Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Exonuclease mut-7 homolog (EC 3.1.-.-) (Exonuclease 3'-5' domain-containing protein 3 homolog) (Protein nibbler)

 MUT7_DROME              Reviewed;         625 AA.
Q9VIF1; Q8MSZ9;
26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
12-SEP-2018, entry version 141.
RecName: Full=Exonuclease mut-7 homolog;
EC=3.1.-.-;
AltName: Full=Exonuclease 3'-5' domain-containing protein 3 homolog;
AltName: Full=Protein nibbler;
Name=Nbr; ORFNames=CG9247;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
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).
[2]
GENOME REANNOTATION.
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Ovary;
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).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION
BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
[5]
FUNCTION, DISRUPTION PHENOTYPE, COFACTOR, AND MUTAGENESIS OF
435-ASP--GLU-437.
PubMed=22055293; DOI=10.1016/j.cub.2011.09.034;
Han B.W., Hung J.H., Weng Z., Zamore P.D., Ameres S.L.;
"The 3'-to-5' exoribonuclease Nibbler shapes the 3' ends of microRNAs
bound to Drosophila Argonaute1.";
Curr. Biol. 21:1878-1887(2011).
[6]
FUNCTION, INTERACTION WITH AGO1, AND DISRUPTION PHENOTYPE.
PubMed=22055292; DOI=10.1016/j.cub.2011.10.006;
Liu N., Abe M., Sabin L.R., Hendriks G.J., Naqvi A.S., Yu Z.,
Cherry S., Bonini N.M.;
"The exoribonuclease Nibbler controls 3' end processing of microRNAs
in Drosophila.";
Curr. Biol. 21:1888-1893(2011).
-!- FUNCTION: Possesses 3'-5' exoribonuclease activity. Required for
3'-end trimming of AGO1-bound miRNAs, in particular multiple-
isoform miRNAs, which represents a critical step in miRNA
maturation. {ECO:0000269|PubMed:22055292,
ECO:0000269|PubMed:22055293}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:22055293};
-!- SUBUNIT: Interacts with AGO1; the interaction is not RNA
dependent. {ECO:0000269|PubMed:22055292}.
-!- DISRUPTION PHENOTYPE: Homozygous semilethal and sterile. Mutant
flies show accumulation of the longest isoforms of multiple-
isoform miRNAs including miR-3 and miR-34.
{ECO:0000269|PubMed:22055292, ECO:0000269|PubMed:22055293}.
-!- SIMILARITY: Belongs to the mut-7 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AE014134; AAF53970.1; -; Genomic_DNA.
EMBL; AY118462; AAM49831.1; -; mRNA.
RefSeq; NP_610094.1; NM_136250.4.
UniGene; Dm.30864; -.
ProteinModelPortal; Q9VIF1; -.
BioGrid; 61340; 4.
IntAct; Q9VIF1; 4.
STRING; 7227.FBpp0081027; -.
iPTMnet; Q9VIF1; -.
PaxDb; Q9VIF1; -.
PRIDE; Q9VIF1; -.
EnsemblMetazoa; FBtr0081499; FBpp0081027; FBgn0032924.
GeneID; 35385; -.
KEGG; dme:Dmel_CG9247; -.
UCSC; CG9247-RA; d. melanogaster.
CTD; 35385; -.
FlyBase; FBgn0032924; Nbr.
eggNOG; KOG2207; Eukaryota.
eggNOG; ENOG410YV3M; LUCA.
GeneTree; ENSGT00390000006843; -.
InParanoid; Q9VIF1; -.
OMA; CSNWANR; -.
OrthoDB; EOG091G04KJ; -.
PhylomeDB; Q9VIF1; -.
GenomeRNAi; 35385; -.
PRO; PR:Q9VIF1; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0032924; Expressed in 28 organ(s), highest expression level in embryo.
ExpressionAtlas; Q9VIF1; baseline and differential.
Genevisible; Q9VIF1; DM.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:1990904; C:ribonucleoprotein complex; IDA:FlyBase.
GO; GO:0044748; F:3'-5'-exoribonuclease activity involved in mature miRNA 3'-end processing; IMP:FlyBase.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0044747; P:mature miRNA 3'-end processing; IMP:FlyBase.
GO; GO:0034587; P:piRNA metabolic process; IMP:FlyBase.
CDD; cd06146; mut-7_like_exo; 1.
Gene3D; 3.30.420.10; -; 1.
InterPro; IPR002562; 3'-5'_exonuclease_dom.
InterPro; IPR037432; Mut-7_DEDDy_dom.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR036397; RNaseH_sf.
Pfam; PF01612; DNA_pol_A_exo1; 1.
SMART; SM00474; 35EXOc; 1.
SUPFAM; SSF53098; SSF53098; 1.
1: Evidence at protein level;
Complete proteome; Exonuclease; Hydrolase; Magnesium; Metal-binding;
Nuclease; Phosphoprotein; Reference proteome.
CHAIN 1 625 Exonuclease mut-7 homolog.
/FTId=PRO_0000319061.
DOMAIN 410 602 3'-5' exonuclease.
MOD_RES 17 17 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MUTAGEN 435 437 DSE->ASA: Reduces miR-34 trimming.
{ECO:0000269|PubMed:22055293}.
CONFLICT 136 136 C -> S (in Ref. 3; AAM49831).
{ECO:0000305}.
SEQUENCE 625 AA; 71953 MW; B7905104CE9212CF CRC64;
MARKSHMYNA IPAGFESDEE NMENLMSNLK IKRLEDITTG AGIDGCNFDA TLDAKAEEFF
KLFREKWNMY SKKKSPHLRQ EFGRALMGHQ DPLLLALKIF ANCPDSSNIK TKSLSHFVLD
TVCKLHKDFP HLGEGCDPNT SMIAFNFVKT SGLLALNNAV IHAYSLRQIR DLLLPKLREL
LDNGLYKEVT QWSISLQLTH EFDMLELAFP LIAIEKLPLA EEYLDHATQQ RLPFVKFLDS
LLHKEKSVLE LCEHLLDRYK NLKISHNVLS YRPMAKIVAR LAKKYGFDDA VTPNYKFTKT
CSYLHYLYRE YEKTRMNLAS FREVVSVHAF NHELRTDFVK YLASAGAHSE AIYWYTEFNI
DPKDCPLEIE TQVSQNGAGK ASGWESPGKE RCPSSRCDMY LTMDLPDECL IIVNKADEFD
RMLYHLQQEC VIYLDSEWMQ SVCGDNQLCV LQIATGHNVY LIDCLARESL RSEHWRLLGA
NIFNNVNIRK VGFSMVSDLS VLQRSLPLQL RLQMPHHYLD LRNLWLELKK QRFGVELPFG
NVNRAGDALT DLSLACLGKK LNKSNQCSNW ANRPLRREQI LYAAIDARCL MLIYNTLIER
VSFIQAVIEK SIASNNFLRR GAHVK


Related products :

Catalog number Product name Quantity
EIAAB25855 EXD3,Exonuclease 3'-5' domain-containing protein 3,HBE269,Homo sapiens,Human,Probable exonuclease mut-7 homolog
18-003-43366 RNA exonuclease 4 - EC 3.1.-.-; Exonuclease XPMC2; hPMC2; Prevents mitotic catastrophe 2 protein homolog Polyclonal 0.1 mg Protein A
18-003-43097 RNA exonuclease 4 - EC 3.1.-.-; Exonuclease XPMC2; hPMC2; Prevents mitotic catastrophe 2 protein homolog Polyclonal 0.05 mg Aff Pur
EIAAB34334 Exonuclease XPMC2,Gm111,Mouse,Mus musculus,Pmc2,Prevents mitotic catastrophe 2 protein homolog,Rexo4,RNA exonuclease 4,Xpmc2h
EIAAB34333 Exonuclease XPMC2,Homo sapiens,hPMC2,Human,PMC2,Prevents mitotic catastrophe 2 protein homolog,REXO4,RNA exonuclease 4,XPMC2H
EIAAB13444 C14orf114,EXD2,EXDL2,Exonuclease 3'-5' domain-containing protein 2,Exonuclease 3'-5' domain-like-containing protein 2,Homo sapiens,Human
EIAAB13442 EXD1,EXDL1,Exonuclease 3'-5' domain-containing protein 1,Exonuclease 3'-5' domain-like-containing protein 1,Homo sapiens,Human
EIAAB13443 Exd1,Exdl1,Exonuclease 3'-5' domain-containing protein 1,Exonuclease 3'-5' domain-like-containing protein 1,Mouse,Mus musculus
EIAAB13445 Exd2,Exdl2,Exonuclease 3'-5' domain-containing protein 2,Exonuclease 3'-5' domain-like-containing protein 2,Mouse,Mus musculus
18-003-44239 Histone mRNA 3'-exonuclease 1 - EC 3.1.-.-; 3'-5' exonuclease ERI1; Eri-1 homolog; Histone mRNA 3'-end-specific exoribonuclease; Protein 3'hExo; HEXO Polyclonal 0.1 mg Protein A
EIAAB13234 3'-5' exonuclease ERI1,3'-5' exoribonuclease 1,3'exo,Eri1,Eri-1 homolog,Histone mRNA 3'-exonuclease 1,Mouse,Mus musculus,Thex1
29-513 THEX1 contains 1 SAP domain and 1 exonuclease domain. It is an RNA exonuclease that binds to the 3' end of histone mRNAs and probably degrades them, suggesting that it plays an essential role in histo 0.05 mg
29-514 THEX1 contains 1 SAP domain and 1 exonuclease domain. It is an RNA exonuclease that binds to the 3' end of histone mRNAs and probably degrades them, suggesting that it plays an essential role in histo 0.1 mg
EIAAB13233 3'-5' exonuclease ERI1,3'-5' exoribonuclease 1,3'EXO,ERI1,Eri-1 homolog,HEXO,Histone mRNA 3'-end-specific exoribonuclease,Histone mRNA 3'-exonuclease 1,Homo sapiens,Human,Protein 3'hExo,THEX1
EIAAB13449 Defects in morphology protein 1 homolog,Dem1,Exo V,Mouse,Mus musculus,Probable exonuclease V
EIAAB13451 Bos taurus,Bovine,Defects in morphology protein 1 homolog,DEM1,Exo V,Probable exonuclease V
EIAAB13450 C1orf176,Defects in morphology protein 1 homolog,DEM1,Exo V,Homo sapiens,Human,Probable exonuclease V
EIAAB10646 5' exonuclease Apollo,Dclre1b,DNA cross-link repair 1B protein,Mouse,Mus musculus,SNM1 homolog B,Snm1b
EIAAB10648 5' exonuclease Apollo,Dclre1b,DNA cross-link repair 1B protein,Rat,Rattus norvegicus,SNM1 homolog B,Snm1b
EIAAB34332 Kiaa1138,Mouse,Mus musculus,Rexo1,RNA exonuclease 1 homolog,Tceb3bp1,Transcription elongation factor B polypeptide 3-binding protein 1
EIAAB34331 ELOABP1,EloA-BP1,Elongin-A-binding protein 1,Homo sapiens,Human,KIAA1138,REXO1,RNA exonuclease 1 homolog,TCEB3BP1,Transcription elongation factor B polypeptide 3-binding protein 1
EIAAB10647 5' exonuclease Apollo,DCLRE1B,DNA cross-link repair 1B protein,Homo sapiens,hSNM1B,Human,SNM1 homolog B,SNM1B,SNMIB
EIAAB33671 Bos taurus,Bovine,Cell cycle checkpoint control protein RAD9B,DNA repair exonuclease rad9 homolog B,RAD9B
EIAAB10649 5' exonuclease Apollo,Chicken,DCLRE1B,DNA cross-link repair 1B protein,Gallus gallus,SNM1 homolog B,SNM1B
EIAAB33672 Cell cycle checkpoint control protein RAD9B,DNA repair exonuclease rad9 homolog B,Rad9b,Rat,Rattus norvegicus


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




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
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

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
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur