MEPCE_DROME
ID MEPCE_DROME Reviewed; 1367 AA.
AC Q7K480; Q86LF5; Q9NJV6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=7SK snRNA methylphosphate capping enzyme bin3 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q7L2J0};
DE AltName: Full=Bicoid-interacting protein 3;
GN Name=bin3; ORFNames=CG8276;
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 [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INTERACTION WITH BCD.
RX PubMed=10717484; DOI=10.1016/s0378-1119(00)00048-2;
RA Zhu W., Hanes S.D.;
RT "Identification of Drosophila bicoid-interacting proteins using a custom
RT two-hybrid selection.";
RL Gene 245:329-339(2000).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-688; THR-1116; SER-1123;
RP SER-1242 AND SER-1251, AND IDENTIFICATION BY 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 [7]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=21262214; DOI=10.1016/j.ydbio.2011.01.017;
RA Singh N., Morlock H., Hanes S.D.;
RT "The Bin3 RNA methyltransferase is required for repression of caudal
RT translation in the Drosophila embryo.";
RL Dev. Biol. 352:104-115(2011).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that adds
CC a methylphosphate cap at the 5'-end of 7SK snRNA, leading to stabilize
CC it (By similarity). Required for dorso-ventral patterning in oogenesis
CC and for anterior-posterior pattern formation during embryogenesis,
CC possibly by binding and stabilizing 7SK RNA, thereby promoting
CC formation of a repressive RNA-protein complex (PubMed:21262214).
CC {ECO:0000250|UniProtKB:Q7L2J0, ECO:0000269|PubMed:21262214}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end triphospho-guanosine-ribonucleotide-snRNA + S-
CC adenosyl-L-methionine = a 5'-end methyltriphosphate-guanosine-
CC ribonucleotide-snRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:58780, Rhea:RHEA-COMP:15220, Rhea:RHEA-COMP:15221,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:138278,
CC ChEBI:CHEBI:142789; Evidence={ECO:0000250|UniProtKB:Q7L2J0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58781;
CC Evidence={ECO:0000250|UniProtKB:Q7L2J0};
CC -!- SUBUNIT: Interacts with bicoid/bcd. {ECO:0000269|PubMed:10717484}.
CC -!- INTERACTION:
CC Q7K480; P09081: bcd; NbExp=4; IntAct=EBI-180984, EBI-196628;
CC -!- TISSUE SPECIFICITY: Distributed throughout the early embryo.
CC {ECO:0000269|PubMed:10717484}.
CC -!- DEVELOPMENTAL STAGE: Detectable in early embryos. Present coincident
CC with bicoid/bcd expression, with peak levels detected in 0-2 hours
CC embryos. Expression is lower during cellularization stages (2-4 hours)
CC and drops dramatically during late embryonic development (4-24 hours).
CC Very little, if any expression is detected in unfertilized eggs.
CC {ECO:0000269|PubMed:10717484, ECO:0000269|PubMed:21262214}.
CC -!- DISRUPTION PHENOTYPE: Severe defect in oogenesis: females lay eggs,
CC however, up to 50% do not initiate development and many show a
CC dorsalized phenotype. Among the eggs that do initiate development, up
CC to 20% fail to complete embryogenesis and of these, nearly all display
CC severe head defects and die as unhatched larvae or die soon after
CC hatching. Mutants show anterior pattern defects and fail to repress the
CC translation of caudal mRNA and exhibit head involution defects. Mutants
CC also display a severe reduction in the level of 7SK RNA and reduced
CC binding of bicoid/bcd to the caudal 3' UTR.
CC {ECO:0000269|PubMed:21262214}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO47868.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF097636; AAF63187.1; -; mRNA.
DR EMBL; AE013599; AAF57267.2; -; Genomic_DNA.
DR EMBL; AY052142; AAK93566.1; -; mRNA.
DR EMBL; BT004890; AAO47868.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001260724.1; NM_001273795.1.
DR RefSeq; NP_001303336.1; NM_001316407.1.
DR RefSeq; NP_523626.2; NM_078902.3.
DR RefSeq; NP_724468.1; NM_165468.2.
DR AlphaFoldDB; Q7K480; -.
DR SMR; Q7K480; -.
DR BioGRID; 61453; 7.
DR IntAct; Q7K480; 13.
DR STRING; 7227.FBpp0085336; -.
DR iPTMnet; Q7K480; -.
DR PaxDb; Q7K480; -.
DR PRIDE; Q7K480; -.
DR DNASU; 35552; -.
DR EnsemblMetazoa; FBtr0085992; FBpp0085336; FBgn0263144.
DR EnsemblMetazoa; FBtr0085993; FBpp0085337; FBgn0263144.
DR EnsemblMetazoa; FBtr0336519; FBpp0307591; FBgn0263144.
DR EnsemblMetazoa; FBtr0346718; FBpp0312329; FBgn0263144.
DR GeneID; 35552; -.
DR KEGG; dme:Dmel_CG8276; -.
DR CTD; 55909; -.
DR FlyBase; FBgn0263144; bin3.
DR VEuPathDB; VectorBase:FBgn0263144; -.
DR eggNOG; KOG2899; Eukaryota.
DR GeneTree; ENSGT00940000153993; -.
DR HOGENOM; CLU_247680_0_0_1; -.
DR InParanoid; Q7K480; -.
DR OMA; KFHRHDA; -.
DR OrthoDB; 1185441at2759; -.
DR PhylomeDB; Q7K480; -.
DR SignaLink; Q7K480; -.
DR BioGRID-ORCS; 35552; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 35552; -.
DR PRO; PR:Q7K480; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0263144; Expressed in cleaving embryo and 41 other tissues.
DR ExpressionAtlas; Q7K480; baseline and differential.
DR Genevisible; Q7K480; DM.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0008168; F:methyltransferase activity; ISS:FlyBase.
DR GO; GO:0008171; F:O-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008173; F:RNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:FlyBase.
DR GO; GO:0017069; F:snRNA binding; IDA:FlyBase.
DR GO; GO:0032502; P:developmental process; IMP:UniProtKB.
DR GO; GO:0032259; P:methylation; ISS:FlyBase.
DR GO; GO:0017148; P:negative regulation of translation; IMP:FlyBase.
DR GO; GO:0040031; P:snRNA modification; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR039772; Bin3-like.
DR InterPro; IPR010675; Bin3_C.
DR InterPro; IPR024160; BIN3_SAM-bd_dom.
DR InterPro; IPR025714; Methyltranfer_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12315; PTHR12315; 1.
DR Pfam; PF06859; Bin3; 1.
DR Pfam; PF13847; Methyltransf_31; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51515; BIN3_SAM; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Phosphoprotein; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..1367
FT /note="7SK snRNA methylphosphate capping enzyme bin3"
FT /id="PRO_0000289269"
FT DOMAIN 806..1115
FT /note="Bin3-type SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00848"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1150..1203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1236..1281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1345..1367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..415
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..926
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 808
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q7L2J0"
FT BINDING 828..830
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q7L2J0"
FT BINDING 851..852
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q7L2J0"
FT BINDING 988..989
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q7L2J0"
FT BINDING 1010
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q7L2J0"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1116
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1123
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1242
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1251
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 573
FT /note="L -> LA (in Ref. 1; AAF63187)"
FT /evidence="ECO:0000305"
FT CONFLICT 1152
FT /note="S -> G (in Ref. 5; AAO47868)"
FT /evidence="ECO:0000305"
FT CONFLICT 1267
FT /note="S -> R (in Ref. 5; AAO47868)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1367 AA; 146234 MW; FA3EDD8FDAA7A551 CRC64;
MEKRLSDSPG DCRVTRSTMT PTLRLDQTSR QEPLPQQPDN GPAAAPGKSK SPTPLPGKSQ
AAQHHQFRAP QQQQGPKNRN KAWSKRQHKA GGKHNPSACV GASSGQAQST GSSVIAATLL
PTAASAHKAD LENIQNIHNK NLTAGGGVNH HGNAGTAHHG GGGGAGAHHA AAGGHHHHHN
TRLAQNAAAG GASGGGTIQM HKKMLRGHHH HVLCAGNNAN HTCCLVTGCN GSSIGGVGVA
GSGGATASAG GGGASCKEAQ SCKDTSSLSG NSSIAGSAGA GNAVHYCCGR SKFFLPEKRL
RKEVIVPPTK FLLGGNISDP LNLNSLQNEN TSNASSTNNT PATTPRQSPI TTPPKVEVII
PPNIHDPLHL LDPVDSMEYE KQLTSPMKRA GPGGGMLHHR QHHYRTRKNR KRRRFDSNNT
SHAGDEGGVG SELTDEPPLP AATSSLAASP VAAPLNVGGS LLLSESAAPA PGETAEMGQQ
QEQAHVHSPQ SASTTTTAAE MPTPTPTSAA AATATAEHKE QSAPAPTATS SPQRQQQHVA
AAAEELPTPE TSAAAETPAE EMLLSCSATS ASLVASTLAE RRASRDLRLD LSSTCYGVGG
TGLSFGGSIS SSVGSSFGGG GRKRKISESS TSQKSKKFHR HDAMDKIVSP VVPQPGAWKR
PPRILQPSGA RKPSTRRSTS VSESELLSPV EEQPPKQLPL IGVEIPRDDT PDLPDHGLGS
PLSTTSGATS HTAGEQDSLA GVDISMGDTL GSGVVGKAPL TSSLMLEPAK IPPIKMLPKF
RADGLKYRYG NFDRYVDFRQ MNEFRDVRLQ VFQRHVELFE NKDILDIGCN VGHMTITVAR
HLAPKTIVGI DIDRELVARA RRNLSIFVRI PKEEKLLEVK AEPTVDAKAN IAVKDETSGA
AHKKTRRGKR RRKVHQGIHH HHHHHHDLEQ LQQQQKLNSL LVKPHEFFPI SFPLTYGRIP
RILSSSKSPN MLGNKNQFPA NVFFRHTNYV LKDESLMASD TQQYDLILCL SVTKWIHLNF
GDNGLKMAFK RMFNQLRPGG KLILEAQNWA SYKKKKNLTP EIYNNYKQIE FFPNKFHEYL
LSSEVGFSHS YTLGVPRHMN KGFCRPIQLY AKGDYTPNHV RWSDAYYPQT PYEAYRGIYA
TLPVHRMGGG GSSAGGSNSG HAQMLHLSSS SRSQNYDTPH YAGSASGSAS CRQTPMYQPT
YNPLETDSYQ PSYDMEYLNH MYVFASPLYQ TVWSPPASLR KSSSHTPVFG SVRDAELDGD
GSGGGGSGGG SYHRHVYPPN DDTCSPNANA CNAFNSIRDA DTDDSNQLPG GSRRHVYATN
CGESSSSPQV NHHDAVGEFV DGLMDDEQKS STGGGTGGAA YCDLSDA
