ID MUT7_DROME Reviewed; 625 AA.
AC Q9VIF1; Q8MSZ9;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 164.
DE RecName: Full=Exonuclease mut-7 homolog;
DE EC=3.1.-.-;
DE AltName: Full=Exonuclease 3'-5' domain-containing protein 3 homolog;
DE AltName: Full=Protein nibbler;
GN Name=Nbr; ORFNames=CG9247;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Ovary;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, COFACTOR, AND MUTAGENESIS OF
RP 435-ASP--GLU-437.
RX PubMed=22055293; DOI=10.1016/j.cub.2011.09.034;
RA Han B.W., Hung J.H., Weng Z., Zamore P.D., Ameres S.L.;
RT "The 3'-to-5' exoribonuclease Nibbler shapes the 3' ends of microRNAs bound
RT to Drosophila Argonaute1.";
RL Curr. Biol. 21:1878-1887(2011).
RN [6]
RP FUNCTION, INTERACTION WITH AGO1, AND DISRUPTION PHENOTYPE.
RX PubMed=22055292; DOI=10.1016/j.cub.2011.10.006;
RA Liu N., Abe M., Sabin L.R., Hendriks G.J., Naqvi A.S., Yu Z., Cherry S.,
RA Bonini N.M.;
RT "The exoribonuclease Nibbler controls 3' end processing of microRNAs in
RT Drosophila.";
RL Curr. Biol. 21:1888-1893(2011).
CC -!- FUNCTION: Possesses 3'-5' exoribonuclease activity. Required for 3'-end
CC trimming of AGO1-bound miRNAs, in particular multiple-isoform miRNAs,
CC which represents a critical step in miRNA maturation.
CC {ECO:0000269|PubMed:22055292, ECO:0000269|PubMed:22055293}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:22055293};
CC -!- SUBUNIT: Interacts with AGO1; the interaction is not RNA dependent.
CC {ECO:0000269|PubMed:22055292}.
CC -!- DISRUPTION PHENOTYPE: Homozygous semilethal and sterile. Mutant flies
CC show accumulation of the longest isoforms of multiple-isoform miRNAs
CC including miR-3 and miR-34. {ECO:0000269|PubMed:22055292,
CC ECO:0000269|PubMed:22055293}.
CC -!- SIMILARITY: Belongs to the mut-7 family. {ECO:0000305}.
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DR EMBL; AE014134; AAF53970.1; -; Genomic_DNA.
DR EMBL; AY118462; AAM49831.1; -; mRNA.
DR RefSeq; NP_610094.1; NM_136250.4.
DR PDB; 7JW6; X-ray; 1.50 A; A=395-625.
DR PDBsum; 7JW6; -.
DR AlphaFoldDB; Q9VIF1; -.
DR SMR; Q9VIF1; -.
DR BioGRID; 61340; 5.
DR IntAct; Q9VIF1; 4.
DR STRING; 7227.FBpp0081027; -.
DR iPTMnet; Q9VIF1; -.
DR PaxDb; 7227-FBpp0081027; -.
DR DNASU; 35385; -.
DR EnsemblMetazoa; FBtr0081499; FBpp0081027; FBgn0032924.
DR GeneID; 35385; -.
DR KEGG; dme:Dmel_CG9247; -.
DR UCSC; CG9247-RA; d. melanogaster.
DR AGR; FB:FBgn0032924; -.
DR CTD; 35385; -.
DR FlyBase; FBgn0032924; Nbr.
DR VEuPathDB; VectorBase:FBgn0032924; -.
DR eggNOG; KOG2207; Eukaryota.
DR GeneTree; ENSGT00390000006843; -.
DR HOGENOM; CLU_437604_0_0_1; -.
DR InParanoid; Q9VIF1; -.
DR OMA; SSKLRMC; -.
DR OrthoDB; 52347at2759; -.
DR PhylomeDB; Q9VIF1; -.
DR BioGRID-ORCS; 35385; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 35385; -.
DR PRO; PR:Q9VIF1; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0032924; Expressed in adult abdomen and 21 other cell types or tissues.
DR ExpressionAtlas; Q9VIF1; baseline and differential.
DR Genevisible; Q9VIF1; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043186; C:P granule; IDA:FlyBase.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:FlyBase.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IBA:GO_Central.
DR GO; GO:0044748; F:3'-5'-exoribonuclease activity involved in mature miRNA 3'-end processing; IMP:FlyBase.
DR GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IMP:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0035196; P:miRNA processing; IMP:FlyBase.
DR GO; GO:0034587; P:piRNA processing; IMP:FlyBase.
DR GO; GO:0044747; P:pre-miRNA 3'-end processing; IMP:FlyBase.
DR GO; GO:0140990; P:primary piRNA processing; IMP:FlyBase.
DR GO; GO:0010526; P:retrotransposon silencing; IMP:FlyBase.
DR GO; GO:0140965; P:secondary piRNA processing; IMP:FlyBase.
DR CDD; cd06146; mut-7_like_exo; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR InterPro; IPR037432; Mut-7_DEDDy_dom.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR47765; 3'-5' EXONUCLEASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47765:SF2; EXONUCLEASE MUT-7 HOMOLOG; 1.
DR Pfam; PF01612; DNA_pol_A_exo1; 1.
DR SMART; SM00474; 35EXOc; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Exonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..625
FT /note="Exonuclease mut-7 homolog"
FT /id="PRO_0000319061"
FT DOMAIN 410..602
FT /note="3'-5' exonuclease"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 435..437
FT /note="DSE->ASA: Reduces miR-34 trimming."
FT /evidence="ECO:0000269|PubMed:22055293"
FT CONFLICT 136
FT /note="C -> S (in Ref. 3; AAM49831)"
FT /evidence="ECO:0000305"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:7JW6"
FT STRAND 410..413
FT /evidence="ECO:0007829|PDB:7JW6"
FT HELIX 416..426
FT /evidence="ECO:0007829|PDB:7JW6"
FT STRAND 430..439
FT /evidence="ECO:0007829|PDB:7JW6"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:7JW6"
FT STRAND 447..454
FT /evidence="ECO:0007829|PDB:7JW6"
FT STRAND 459..463
FT /evidence="ECO:0007829|PDB:7JW6"
FT TURN 467..469
FT /evidence="ECO:0007829|PDB:7JW6"
FT HELIX 472..481
FT /evidence="ECO:0007829|PDB:7JW6"
FT TURN 482..484
FT /evidence="ECO:0007829|PDB:7JW6"
FT STRAND 488..494
FT /evidence="ECO:0007829|PDB:7JW6"
FT HELIX 495..505
FT /evidence="ECO:0007829|PDB:7JW6"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:7JW6"
FT HELIX 521..528
FT /evidence="ECO:0007829|PDB:7JW6"
FT HELIX 542..544
FT /evidence="ECO:0007829|PDB:7JW6"
FT HELIX 549..557
FT /evidence="ECO:0007829|PDB:7JW6"
FT TURN 564..567
FT /evidence="ECO:0007829|PDB:7JW6"
FT HELIX 577..600
FT /evidence="ECO:0007829|PDB:7JW6"
FT HELIX 604..614
FT /evidence="ECO:0007829|PDB:7JW6"
FT STRAND 617..619
FT /evidence="ECO:0007829|PDB:7JW6"
SQ 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
//
