ RGHLLLKQGK
LDEAEDDFKK VLKSNPSENE EKEAQSQLIK SDEMQRLRSQ ALNAFGSGDY TAAIAFLDKI
LEVCVWDAEL RELRAECFIK EGEPRKAISD LKAASKLKND NTEAFYKIST LYYQLGDHEL
SLSEVRECLK LDQDHKRCFA HYKQVKKLNK LIESAEELIR DGRYTDATSK YESVMKTEPS
IAEYTVRSKE RICHCFSKDE KPVEAIRVCS EVLQMEPDNV NALKDRAEAY LIEEMYDEAI
QDYETAQEHN ENDQQIREGL EKAQRLLKQS QKRDYYKILG VKRNAKKQEI IKAYRKLALQ
WHPDNFQNEE EKKKAEKKFI DIAAAKEVLS DPEMRKKFDD GEDPLDAESQ QGGGGNPFHR
SWNSWQGFNP FSSGGPFRFK FHFN


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CSB-EL007511HU Human Interferon-induced, double-stranded RNA-activated protein kinase(EIF2AK2) ELISA kit 96T
PRL PRKRIR Gene protein-kinase, interferon-inducible double stranded RNA dependent inhibitor, repressor of (P58 repressor)
CSB-EL007511MO Mouse Interferon-induced, double-stranded RNA-activated protein kinase(EIF2AK2) ELISA kit SpeciesMouse 96T
AVARP09033_P050 Anti-Interferon-induced, double-stranded RNA-activated protein kinase (EIF2AK2) Species_Reactivity: Human
CSB-EL007511HU Human Interferon-induced, double-stranded RNA-activated protein kinase(EIF2AK2) ELISA kit SpeciesHuman 96T


 

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