NCBP2_ARATH
ID NCBP2_ARATH Reviewed; 257 AA.
AC Q9XFD1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 146.
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=AtCBP20;
GN Name=CBP20; OrderedLocusNames=At5g44200; ORFNames=MLN1.12;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11867224; DOI=10.1016/s0378-1119(01)00859-9;
RA Kmieciak M., Simpson C.G., Lewandowska D., Brown J.W.S., Jarmolowski A.;
RT "Cloning and characterization of two subunits of Arabidopsis thaliana
RT nuclear cap-binding complex.";
RL Gene 283:171-183(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH ABH1.
RX PubMed=11525733; DOI=10.1016/s0092-8674(01)00460-3;
RA Hugouvieux V., Kwak J.M., Schroeder J.I.;
RT "An mRNA cap binding protein, ABH1, modulates early abscisic acid signal
RT transduction in Arabidopsis.";
RL Cell 106:477-487(2001).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=12427994; DOI=10.1104/pp.009480;
RA Hugouvieux V., Murata Y., Young J.J., Kwak J.M., Mackesy D.Z.,
RA Schroeder J.I.;
RT "Localization, ion channel regulation, and genetic interactions during
RT abscisic acid signaling of the nuclear mRNA cap-binding protein, ABH1.";
RL Plant Physiol. 130:1276-1287(2002).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=15604709; DOI=10.1007/s11103-004-1680-2;
RA Papp I., Mur L.A., Dalmadi A., Dulai S., Koncz C.;
RT "A mutation in the cap binding protein 20 gene confers drought tolerance to
RT Arabidopsis.";
RL Plant Mol. Biol. 55:679-686(2004).
RN [9]
RP LACK OF FUNCTION IN NMD.
RX PubMed=19081850;
RA Dzikiewicz-Krawczyk A., Piontek P., Szweykowska-Kulinska Z.,
RA Jarmolowski A.;
RT "The nuclear cap-binding protein complex is not essential for nonsense-
RT mediated mRNA decay (NMD) in plants.";
RL Acta Biochim. Pol. 55:825-828(2008).
RN [10]
RP FUNCTION.
RX PubMed=18829588; DOI=10.1093/pcp/pcn146;
RA Kim S., Yang J.-Y., Xu J., Jang I.-C., Prigge M.J., Chua N.-H.;
RT "Two cap-binding proteins CBP20 and CBP80 are involved in processing
RT primary MicroRNAs.";
RL Plant Cell Physiol. 49:1634-1644(2008).
RN [11]
RP FUNCTION.
RX PubMed=18550839; DOI=10.1073/pnas.0802493105;
RA Laubinger S., Sachsenberg T., Zeller G., Busch W., Lohmann J.U.,
RA Raetsch G., Weigel D.;
RT "Dual roles of the nuclear cap-binding complex and SERRATE in pre-mRNA
RT splicing and microRNA processing in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:8795-8800(2008).
RN [12]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ABH1.
RX PubMed=19453442; DOI=10.1111/j.1365-313x.2009.03915.x;
RA Kierzkowski D., Kmieciak M., Piontek P., Wojtaszek P.,
RA Szweykowska-Kulinska Z., Jarmolowski A.;
RT "The Arabidopsis CBP20 targets the cap-binding complex to the nucleus, and
RT is stabilized by CBP80.";
RL Plant J. 59:814-825(2009).
RN [13]
RP FUNCTION, AND INTERACTION WITH FRIGIDA.
RX PubMed=19429606; DOI=10.1104/pp.109.137448;
RA Geraldo N., Baeurle I., Kidou S., Hu X., Dean C.;
RT "FRIGIDA delays flowering in Arabidopsis via a cotranscriptional mechanism
RT involving direct interaction with the nuclear cap-binding complex.";
RL Plant Physiol. 150:1611-1618(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(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) by microRNAs (miRNAs). The CBC complex is involved in miRNA-
CC mediated RNA interference and is required for primary miRNA processing.
CC In the CBC complex, CBP20 recognizes and binds capped RNAs (m7GpppG-
CC capped RNA) but requires ABH1/CBP80 to stabilize the movement of its N-
CC terminal loop and lock the CBC into a high affinity cap-binding state
CC with the cap structure. CBP20 also plays a role in stabilization of
CC ABH1/CBP80 and ABH1/CBP80 localization to the nucleus. Involved in
CC flowering regulation via its interaction with FRIGIDA.
CC {ECO:0000269|PubMed:18550839, ECO:0000269|PubMed:18829588,
CC ECO:0000269|PubMed:19429606}.
CC -!- SUBUNIT: Component of the nuclear cap-binding complex (CBC), a
CC heterodimer composed of ABH1/CBP80 and CBP20 that interacts with
CC m7GpppG-capped RNA. Interacts with FRIGIDA; the interaction is direct.
CC {ECO:0000269|PubMed:11525733, ECO:0000269|PubMed:19429606,
CC ECO:0000269|PubMed:19453442}.
CC -!- INTERACTION:
CC Q9XFD1; Q9SIU2: ABH1; NbExp=7; IntAct=EBI-2354070, EBI-2359412;
CC Q9XFD1; Q9FDW0: FRI; NbExp=2; IntAct=EBI-2354070, EBI-2126171;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19453442}. Cytoplasm
CC {ECO:0000269|PubMed:19453442}. Note=Predominantly nuclear.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues analyzed, including roots,
CC stems, leaves and flowers. {ECO:0000269|PubMed:11867224,
CC ECO:0000269|PubMed:12427994}.
CC -!- DISRUPTION PHENOTYPE: Hypersensitivity to abscisic acid during
CC germination, significant reduction of stomatal conductance and greatly
CC enhanced tolerance to drought. Plants also display mild developmental
CC abnormalities, such as serrated rosette leaves, delayed development and
CC slightly reduced stature. {ECO:0000269|PubMed:15604709}.
CC -!- MISCELLANEOUS: In contrast to other organisms, the CBC complex is
CC apparently not essential for nonsense-mediated mRNA decay (NMD) in
CC Arabidopsis.
CC -!- SIMILARITY: Belongs to the RRM NCBP2 family. {ECO:0000305}.
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DR EMBL; AF140219; AAD29697.1; -; mRNA.
DR EMBL; AB005239; BAB10987.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95073.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95074.1; -; Genomic_DNA.
DR EMBL; BT004813; AAO44079.1; -; mRNA.
DR EMBL; AK227850; BAE99827.1; -; mRNA.
DR RefSeq; NP_001078705.1; NM_001085236.2.
DR RefSeq; NP_199233.1; NM_123787.4.
DR AlphaFoldDB; Q9XFD1; -.
DR SMR; Q9XFD1; -.
DR BioGRID; 19693; 8.
DR ComplexPortal; CPX-1334; Nuclear cap-binding complex.
DR IntAct; Q9XFD1; 2.
DR STRING; 3702.AT5G44200.1; -.
DR iPTMnet; Q9XFD1; -.
DR PaxDb; Q9XFD1; -.
DR PRIDE; Q9XFD1; -.
DR ProteomicsDB; 251098; -.
DR EnsemblPlants; AT5G44200.1; AT5G44200.1; AT5G44200.
DR EnsemblPlants; AT5G44200.2; AT5G44200.2; AT5G44200.
DR GeneID; 834443; -.
DR Gramene; AT5G44200.1; AT5G44200.1; AT5G44200.
DR Gramene; AT5G44200.2; AT5G44200.2; AT5G44200.
DR KEGG; ath:AT5G44200; -.
DR Araport; AT5G44200; -.
DR TAIR; locus:2167649; AT5G44200.
DR eggNOG; KOG0121; Eukaryota.
DR HOGENOM; CLU_070952_0_0_1; -.
DR InParanoid; Q9XFD1; -.
DR OMA; APPQYDR; -.
DR OrthoDB; 1421503at2759; -.
DR PhylomeDB; Q9XFD1; -.
DR PRO; PR:Q9XFD1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9XFD1; baseline and differential.
DR Genevisible; Q9XFD1; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005845; C:mRNA cap binding complex; IPI:ComplexPortal.
DR GO; GO:0005846; C:nuclear cap binding complex; IPI:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0000339; F:RNA cap binding; IDA:TAIR.
DR GO; GO:1901527; P:abscisic acid-activated signaling pathway involved in stomatal movement; IDA:ComplexPortal.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IMP:ComplexPortal.
DR GO; GO:0051607; P:defense response to virus; IMP:TAIR.
DR GO; GO:0035195; P:miRNA-mediated gene silencing; IC:ComplexPortal.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IEA:InterPro.
DR GO; GO:0006406; P:mRNA export from nucleus; IC:ComplexPortal.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IC:ComplexPortal.
DR GO; GO:0031053; P:primary miRNA processing; IMP:ComplexPortal.
DR GO; GO:0016070; P:RNA metabolic process; TAS:TAIR.
DR GO; GO:0000394; P:RNA splicing, via endonucleolytic cleavage and ligation; IMP:TAIR.
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 Cytoplasm; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; RNA-mediated gene silencing.
FT CHAIN 1..257
FT /note="Nuclear cap-binding protein subunit 2"
FT /id="PRO_0000385277"
FT DOMAIN 34..112
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 119..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 201..207
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 254..257
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 124..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 14
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
FT BINDING 106..110
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
FT BINDING 117..121
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
FT BINDING 127..128
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 257 AA; 29609 MW; DD8B12A0639E1D58 CRC64;
MASLFKEQAK LSAYRDRRFS GTQEEFDEAL RASTTVYIGN VSFYTTEEQL YELFSRAGEI
KKIIMGLDKN TKTPCGFCFV LFYSREDTED AVKYISGTIL DDRPIRVDFD WGFQEGRQWG
RGRSGGQVRD EYRTDYDPAR GGYGKLVQKE LEAQRQLVDY GTGSLGAYPQ AAPTNYGNGR
RGGGNYGQGG QNRHGRGDYH RKRQRDDDRY GRDNSRRNTD HESRRDTDSD MRPEKNPRFR
ESGDSDDDGE DDRKRRS
