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Single-strand selective monofunctional uracil DNA glycosylase (EC 3.2.2.-)

 SMUG1_HUMAN             Reviewed;         270 AA.
Q53HV7; A8K2K9; O95862; Q0D2M0; Q8NB71; Q9BWC8;
16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
25-OCT-2017, entry version 111.
RecName: Full=Single-strand selective monofunctional uracil DNA glycosylase;
EC=3.2.2.-;
Name=SMUG1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR
LOCATION.
TISSUE=Ovary;
PubMed=10074426; DOI=10.1016/S0960-9822(99)80087-6;
Haushalter K.A., Stukenberg P.T., Kirschner M.W., Verdine G.L.;
"Identification of a new uracil-DNA glycosylase family by expression
cloning using synthetic inhibitors.";
Curr. Biol. 9:174-185(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
TISSUE=Liver;
PubMed=12718543; DOI=10.1021/bi0273213;
Masaoka A., Matsubara M., Hasegawa R., Tanaka T., Kurisu S.,
Terato H., Ohyama Y., Karino N., Matsuda A., Ide H.;
"Mammalian 5-formyluracil-DNA glycosylase. 2. Role of SMUG1 uracil-DNA
glycosylase in repair of 5-formyluracil and other oxidized and
deaminated base lesions.";
Biochemistry 42:5003-5012(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Colon;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Adipose tissue;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-15 AND TRP-105.
NIEHS SNPs program;
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Muscle, and Uterus;
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).
[8]
PROTEIN SEQUENCE OF 13-21; 26-37; 46-66; 79-105; 124-140; 141-146;
147-157; 188-200; 201-208; 224-243 AND 259-270, FUNCTION, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=11526119; DOI=10.1074/jbc.M106953200;
Boorstein R.J., Cummings A. Jr., Marenstein D.R., Chan M.K., Ma Y.,
Neubert T.A., Brown S.M., Teebor G.W.;
"Definitive identification of mammalian 5-hydroxymethyluracil DNA N-
glycosylase activity as SMUG1.";
J. Biol. Chem. 276:41991-41997(2001).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12161446; DOI=10.1074/jbc.M207107200;
Kavli B., Sundheim O., Akbari M., Otterlei M., Nilsen H., Skorpen F.,
Aas P.A., Hagen L., Krokan H.E., Slupphaug G.;
"hUNG2 is the major repair enzyme for removal of uracil from U:A
matches, U:G mismatches, and U in single-stranded DNA, with hSMUG1 as
a broad specificity backup.";
J. Biol. Chem. 277:39926-39936(2002).
[10]
MUTAGENESIS OF ASN-85; GLY-87; PHE-89; GLY-90; MET-91; PHE-98; ASN-163
AND HIS-239.
PubMed=15466595; DOI=10.1093/nar/gkh859;
Matsubara M., Tanaka T., Terato H., Ohmae E., Izumi S., Katayanagi K.,
Ide H.;
"Mutational analysis of the damage-recognition and catalytic mechanism
of human SMUG1 DNA glycosylase.";
Nucleic Acids Res. 32:5291-5302(2004).
-!- FUNCTION: Recognizes base lesions in the genome and initiates base
excision DNA repair. Acts as a monofunctional DNA glycosylase
specific for uracil (U) residues in DNA with a preference for
single-stranded DNA substrates. The activity is greater toward
mismatches (U/G) compared to matches (U/A). Excises uracil (U), 5-
formyluracil (fU) and uracil derivatives bearing an oxidized group
at C5 [5-hydroxyuracil (hoU) and 5-hydroxymethyluracil (hmU)] in
ssDNA and dsDNA, but not analogous cytosine derivatives (5-
hydroxycytosine and 5-formylcytosine), nor other oxidized bases.
The activity is damage-specific and salt-dependent. The substrate
preference is the following: ssDNA > dsDNA (G pair) = dsDNA (A
pair) at low salt concentration, and dsDNA (G pair) > dsDNA (A
pair) > ssDNA at high salt concentration.
{ECO:0000269|PubMed:10074426, ECO:0000269|PubMed:11526119,
ECO:0000269|PubMed:12161446, ECO:0000269|PubMed:12718543}.
-!- INTERACTION:
Q52LG2:KRTAP13-2; NbExp=4; IntAct=EBI-12275818, EBI-11953846;
O75360:PROP1; NbExp=4; IntAct=EBI-12275818, EBI-9027467;
Q93062:RBPMS; NbExp=2; IntAct=EBI-749970, EBI-740322;
Q93062-3:RBPMS; NbExp=4; IntAct=EBI-12275818, EBI-740343;
Q08AM6:VAC14; NbExp=3; IntAct=EBI-749970, EBI-2107455;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10074426,
ECO:0000269|PubMed:12161446}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q53HV7-1; Sequence=Displayed;
Name=2;
IsoId=Q53HV7-2; Sequence=VSP_015150, VSP_015151;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG)
superfamily. SMUG1 family.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/smug1/";
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EMBL; AF125182; AAD17301.1; -; mRNA.
EMBL; AK001235; BAA91571.1; -; mRNA.
EMBL; AK091468; BAC03670.1; -; mRNA.
EMBL; AK222473; BAD96193.1; -; mRNA.
EMBL; AK290274; BAF82963.1; -; mRNA.
EMBL; AF489699; AAL86910.1; -; Genomic_DNA.
EMBL; CH471054; EAW96752.1; -; Genomic_DNA.
EMBL; CH471054; EAW96756.1; -; Genomic_DNA.
EMBL; BC000417; AAH00417.1; -; mRNA.
EMBL; BC088352; AAH88352.1; -; mRNA.
EMBL; BC105607; AAI05608.1; -; mRNA.
CCDS; CCDS58239.1; -. [Q53HV7-2]
CCDS; CCDS8874.1; -. [Q53HV7-1]
RefSeq; NP_001230716.1; NM_001243787.1. [Q53HV7-1]
RefSeq; NP_001230717.1; NM_001243788.1. [Q53HV7-1]
RefSeq; NP_001230718.1; NM_001243789.1. [Q53HV7-2]
RefSeq; NP_001230719.1; NM_001243790.1. [Q53HV7-2]
RefSeq; NP_001230720.1; NM_001243791.1. [Q53HV7-2]
RefSeq; NP_055126.1; NM_014311.2. [Q53HV7-1]
RefSeq; XP_006719382.1; XM_006719319.3. [Q53HV7-1]
RefSeq; XP_006719383.1; XM_006719320.3.
RefSeq; XP_006719384.1; XM_006719321.3.
RefSeq; XP_006719385.1; XM_006719322.3.
RefSeq; XP_011536411.1; XM_011538109.2. [Q53HV7-1]
RefSeq; XP_011536412.1; XM_011538110.2.
RefSeq; XP_011536413.1; XM_011538111.2.
RefSeq; XP_011536414.1; XM_011538112.2. [Q53HV7-1]
RefSeq; XP_011536415.1; XM_011538113.2.
RefSeq; XP_011536416.1; XM_011538114.2.
RefSeq; XP_011536417.1; XM_011538115.2.
RefSeq; XP_011536418.1; XM_011538116.2. [Q53HV7-1]
RefSeq; XP_011536419.1; XM_011538117.2.
RefSeq; XP_011536420.1; XM_011538118.2. [Q53HV7-1]
RefSeq; XP_011536421.1; XM_011538119.2. [Q53HV7-1]
RefSeq; XP_011536422.1; XM_011538120.2.
RefSeq; XP_011536423.1; XM_011538121.2. [Q53HV7-1]
RefSeq; XP_011536424.1; XM_011538122.2. [Q53HV7-2]
RefSeq; XP_016874602.1; XM_017019113.1.
RefSeq; XP_016874603.1; XM_017019114.1. [Q53HV7-1]
RefSeq; XP_016874604.1; XM_017019115.1.
RefSeq; XP_016874605.1; XM_017019116.1.
RefSeq; XP_016874606.1; XM_017019117.1.
RefSeq; XP_016874607.1; XM_017019118.1.
RefSeq; XP_016874608.1; XM_017019119.1. [Q53HV7-2]
RefSeq; XP_016874609.1; XM_017019120.1.
UniGene; Hs.632721; -.
UniGene; Hs.731659; -.
ProteinModelPortal; Q53HV7; -.
SMR; Q53HV7; -.
BioGrid; 117118; 5.
IntAct; Q53HV7; 35.
MINT; MINT-6631537; -.
STRING; 9606.ENSP00000338606; -.
PhosphoSitePlus; Q53HV7; -.
BioMuta; SMUG1; -.
EPD; Q53HV7; -.
MaxQB; Q53HV7; -.
PaxDb; Q53HV7; -.
PeptideAtlas; Q53HV7; -.
PRIDE; Q53HV7; -.
TopDownProteomics; Q53HV7-2; -. [Q53HV7-2]
Ensembl; ENST00000243112; ENSP00000243112; ENSG00000123415. [Q53HV7-2]
Ensembl; ENST00000337581; ENSP00000338606; ENSG00000123415. [Q53HV7-1]
Ensembl; ENST00000401977; ENSP00000384828; ENSG00000123415. [Q53HV7-1]
Ensembl; ENST00000506595; ENSP00000421206; ENSG00000123415. [Q53HV7-2]
Ensembl; ENST00000508394; ENSP00000424191; ENSG00000123415. [Q53HV7-1]
Ensembl; ENST00000513838; ENSP00000423629; ENSG00000123415. [Q53HV7-2]
Ensembl; ENST00000514685; ENSP00000421139; ENSG00000123415. [Q53HV7-2]
GeneID; 23583; -.
KEGG; hsa:23583; -.
UCSC; uc001sfb.5; human. [Q53HV7-1]
CTD; 23583; -.
DisGeNET; 23583; -.
EuPathDB; HostDB:ENSG00000123415.15; -.
GeneCards; SMUG1; -.
H-InvDB; HIX0010683; -.
HGNC; HGNC:17148; SMUG1.
HPA; HPA051149; -.
HPA; HPA071486; -.
MIM; 607753; gene.
neXtProt; NX_Q53HV7; -.
OpenTargets; ENSG00000123415; -.
PharmGKB; PA142670895; -.
eggNOG; ENOG410IFBA; Eukaryota.
eggNOG; ENOG410XQUR; LUCA.
GeneTree; ENSGT00390000004897; -.
HOGENOM; HOG000220288; -.
HOVERGEN; HBG084399; -.
InParanoid; Q53HV7; -.
KO; K10800; -.
OMA; RFWGFFR; -.
OrthoDB; EOG091G0R85; -.
PhylomeDB; Q53HV7; -.
TreeFam; TF324356; -.
BRENDA; 3.2.2.27; 2681.
Reactome; R-HSA-110328; Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
Reactome; R-HSA-110329; Cleavage of the damaged pyrimidine.
Reactome; R-HSA-110357; Displacement of DNA glycosylase by APEX1.
GeneWiki; SMUG1; -.
GenomeRNAi; 23583; -.
PRO; PR:Q53HV7; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000123415; -.
CleanEx; HS_SMUG1; -.
ExpressionAtlas; Q53HV7; baseline and differential.
Genevisible; Q53HV7; HS.
GO; GO:0005730; C:nucleolus; IDA:HGNC.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0019104; F:DNA N-glycosylase activity; IDA:HGNC.
GO; GO:0000703; F:oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity; IBA:GO_Central.
GO; GO:0017065; F:single-strand selective uracil DNA N-glycosylase activity; IDA:HGNC.
GO; GO:0004844; F:uracil DNA N-glycosylase activity; IDA:HGNC.
GO; GO:0006284; P:base-excision repair; IDA:HGNC.
GO; GO:0045008; P:depyrimidination; TAS:Reactome.
Gene3D; 3.40.470.10; -; 1.
InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
SUPFAM; SSF52141; SSF52141; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Direct protein sequencing;
DNA damage; DNA repair; DNA-binding; Hydrolase; Nucleus; Polymorphism;
Reference proteome.
CHAIN 1 270 Single-strand selective monofunctional
uracil DNA glycosylase.
/FTId=PRO_0000071992.
REGION 173 187 DNA binding. {ECO:0000250}.
BINDING 84 84 Substrate; via amide nitrogen.
{ECO:0000250}.
BINDING 98 98 Substrate; via amide nitrogen.
BINDING 163 163 Substrate.
BINDING 239 239 Substrate.
VAR_SEQ 136 177 VSGARFWGFFRNLCGQPEVFFHHCFVHNLCPLLFLAPSGRN
L -> GPRQSMGHEIKSELLMGGCSWIRGKIQCDRVQVRRP
GFSSQL (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_015150.
VAR_SEQ 178 270 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_015151.
VARIANT 15 15 G -> V (in dbSNP:rs2233920).
{ECO:0000269|Ref.5}.
/FTId=VAR_023243.
VARIANT 105 105 R -> W (in dbSNP:rs3136389).
{ECO:0000269|Ref.5}.
/FTId=VAR_023244.
MUTAGEN 85 85 N->A: Markedly impaired damage-excising
activity for U/G, hoU/G, hmU/A and fU/A.
No cytosine-excising activity for C/G,
C/A, C/T and C/C.
{ECO:0000269|PubMed:15466595}.
MUTAGEN 87 87 G->A,S: Impaired the damage-excising
activity for U/G, hoU/G, hmU/A and fU/A.
{ECO:0000269|PubMed:15466595}.
MUTAGEN 87 87 G->F: Loss of damage-excising activity.
{ECO:0000269|PubMed:15466595}.
MUTAGEN 89 89 F->A,G,S: No effect on damage-excising
activity for U/G, hoU/G, hmU/A and fU/A.
{ECO:0000269|PubMed:15466595}.
MUTAGEN 90 90 G->A: Loss of damage-excising activity
for U/G. Weak, but significant activity
toward hoU/G, hmU/A and fU/A.
{ECO:0000269|PubMed:15466595}.
MUTAGEN 91 91 M->A: No effect on damage-excising
activity for U/G, hoU/G, hmU/A and fU/A.
{ECO:0000269|PubMed:15466595}.
MUTAGEN 98 98 F->L: Impaired the damage-excising
activity for U/G, hoU/G, hmU/A and fU/A.
{ECO:0000269|PubMed:15466595}.
MUTAGEN 163 163 N->D: Impaired the damage-excising
activity for U/G, hoU/G, hmU/A and fU/A.
No cytosine-excising activity for C/G,
C/A, C/T and C/C. hoC-excising activity
for hoC/A, hoC/T and hoC/C.
{ECO:0000269|PubMed:15466595}.
MUTAGEN 239 239 H->L,N: Markedly impaired the damage-
excising activity for U/G, hoU/G, hmU/A
and fU/A. {ECO:0000269|PubMed:15466595}.
CONFLICT 30 30 S -> G (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 48 48 S -> L (in Ref. 3; BAC03670).
{ECO:0000305}.
CONFLICT 50 50 P -> I (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 54 54 I -> V (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 66 174 Missing (in Ref. 3; BAC03670).
{ECO:0000305}.
CONFLICT 70 70 T -> I (in Ref. 4; BAD96193).
{ECO:0000305}.
CONFLICT 103 103 M -> V (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 157 157 H -> R (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 193 193 I -> V (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 227 227 G -> S (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 259 260 LN -> NL (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 269 270 LK -> TS (in Ref. 8; AA sequence).
{ECO:0000305}.
SEQUENCE 270 AA; 29862 MW; 2AB18F6F757F6DD7 CRC64;
MPQAFLLGSI HEPAGALMEP QPCPGSLAES FLEEELRLNA ELSQLQFSEP VGIIYNPVEY
AWEPHRNYVT RYCQGPKEVL FLGMNPGPFG MAQTGVPFGE VSMVRDWLGI VGPVLTPPQE
HPKRPVLGLE CPQSEVSGAR FWGFFRNLCG QPEVFFHHCF VHNLCPLLFL APSGRNLTPA
ELPAKQREQL LGICDAALCR QVQLLGVRLV VGVGRLAEQR ARRALAGLMP EVQVEGLLHP
SPRNPQANKG WEAVAKERLN ELGLLPLLLK


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GENTAUR France SARL
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Tel 01 43 25 01 50

Fax 01 43 25 01 60
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BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

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GENTAUR GmbH
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Support Karolina Elandt
Tel: 0035929830070
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San Jose, CA 95123
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Tel (408) 780-0908,
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Genprice Inc, Invoices and accounting
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GENTAUR Poland Sp. z o.o.


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