MBM_DROME
ID MBM_DROME Reviewed; 539 AA.
AC Q9VPM5;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Protein mushroom body miniature {ECO:0000303|PubMed:15375215};
GN Name=mbm {ECO:0000312|FlyBase:FBgn0086912};
GN ORFNames=CG11604 {ECO:0000312|FlyBase:FBgn0086912};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|EMBL:AAL39452.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL39452.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL39452.1};
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] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=15375215; DOI=10.1073/pnas.0405887101;
RA Raabe T., Clemens-Richter S., Twardzik T., Ebert A., Gramlich G.,
RA Heisenberg M.;
RT "Identification of mushroom body miniature, a zinc-finger protein
RT implicated in brain development of Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14276-14281(2004).
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-288; SER-290;
RP THR-292; THR-327; SER-332 AND THR-333, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF SER-288; SER-290; THR-292; THR-327; SER-332 AND THR-333.
RX PubMed=24615015; DOI=10.1128/mcb.00658-13;
RA Hovhanyan A., Herter E.K., Pfannstiel J., Gallant P., Raabe T.;
RT "Drosophila mbm is a nucleolar myc and casein kinase 2 target required for
RT ribosome biogenesis and cell growth of central brain neuroblasts.";
RL Mol. Cell. Biol. 34:1878-1891(2014).
CC -!- FUNCTION: Required for small ribosomal subunit biogenesis in
CC neuroblasts (PubMed:24615015). Plays a role in mushroom body
CC development (PubMed:15375215). {ECO:0000269|PubMed:15375215,
CC ECO:0000269|PubMed:24615015}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:15375215,
CC ECO:0000269|PubMed:24615015}. Cytoplasm {ECO:0000269|PubMed:15375215,
CC ECO:0000269|PubMed:24615015}. Note=Nuclear from interphase until early
CC prophase and is then redistributed to the cytoplasm during mitosis when
CC the nucleus is disassembled. {ECO:0000269|PubMed:24615015}.
CC -!- TISSUE SPECIFICITY: Shows widespread expression in third instar larval
CC brain with no apparent difference between males and females (at protein
CC level). Detected at low levels in the mushroom body neuropil and is
CC also expressed in many cells of the brain outside the mushroom body (at
CC protein level). Not detected in third instar larval brain cells in
CC anaphase (at protein level). {ECO:0000269|PubMed:15375215}.
CC -!- DEVELOPMENTAL STAGE: Detected in male and female third instar larvae
CC with very low levels detected in adults (at protein level).
CC {ECO:0000269|PubMed:15375215}.
CC -!- PTM: May be phosphorylated in vivo by CkIIalpha. mbm and CkIIalpha
CC colocalize to the nucleolus and mbm is phosphorylated in vitro by
CC CkIIalpha. {ECO:0000269|PubMed:24615015}.
CC -!- DISRUPTION PHENOTYPE: Lethality around pupal formation with rare
CC escapers with a delayed eclosion time (PubMed:24615015). Reduced size
CC of neuroblasts and ganglion mother cells with no effect on cell size in
CC wing imaginal disks (PubMed:24615015). Grossly reduced mushroom bodies
CC with degeneration of Kenyon cells (PubMed:15375215).
CC {ECO:0000269|PubMed:15375215, ECO:0000269|PubMed:24615015}.
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DR EMBL; AE014134; AAF51521.1; -; Genomic_DNA.
DR EMBL; AY069307; AAL39452.1; -; mRNA.
DR RefSeq; NP_608511.1; NM_134667.5.
DR AlphaFoldDB; Q9VPM5; -.
DR IntAct; Q9VPM5; 5.
DR STRING; 7227.FBpp0077798; -.
DR iPTMnet; Q9VPM5; -.
DR PaxDb; Q9VPM5; -.
DR PRIDE; Q9VPM5; -.
DR DNASU; 33194; -.
DR EnsemblMetazoa; FBtr0078139; FBpp0077798; FBgn0086912.
DR GeneID; 33194; -.
DR KEGG; dme:Dmel_CG11604; -.
DR UCSC; CG11604-RA; d. melanogaster.
DR CTD; 33194; -.
DR FlyBase; FBgn0086912; mbm.
DR VEuPathDB; VectorBase:FBgn0086912; -.
DR eggNOG; ENOG502SB0T; Eukaryota.
DR HOGENOM; CLU_490280_0_0_1; -.
DR InParanoid; Q9VPM5; -.
DR OMA; FECQMIC; -.
DR OrthoDB; 1337711at2759; -.
DR PhylomeDB; Q9VPM5; -.
DR BioGRID-ORCS; 33194; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33194; -.
DR PRO; PR:Q9VPM5; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0086912; Expressed in ovary and 28 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007628; P:adult walking behavior; IDA:FlyBase.
DR GO; GO:0007612; P:learning; IMP:FlyBase.
DR GO; GO:0016319; P:mushroom body development; IMP:FlyBase.
DR GO; GO:0008355; P:olfactory learning; TAS:FlyBase.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:UniProtKB.
DR GO; GO:0007632; P:visual behavior; IDA:FlyBase.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF57756; SSF57756; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Zinc; Zinc-finger.
FT CHAIN 1..539
FT /note="Protein mushroom body miniature"
FT /id="PRO_0000436781"
FT ZN_FING 354..367
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 371..386
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 1..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..183
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..446
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..477
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24615015"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24615015"
FT MOD_RES 292
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24615015"
FT MOD_RES 327
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24615015"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24615015"
FT MOD_RES 333
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24615015"
FT MUTAGEN 288
FT /note="S->A: Strongly reduced in vitro phosphorylation by
FT CkIIalpha; when associated with A-290 and A-292."
FT /evidence="ECO:0000269|PubMed:24615015"
FT MUTAGEN 290
FT /note="S->A: Strongly reduced in vitro phosphorylation by
FT CkIIalpha; when associated with A-288 and A-292."
FT /evidence="ECO:0000269|PubMed:24615015"
FT MUTAGEN 292
FT /note="T->A: Strongly reduced in vitro phosphorylation by
FT CkIIalpha; when associated with A-288 and A-290."
FT /evidence="ECO:0000269|PubMed:24615015"
FT MUTAGEN 327
FT /note="T->A: Minor reduction of in vitro phosphorylation by
FT CkIIalpha; when associated with A-332 and A-333."
FT /evidence="ECO:0000269|PubMed:24615015"
FT MUTAGEN 332
FT /note="S->A: Minor reduction of in vitro phosphorylation by
FT CkIIalpha; when associated with A-327 and A-333."
FT /evidence="ECO:0000269|PubMed:24615015"
FT MUTAGEN 333
FT /note="T->A: Minor reduction of in vitro phosphorylation by
FT CkIIalpha; when associated with A-327 and A-332."
FT /evidence="ECO:0000269|PubMed:24615015"
SQ SEQUENCE 539 AA; 58629 MW; 656DB46EE5411CF4 CRC64;
MHNSGGQSGW NLSGEERKPF SNYGRNNQQR RSSGGGGRGS HSQNRAANGN WPDAGSEGGQ
NGNAFNKFRD PQQELDNHQP NKRGGRRNRG GGGGGGGWGG RRGNRGRDSN RRGGRNNSWQ
PKDQHVSPGQ SNMLYFDNVG DFTEDPPLPR SSPAPSSLRQ ESLPPVTFAA DLTPPPPVSV
APPDVAVTPE EPTVPLINIK KEKEMEHKSK IKQFVKAEPK SPKKKKVNSS RSSSTSGEES
EPEPGEMVVN TKAVVVPSPK AKAIKTPVAS TPKPKAVKPV SSSDSSTSDS DTDDEQSHPP
AKSKKMEKNT EEDVVCMGSQ ERQFTITDEE ESTEPEDDKK ARKQKNKGKT VDVCGICDKK
GHTSFQCQMI CRNCSGSYHG LKNCPNPPNL NIAIQSFVEF AMQQMTAFHC EQGFGFPAGT
VTAPVSAKPK KDKKASIKKI KKSSQKRMKV EPKDHDEEDD EEDDDEDEDD SSESDDSESS
EEPHPAPVSK QKRKRGTKAS VSAAASLPPQ VFPFPLLGAP GAPFNSMMYS YRAPFNFSK
