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Caspase-8 (EC 3.4.22.61) (Death-related ced-3/NEDD2-like protein) [Cleaved into: Caspase-8 subunit p15; Caspase-8 subunit p10]

 CASP8_DROME             Reviewed;         494 AA.
Q8IRY7; O02433; O76797; O76798; Q95T94; Q9UB42; Q9W5E3;
07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
16-JUN-2009, sequence version 3.
27-SEP-2017, entry version 134.
RecName: Full=Caspase-8;
EC=3.4.22.61;
AltName: Full=Death-related ced-3/NEDD2-like protein;
Contains:
RecName: Full=Caspase-8 subunit p15;
Contains:
RecName: Full=Caspase-8 subunit p10;
Flags: Precursor;
Name=Dredd; Synonyms=DCP2; ORFNames=CG7486;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS D; E AND ALPHA), FUNCTION,
SUBUNIT, PROTEOLYTIC CLEAVAGE, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
STAGE.
TISSUE=Embryo {ECO:0000269|PubMed:9740659};
PubMed=9740659; DOI=10.1006/dbio.1998.9000;
Chen P., Rodriguez A., Erskine R., Thach T., Abrams J.M.;
"Dredd, a novel effector of the apoptosis activators reaper, grim, and
hid in Drosophila.";
Dev. Biol. 201:202-216(1998).
[2] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3] {ECO:0000305}
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Oregon-R {ECO:0000269|PubMed:10731137};
PubMed=10731137; DOI=10.1126/science.287.5461.2220;
Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D.,
Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E.,
Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D.,
Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S.,
Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B.,
Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F.,
Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A.,
Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
Glover D.M.;
"From sequence to chromosome: the tip of the X chromosome of D.
melanogaster.";
Science 287:2220-2222(2000).
[5] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM F).
STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
TISSUE=Head {ECO:0000269|PubMed:12537569};
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] OF 25-494 (ISOFORM E).
PubMed=9380701; DOI=10.1073/pnas.94.20.10717;
Inohara N., Koseki T., Hu Y., Chen S., Nunez G.;
"CLARP, a death effector domain-containing protein interacts with
caspase-8 and regulates apoptosis.";
Proc. Natl. Acad. Sci. U.S.A. 94:10717-10722(1997).
[7] {ECO:0000305}
FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF GLY-98 AND TRP-436.
PubMed=11269502; DOI=10.1093/embo-reports/kvd073;
Leulier F., Rodriguez A., Khush R.S., Abrams J.M., Lemaitre B.;
"The Drosophila caspase Dredd is required to resist Gram-negative
bacterial infection.";
EMBO Rep. 1:353-358(2000).
[8]
FUNCTION, INTERACTION WITH FADD, AND SUBCELLULAR LOCATION.
PubMed=10934188; DOI=10.1074/jbc.C000341200;
Hu S., Yang X.;
"dFADD, a novel death domain-containing adapter protein for the
Drosophila caspase DREDD.";
J. Biol. Chem. 275:30761-30764(2000).
[9]
FUNCTION, UBIQUITINATION, MUTAGENESIS OF GLY-98, AND INTERACTION WITH
FADD AND DIAP2.
PubMed=22549468; DOI=10.1038/emboj.2012.121;
Meinander A., Runchel C., Tenev T., Chen L., Kim C.H., Ribeiro P.S.,
Broemer M., Leulier F., Zvelebil M., Silverman N., Meier P.;
"Ubiquitylation of the initiator caspase DREDD is required for innate
immune signalling.";
EMBO J. 31:2770-2783(2012).
-!- FUNCTION: Effector of the programmed cell death (PCD) activators
rpr, grim and hid (PubMed:9740659). May play an apoptotic role in
the germline as well as soma. Fadd interacts with Dredd to promote
cleavage of Dredd and is necessary and sufficient for enhancing
Dredd-induced apoptosis (PubMed:10934188). Plays a role in the
innate immune response. Required for resistance to Gram-negative
bacterial infection (PubMed:11269502). Diap2-mediated
ubiquitination of Dredd is critical for processing of imd and rel
and the subsequent expression of antimicrobial genes such as Dpt
(PubMed:22549468). {ECO:0000269|PubMed:10934188,
ECO:0000269|PubMed:11269502, ECO:0000269|PubMed:22549468,
ECO:0000269|PubMed:9740659}.
-!- CATALYTIC ACTIVITY: Strict requirement for Asp at position P1 and
has a preferred cleavage sequence of (Leu/Asp/Val)-Glu-Thr-Asp-|-
(Gly/Ser/Ala).
-!- SUBUNIT: Heterotetramer that consists of two anti-parallel
arranged heterodimers, each one formed by a 15 kDa (caspase-8
subunit p15) and a 10 kDa (caspase-8 subunit p10) subunit
(PubMed:9740659). Interacts (via N-terminus) with Diap2; likely to
bind Diap2 simultaneously with Fadd to form a trimeric complex
(PubMed:10934188, PubMed:22549468). {ECO:0000269|PubMed:10934188,
ECO:0000269|PubMed:22549468, ECO:0000269|PubMed:9740659}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10934188,
ECO:0000269|PubMed:9740659}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=E; Synonyms=Caspase-8 delta;
IsoId=Q8IRY7-1; Sequence=Displayed;
Name=D; Synonyms=Caspase-8 gamma;
IsoId=Q8IRY7-2; Sequence=VSP_050749;
Name=F;
IsoId=Q8IRY7-3; Sequence=VSP_050750, VSP_050751;
Name=alpha {ECO:0000269|PubMed:9740659};
IsoId=Q8IRY7-4; Sequence=VSP_050748;
-!- TISSUE SPECIFICITY: Constitutively expressed in fat bodies of
larvae and adults. {ECO:0000269|PubMed:11269502}.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
Embryos exhibit ubiquitous low level of expression until stage 11
and then expression becomes spatially and temporally restricted to
areas of PCD. {ECO:0000269|PubMed:9740659}.
-!- PTM: Polyubiquitinated by Diap2 following activation of the immune
deficiency (Imd) pathway. {ECO:0000269|PubMed:22549468}.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAL25314.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF007016; AAC31214.1; -; mRNA.
EMBL; AF083894; AAC33117.1; -; mRNA.
EMBL; AF083895; AAC33118.1; -; mRNA.
EMBL; AE014298; AAF45533.3; -; Genomic_DNA.
EMBL; AE014298; AAN09022.2; -; Genomic_DNA.
EMBL; AE014298; AAN09023.2; -; Genomic_DNA.
EMBL; AL031581; CAA20893.1; -; Genomic_DNA.
EMBL; AY060275; AAL25314.1; ALT_INIT; mRNA.
EMBL; AF031652; AAC15843.1; -; mRNA.
PIR; T13385; T13385.
RefSeq; NP_477249.3; NM_057901.4. [Q8IRY7-1]
RefSeq; NP_477250.3; NM_057902.4. [Q8IRY7-3]
RefSeq; NP_477251.3; NM_057903.4. [Q8IRY7-2]
ProteinModelPortal; Q8IRY7; -.
SMR; Q8IRY7; -.
BioGrid; 57579; 72.
IntAct; Q8IRY7; 12.
MINT; MINT-142252; -.
STRING; 7227.FBpp0113052; -.
MEROPS; C14.040; -.
PaxDb; Q8IRY7; -.
PRIDE; Q8IRY7; -.
EnsemblMetazoa; FBtr0114559; FBpp0113051; FBgn0020381. [Q8IRY7-2]
EnsemblMetazoa; FBtr0114560; FBpp0113052; FBgn0020381. [Q8IRY7-1]
EnsemblMetazoa; FBtr0114561; FBpp0113053; FBgn0020381. [Q8IRY7-3]
GeneID; 31011; -.
KEGG; dme:Dmel_CG7486; -.
CTD; 31011; -.
FlyBase; FBgn0020381; Dredd.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00760000118912; -.
InParanoid; Q8IRY7; -.
KO; K04398; -.
OMA; IEHLKFN; -.
OrthoDB; EOG091G0606; -.
PhylomeDB; Q8IRY7; -.
Reactome; R-DME-111465; Apoptotic cleavage of cellular proteins.
Reactome; R-DME-264870; Caspase-mediated cleavage of cytoskeletal proteins.
Reactome; R-DME-75153; Apoptotic execution phase.
GenomeRNAi; 31011; -.
PRO; PR:Q8IRY7; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0020381; -.
ExpressionAtlas; Q8IRY7; differential.
Genevisible; Q8IRY7; DM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; IMP:UniProtKB.
GO; GO:0004197; F:cysteine-type endopeptidase activity; TAS:FlyBase.
GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IBA:GO_Central.
GO; GO:0004175; F:endopeptidase activity; IDA:FlyBase.
GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
GO; GO:0006952; P:defense response; IMP:FlyBase.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
GO; GO:0097194; P:execution phase of apoptosis; IBA:GO_Central.
GO; GO:0006955; P:immune response; IMP:FlyBase.
GO; GO:0045087; P:innate immune response; TAS:FlyBase.
GO; GO:0043069; P:negative regulation of programmed cell death; IMP:FlyBase.
GO; GO:0061057; P:peptidoglycan recognition protein signaling pathway; IMP:UniProtKB.
GO; GO:0048935; P:peripheral nervous system neuron development; IMP:FlyBase.
GO; GO:0006963; P:positive regulation of antibacterial peptide biosynthetic process; TAS:FlyBase.
GO; GO:0006964; P:positive regulation of biosynthetic process of antibacterial peptides active against Gram-negative bacteria; IMP:UniProtKB.
GO; GO:0002230; P:positive regulation of defense response to virus by host; IMP:FlyBase.
GO; GO:0045089; P:positive regulation of innate immune response; IMP:FlyBase.
GO; GO:0016485; P:protein processing; IDA:FlyBase.
GO; GO:0007291; P:sperm individualization; IMP:FlyBase.
CDD; cd00032; CASc; 1.
InterPro; IPR029030; Caspase-like_dom.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
PRINTS; PR00376; IL1BCENZYME.
SMART; SM00115; CASc; 1.
SUPFAM; SSF52129; SSF52129; 1.
PROSITE; PS01122; CASPASE_CYS; 1.
PROSITE; PS50207; CASPASE_P10; 1.
PROSITE; PS50208; CASPASE_P20; 1.
1: Evidence at protein level;
Alternative splicing; Apoptosis; Complete proteome; Cytoplasm;
Hydrolase; Immunity; Innate immunity; Protease; Reference proteome;
Thiol protease; Ubl conjugation; Zymogen.
PROPEP 1 242 {ECO:0000250}.
/FTId=PRO_0000004636.
CHAIN 243 400 Caspase-8 subunit p15.
/FTId=PRO_0000004637.
PROPEP 401 410 {ECO:0000250}.
/FTId=PRO_0000004638.
CHAIN 411 494 Caspase-8 subunit p10.
/FTId=PRO_0000004639.
ACT_SITE 345 345 {ECO:0000250}.
ACT_SITE 386 386 {ECO:0000250}.
VAR_SEQ 1 128 Missing (in isoform alpha).
{ECO:0000303|PubMed:9740659}.
/FTId=VSP_050748.
VAR_SEQ 273 278 Missing (in isoform D).
{ECO:0000303|PubMed:9740659}.
/FTId=VSP_050749.
VAR_SEQ 279 284 KFLSPD -> VSSLQY (in isoform F).
{ECO:0000303|PubMed:12537569}.
/FTId=VSP_050750.
VAR_SEQ 285 494 Missing (in isoform F).
{ECO:0000303|PubMed:12537569}.
/FTId=VSP_050751.
MUTAGEN 98 98 G->R: In D44; reduces polyubiquitination
by Diap2, abolishes rel cleavage and
blocks expression of Dpt following
bacterial infection. No effect on binding
to Diap2 or Fadd, processing,
dimerization, catalytic activity or
stability. {ECO:0000269|PubMed:11269502,
ECO:0000269|PubMed:22549468}.
MUTAGEN 436 436 W->R: In L23; blocks expression of Dpt
following bacterial infection.
{ECO:0000269|PubMed:11269502}.
CONFLICT 481 481 K -> N (in Ref. 1; AAC33117/AAC33118).
{ECO:0000305}.
SEQUENCE 494 AA; 56153 MW; B9730DB3FDC58D4C CRC64;
MAGSNLLIHL DTIDQNDLIY VERDMNFAQK VGLCFLLYGD DHSDATYILQ KLLAMTRSDF
PQSDLLIKFA KSRPETWRRH LVEALCIIGA RKVLRRLGFC WQELRMHYLP HIAGITLHVH
PLLKSLYRMC EELSLVQSGR LLLDVREKVE SQQAGDPLRF YDPAYLEIFL LDWLTRRSIK
LGDINAAGSD VQLLVGHLKS NGLQAQANLL KDTIISNAPE PDAAGTAAMA VKQEIESDNQ
QSYCSTQIDA LKLTRENAGI ALIINQQKFH RNVSRDNMKF LSPDPLRRRD GTDVDKERLI
EVFSSMGYNV EAYDNVDHMG IIERIRSACD RSLVRDSLVV FILSHGFEEA VYASNSIAMK
ITDIEDLLCS YDTLYYKPKL LIIQACQEKL VHKKKPNELF RIDVTTVSPD QHIDMLRAMS
TVNGYAALRH TQTGSWFIGS LCDAIDRRSA SEHIADILTI VTNEVSKKRG SNDESMVPNV
KSTFRQHVYF PPRL


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Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
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GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
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GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
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GENTAUR U.S.A
Genprice Inc, Logistics
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
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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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e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


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81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

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GENTAUR Italy
SRL IVA IT03841300167
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Fax 02 36 00 65 94
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