NCBP2_DROME
ID NCBP2_DROME Reviewed; 154 AA.
AC Q9V3L6;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Nuclear cap-binding protein subunit 2;
DE AltName: Full=20 kDa nuclear cap-binding protein;
DE AltName: Full=NCBP 20 kDa subunit;
DE Short=CBP20;
GN Name=Cbp20; ORFNames=CG12357;
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 FUNCTION, AND INTERACTION WITH ARS2.
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 co-
CC transcriptionally to the 5' cap of pre-mRNAs and is involved in various
CC processes such as pre-mRNA splicing and RNA-mediated gene silencing
CC (RNAi). The CBC complex is involved in miRNA-mediated RNA interference
CC via its interaction with Ars2 and is required for primary microRNAs
CC (miRNAs) processing. Also involved in innate immunity via the short
CC interfering RNAs (siRNAs) processing machinery by restricting the viral
CC RNA production. In the CBC complex, Cbp20 recognizes and binds capped
CC RNAs (m7GpppG-capped RNA) but requires Cbp80 to stabilize the movement
CC of its N-terminal loop and lock the CBC into a high affinity cap-
CC binding state with the cap structure. {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 (By similarity). Interacts with Ars2. {ECO:0000250,
CC ECO:0000269|PubMed:19632183}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RRM NCBP2 family. {ECO:0000305}.
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DR EMBL; AJ238969; CAB53185.1; -; mRNA.
DR EMBL; AE014297; AAF55496.1; -; Genomic_DNA.
DR EMBL; AY070578; AAL48049.1; -; mRNA.
DR RefSeq; NP_524396.1; NM_079672.3.
DR AlphaFoldDB; Q9V3L6; -.
DR SMR; Q9V3L6; -.
DR BioGRID; 67190; 5.
DR IntAct; Q9V3L6; 2.
DR STRING; 7227.FBpp0082973; -.
DR PaxDb; Q9V3L6; -.
DR PRIDE; Q9V3L6; -.
DR ABCD; Q9V3L6; 1 sequenced antibody.
DR DNASU; 42166; -.
DR EnsemblMetazoa; FBtr0083551; FBpp0082973; FBgn0022943.
DR GeneID; 42166; -.
DR KEGG; dme:Dmel_CG12357; -.
DR UCSC; CG12357-RA; d. melanogaster.
DR CTD; 42166; -.
DR FlyBase; FBgn0022943; Cbp20.
DR VEuPathDB; VectorBase:FBgn0022943; -.
DR eggNOG; KOG0121; Eukaryota.
DR GeneTree; ENSGT00390000003197; -.
DR HOGENOM; CLU_070952_2_0_1; -.
DR InParanoid; Q9V3L6; -.
DR OMA; AENCMRY; -.
DR OrthoDB; 1421503at2759; -.
DR PhylomeDB; Q9V3L6; -.
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 BioGRID-ORCS; 42166; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 42166; -.
DR PRO; PR:Q9V3L6; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0022943; Expressed in brain and 24 other tissues.
DR ExpressionAtlas; Q9V3L6; baseline and differential.
DR Genevisible; Q9V3L6; DM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; HDA:FlyBase.
DR GO; GO:0005846; C:nuclear cap binding complex; IBA:GO_Central.
DR GO; GO:0071011; C:precatalytic spliceosome; HDA:FlyBase.
DR GO; GO:0005681; C:spliceosomal complex; ISS:FlyBase.
DR GO; GO:0003729; F:mRNA binding; ISS:FlyBase.
DR GO; GO:0000339; F:RNA cap binding; IBA:GO_Central.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; 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: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 CDD; cd12240; RRM_NCBP2; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR027157; NCBP2.
DR InterPro; IPR034148; NCBP2_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR18847; PTHR18847; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing.
FT CHAIN 1..154
FT /note="Nuclear cap-binding protein subunit 2"
FT /id="PRO_0000385266"
FT DOMAIN 30..108
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT BINDING 10
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
FT BINDING 33
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
FT BINDING 102..106
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
FT BINDING 113..117
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
FT BINDING 123..124
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
SQ SEQUENCE 154 AA; 17719 MW; A52A5BA575757A41 CRC64;
MFASVELSSY RDQHFKGSRS EQERSLRDSC TLYVGNLSFY TTEEQIHELF SRCGDVRVIV
MGLDKYKKTP CGFCFVEYYV RSEAEAAMRF VNGTRLDDRL IRVDWDAGFV EGRQYGRGKT
GGQVRDEYRT DYDAGRGGYG KLLSQKIAPN TDNR
