MIB_DROME
ID MIB_DROME Reviewed; 1226 AA.
AC Q9VUX2; Q8MSR3;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=E3 ubiquitin-protein ligase mind-bomb;
DE EC=2.3.2.27;
DE AltName: Full=Mind bomb homolog;
DE Short=D-mib;
DE AltName: Full=RING-type E3 ubiquitin transferase mind-bomb {ECO:0000305};
GN Name=mib1; Synonyms=mind-bomb; ORFNames=CG5841;
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=Embryo;
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 FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DL AND SER, AND TISSUE
RP SPECIFICITY.
RX PubMed=15829515; DOI=10.1242/dev.01825;
RA Lai E.C., Roegiers F., Qin X., Jan Y.N., Rubin G.M.;
RT "The ubiquitin ligase Drosophila Mind bomb promotes Notch signaling by
RT regulating the localization and activity of Serrate and Delta.";
RL Development 132:2319-2332(2005).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP VAL-457.
RX PubMed=15760269; DOI=10.1371/journal.pbio.0030096;
RA Le Borgne R., Remaud S., Hamel S., Schweisguth F.;
RT "Two distinct E3 ubiquitin ligases have complementary functions in the
RT regulation of delta and serrate signaling in Drosophila.";
RL PLoS Biol. 3:688-696(2005).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of
CC Delta (Dl) and Serrate (Ser) receptors, which act as ligands of Notch
CC proteins. Positively regulates the Notch signaling by ubiquitinating
CC the intracellular domain of Dl and Ser, leading to endocytosis of Dl
CC and Ser receptors. Regulates a subset of Notch signaling events,
CC including wing margin specification, leg segmentation and vein
CC determination, that are distinct from those events requiring neuralize
CC (neur) activity. Also modulates lateral inhibition, a neur- and Dl-
CC dependent signaling event, suggesting a distinct but partially
CC complementary function with neur. {ECO:0000269|PubMed:15760269,
CC ECO:0000269|PubMed:15829515}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with intracellular domain of Dl and Ser.
CC {ECO:0000269|PubMed:15829515}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:15760269, ECO:0000269|PubMed:15829515}.
CC Note=Localizes at the apical cortex of cells.
CC -!- TISSUE SPECIFICITY: Ubiquitous in the wing imaginal disk (at protein
CC level). {ECO:0000269|PubMed:15760269, ECO:0000269|PubMed:15829515}.
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DR EMBL; AE014296; AAF49551.3; -; Genomic_DNA.
DR EMBL; AY118647; AAM50016.1; -; mRNA.
DR RefSeq; NP_648826.2; NM_140569.2.
DR AlphaFoldDB; Q9VUX2; -.
DR SMR; Q9VUX2; -.
DR BioGRID; 65061; 7.
DR IntAct; Q9VUX2; 1.
DR STRING; 7227.FBpp0075275; -.
DR PaxDb; Q9VUX2; -.
DR PRIDE; Q9VUX2; -.
DR DNASU; 39750; -.
DR EnsemblMetazoa; FBtr0075520; FBpp0075275; FBgn0263601.
DR GeneID; 39750; -.
DR KEGG; dme:Dmel_CG5841; -.
DR CTD; 57534; -.
DR FlyBase; FBgn0263601; mib1.
DR VEuPathDB; VectorBase:FBgn0263601; -.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG4582; Eukaryota.
DR GeneTree; ENSGT00940000156781; -.
DR InParanoid; Q9VUX2; -.
DR OrthoDB; 220300at2759; -.
DR PhylomeDB; Q9VUX2; -.
DR SignaLink; Q9VUX2; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 39750; 0 hits in 1 CRISPR screen.
DR ChiTaRS; mib1; fly.
DR GenomeRNAi; 39750; -.
DR PRO; PR:Q9VUX2; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0263601; Expressed in capitellum (Drosophila) and 23 other tissues.
DR ExpressionAtlas; Q9VUX2; baseline and differential.
DR Genevisible; Q9VUX2; DM.
DR GO; GO:0045179; C:apical cortex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:FlyBase.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; ISM:FlyBase.
DR GO; GO:0006897; P:endocytosis; IMP:UniProtKB.
DR GO; GO:0046331; P:lateral inhibition; IMP:FlyBase.
DR GO; GO:0007219; P:Notch signaling pathway; IBA:GO_Central.
DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:FlyBase.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IMP:UniProtKB.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:FlyBase.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; IMP:UniProtKB.
DR GO; GO:0007423; P:sensory organ development; IMP:FlyBase.
DR CDD; cd02339; ZZ_Mind_bomb; 1.
DR Gene3D; 1.25.40.20; -; 3.
DR Gene3D; 3.30.40.10; -; 3.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR042056; MIB1/2_ZZ.
DR InterPro; IPR010606; Mib_Herc2.
DR InterPro; IPR037252; Mib_Herc2_sf.
DR InterPro; IPR040847; SH3_15.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF06701; MIB_HERC2; 2.
DR Pfam; PF18346; SH3_15; 2.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 8.
DR SMART; SM00184; RING; 3.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF159034; SSF159034; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 6.
DR PROSITE; PS51416; MIB_HERC2; 2.
DR PROSITE; PS50089; ZF_RING_2; 3.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW ANK repeat; Coiled coil; Cytoplasm; Metal-binding; Notch signaling pathway;
KW Reference proteome; Repeat; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..1226
FT /note="E3 ubiquitin-protein ligase mind-bomb"
FT /id="PRO_0000055951"
FT DOMAIN 100..168
FT /note="MIB/HERC2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00749"
FT DOMAIN 237..315
FT /note="MIB/HERC2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00749"
FT REPEAT 567..596
FT /note="ANK 1"
FT REPEAT 600..629
FT /note="ANK 2"
FT REPEAT 633..662
FT /note="ANK 3"
FT REPEAT 666..695
FT /note="ANK 4"
FT REPEAT 699..731
FT /note="ANK 5"
FT REPEAT 735..765
FT /note="ANK 6"
FT REPEAT 769..798
FT /note="ANK 7"
FT REPEAT 802..833
FT /note="ANK 8"
FT ZN_FING 174..226
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT ZN_FING 970..1005
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 1017..1052
FT /note="RING-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 1183..1216
FT /note="RING-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1159..1181
FT /evidence="ECO:0000255"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..919
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MUTAGEN 457
FT /note="V->M: In D-mib4; induces defects in Notch
FT signaling."
FT /evidence="ECO:0000269|PubMed:15760269"
SQ SEQUENCE 1226 AA; 129872 MW; A6D9212DC22211B8 CRC64;
MSCAATLSSA KDSTNANASG GGGGGGGGGA PTNSNTNTNT NTQSTAVGVV VSSAAGTGVG
VGGGGGGGGS LPGGTTSSSS ASAAGGVAAG GGGNSAAALV RRFSMEGVGA RVIRGPDWKW
NKQDGGEGHV GTVRNFESAE EVVVVWDNGT AANYRCAGAY DLRILDSAPT GVKHEGTMCD
TCRQQPIFGI RWKCAECINY DLCSICYHGD KHHLRHRFYR ITTPGGERTM LEPRRKSKKV
LARGIFPGAR VVRGVDWQWE DQDGGVGRRG KVNEIQDWSS ASPRSAAYVI WDNGSKNLYR
VGFEGMADLK VVNDAKGSNV YRDHLPLLGE NGPGKGPHGF QIGDKVTVDL DLEIVQSLQH
GHGGWTDGMF ECLSNAGMVV GIDEDHDIVV AYNSGNRWTF NPAVLTKVSS PTTAPPEFQV
GDIVKICSDV ESIKILQRGH GEWADAMQLT LGKIGRVQQV YHDNDLKVEV GNTSWTYNPL
AVCKVASSTA SDGSCAPVIP SSERLSAILK KLFEPNVSGD ATEEFVKAAA NGFAARCEEY
LAGAAQPSTS SASPSSGPDV NVNGVFAGHT ALQAASQNGH IEVIQVLLRH AVDVEIEDKD
GDRAVHHAAF GDEAAVIEIL AKAGADLNAR NKRRQTSLHI AVNKGHLNVV KTLLTLGCHP
SLQDSEGDTP LHDAISKEHD EMLSLLLDFG ADITLNNNNG FNALHHAALK GNPSAMKILL
TKTNRPWIVE EKKDDGYTAL HLAALNNHVE IAELLVHMGK ANMDRQNVNL QTALHLAVER
QHVQIVKLLV QDGADLNIPD KDGDTPLHEA LRHHTLSQLK QLQDVEGFGK LLMGLRNANN
KKASASIACF LAANGADLTL KNRKQQTPLD LCPDPNLCKT LVKCYNERKT DDSELPGNVA
GTSSSARARA ASGSLNQSSS VNMPLSSLAA SSTFPAASSS SIFALNGIAN EMSQSLHEDP
PKSSASLDEC LVCSDAKRDT VFKPCGHVSC CETCAPRVKK CLICRETVSS REKIDECLVC
SDRRAAVFFR PCGHMVACEH CSALMKKCVL CRTQIDEILS FSLCCGGSGR PEKVSVAAGA
MATVGLPLPD DRFMEAAAAA ACANASGHSV AMNNTVVTPV AGSSNQLNSQ NNLLAAAAAS
SNVSNLSAAG NAMVAPSNVN NFQMDDVQKL KQQLQDIKEQ TMCPVCFDRI KNMVFLCGHG
TCQMCGDQIE GCPICRKTVE KRILLF
