NCBP1_DROME
ID NCBP1_DROME Reviewed; 800 AA.
AC Q7K4N3; Q7K7B2; Q9U980;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Nuclear cap-binding protein subunit 1;
DE AltName: Full=80 kDa nuclear cap-binding protein;
DE Short=CBP80;
DE Short=NCBP 80 kDa subunit;
GN Name=Cbp80; ORFNames=CG7035;
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].
RC STRAIN=Oregon-R; TISSUE=Imaginal disk;
RA Lewis J.D.;
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
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 GENOMIC DNA] OF 1-348.
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-9, AND IDENTIFICATION BY MASS
RP 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.
RX PubMed=19632183; DOI=10.1016/j.cell.2009.04.045;
RA Sabin L.R., Zhou R., Gruber J.J., Lukinova N., Bambina S., Berman A.,
RA Lau C.-K., Thompson C.B., Cherry S.;
RT "Ars2 regulates both miRNA- and siRNA- dependent silencing and suppresses
RT RNA virus infection in Drosophila.";
RL Cell 138:340-351(2009).
CC -!- FUNCTION: Component of the cap-binding complex (CBC), which binds
CC cotranscriptionally to the 5'-cap of pre-mRNAs and is involved in
CC various processes such as pre-mRNA splicing and RNA-mediated gene
CC silencing (RNAi). The CBC complex is involved in miRNA-mediated RNA
CC interference via its interaction with Ars2 and is required for primary
CC microRNAs (miRNAs) processing. Also involved in innate immunity via the
CC short interfering RNAs (siRNAs) processing machinery by restricting the
CC viral RNA production. In the CBC complex, Cbp80 does not bind directly
CC capped RNAs (m7GpppG-capped RNA) but is required to stabilize the
CC movement of the N-terminal loop of Cbp20 and lock the CBC into a high
CC affinity cap-binding state with the cap structure.
CC {ECO:0000269|PubMed:19632183}.
CC -!- SUBUNIT: Component of the nuclear cap-binding complex (CBC), a
CC heterodimer composed of Cbp80 and Cbp20 that interacts with m7GpppG-
CC capped RNA. {ECO:0000250}.
CC -!- INTERACTION:
CC Q7K4N3; P83949: Ubx; NbExp=3; IntAct=EBI-137965, EBI-202590;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NCBP1 family. {ECO:0000305}.
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DR EMBL; AJ238970; CAB53186.1; -; mRNA.
DR EMBL; AE014298; AAN09124.1; -; Genomic_DNA.
DR EMBL; AY051796; AAK93220.1; -; mRNA.
DR EMBL; AL031766; CAA21136.1; -; Genomic_DNA.
DR RefSeq; NP_524750.2; NM_080011.3.
DR RefSeq; NP_726938.1; NM_167012.3.
DR AlphaFoldDB; Q7K4N3; -.
DR SMR; Q7K4N3; -.
DR BioGRID; 69037; 15.
DR IntAct; Q7K4N3; 3.
DR STRING; 7227.FBpp0070652; -.
DR iPTMnet; Q7K4N3; -.
DR PaxDb; Q7K4N3; -.
DR PRIDE; Q7K4N3; -.
DR ABCD; Q7K4N3; 7 sequenced antibodies.
DR DNASU; 44409; -.
DR EnsemblMetazoa; FBtr0070683; FBpp0070651; FBgn0022942.
DR EnsemblMetazoa; FBtr0070684; FBpp0070652; FBgn0022942.
DR GeneID; 44409; -.
DR KEGG; dme:Dmel_CG7035; -.
DR UCSC; CG7035-RA; d. melanogaster.
DR CTD; 44409; -.
DR FlyBase; FBgn0022942; Cbp80.
DR VEuPathDB; VectorBase:FBgn0022942; -.
DR eggNOG; KOG1104; Eukaryota.
DR GeneTree; ENSGT00390000001733; -.
DR HOGENOM; CLU_013207_0_0_1; -.
DR InParanoid; Q7K4N3; -.
DR OMA; QPFKIPF; -.
DR OrthoDB; 270650at2759; -.
DR PhylomeDB; Q7K4N3; -.
DR Reactome; R-DME-111367; SLBP independent Processing of Histone Pre-mRNAs.
DR Reactome; R-DME-113418; Formation of the Early Elongation Complex.
DR Reactome; R-DME-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-DME-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-DME-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-DME-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-DME-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-DME-6803529; FGFR2 alternative splicing.
DR Reactome; R-DME-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-DME-72086; mRNA Capping.
DR Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-DME-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-DME-72187; mRNA 3'-end processing.
DR Reactome; R-DME-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR Reactome; R-DME-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-DME-77588; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
DR Reactome; R-DME-77595; Processing of Intronless Pre-mRNAs.
DR Reactome; R-DME-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-DME-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; Q7K4N3; -.
DR BioGRID-ORCS; 44409; 1 hit in 1 CRISPR screen.
DR ChiTaRS; Cbp80; fly.
DR GenomeRNAi; 44409; -.
DR PRO; PR:Q7K4N3; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0022942; Expressed in egg chamber and 26 other tissues.
DR ExpressionAtlas; Q7K4N3; baseline and differential.
DR Genevisible; Q7K4N3; DM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; HDA:FlyBase.
DR GO; GO:0005845; C:mRNA cap binding complex; IBA:GO_Central.
DR GO; GO:0005846; C:nuclear cap binding complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0071011; C:precatalytic spliceosome; HDA:FlyBase.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0000339; F:RNA cap binding; IBA:GO_Central.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW.
DR GO; GO:0006406; P:mRNA export from nucleus; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:FlyBase.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IMP:FlyBase.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IBA:GO_Central.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IMP:UniProtKB.
DR GO; GO:0031053; P:primary miRNA processing; IMP:UniProtKB.
DR GO; GO:0030422; P:siRNA processing; IMP:FlyBase.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR027159; CBP80.
DR InterPro; IPR015172; MIF4G-like_typ-1.
DR InterPro; IPR015174; MIF4G-like_typ-2.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR PANTHER; PTHR12412; PTHR12412; 1.
DR Pfam; PF02854; MIF4G; 1.
DR Pfam; PF09088; MIF4G_like; 1.
DR Pfam; PF09090; MIF4G_like_2; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; SSF48371; 3.
PE 1: Evidence at protein level;
KW mRNA capping; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-mediated gene silencing.
FT CHAIN 1..800
FT /note="Nuclear cap-binding protein subunit 1"
FT /id="PRO_0000385235"
FT DOMAIN 31..243
FT /note="MIF4G"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 44..45
FT /note="RS -> AT (in Ref. 1; CAB53186)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="R -> A (in Ref. 1; CAB53186)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 800 AA; 93227 MW; 4D90C157E9A33B9B CRC64;
MSRRRAHDTE DEGYDHRRNK RRRVSENQEI EDRLESLILR VGERSTSSVE SNLEGLVSVL
EADLGTFRLK ILRILSDCAV RMPEKCTVYT TLVGLLNAKN YKFGGEFVDH MVKTFKESLK
MCRWDAARYS LRFLADLVNC HVISATSLLQ LLDTMIDVSN EDTVPQVRRD WFVFAVLSTL
PWVGRDLYEK KESALESLLL RIEVYLNKRS KKHHNALRVW SSDAPHPQEE YLDCLWAQIR
KLRQDNWAEK HIPRPYLVFD SILCEALQHN LPTIVPPPHH DNFEYPMPWV VYRMFDYTDC
PDGPNLPGAH SIERFLIEEH LHHIIETYHH ERKDCAAQLL SFPYKHKIPL EYCIVEVVFA
ELFHMPTPRY LDICYGSILI ELCKLQPATL PQVLAQATEI LFMRIDSMNT SCFDRFVNWF
SYHLSNFKFT WSWDEWDSCL LLDGEHPRPK FIQEVLQKCL RLSYHQRITE MMPTTYAKLI
PLTPVPNYKY ANEEAANLPG TTVAHQLVVA IRQKCTPEEV VNILKDIPNS GYSGEEMSDG
SFNALKIDVF VQTLLNLGSK SFSHSFAAIS KFHSVFRALA ETEEAQICIL HNIFELWSSH
QQMMVVLIDK LLKLQIVDCS AVATWIFSKE MTGEFTKLYL WEILHLTIKK MNKHVIKLNT
ELSEAKEKLA KADSSSSDSE DDSSHKRKKP ITHADKPSEE VVERMEEKLE AANVNQKRLF
LIVFQRFIMI LSEHLLRSDT DGRDPDTDWY RWTIGRLQQV FLMHHEQVQK YSSTLETLLF
TSDLDTHILE VFQQFVALRA
