NCBP1_ARATH
ID NCBP1_ARATH Reviewed; 848 AA.
AC Q9SIU2; Q8VZH3; Q9LKN6;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Nuclear cap-binding protein subunit 1;
DE AltName: Full=80 kDa nuclear cap-binding protein;
DE Short=AtCBP80;
DE Short=NCBP 80 kDa subunit;
DE AltName: Full=Abscisic acid-hypersensitive protein 1;
DE Short=ABA-hypersensitive protein 1;
DE AltName: Full=Protein ENSALADA;
GN Name=ABH1; Synonyms=CBP80, ENS; OrderedLocusNames=At2g13540;
GN ORFNames=T10F5.8;
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], FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION
RP WITH CBP20.
RC STRAIN=cv. Columbia;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
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 [5]
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND 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 [7]
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 [8]
RP FUNCTION.
RX PubMed=18486559; DOI=10.1016/j.devcel.2008.04.005;
RA Gregory B.D., O'Malley R.C., Lister R., Urich M.A., Tonti-Filippini J.,
RA Chen H., Millar A.H., Ecker J.R.;
RT "A link between RNA metabolism and silencing affecting Arabidopsis
RT development.";
RL Dev. Cell 14:854-866(2008).
RN [9]
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 [10]
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 [11]
RP INTERACTION WITH CBP20.
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).
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) by microRNAs (miRNAs). The CBC complex is involved in
CC miRNA-mediated RNA interference and is required for primary miRNA
CC processing. In the CBC complex, ABH1/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. Involved in
CC flowering regulation, possibly by regulating pre-mRNA splicing of FLC
CC gene. Acts as a negative regulator of abscisic acid signaling in guard
CC cells. {ECO:0000269|PubMed:11525733, ECO:0000269|PubMed:12427994,
CC ECO:0000269|PubMed:18486559, ECO:0000269|PubMed:18550839,
CC ECO:0000269|PubMed:18829588}.
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. {ECO:0000269|PubMed:11525733,
CC ECO:0000269|PubMed:19453442}.
CC -!- INTERACTION:
CC Q9SIU2; Q9XFD1: CBP20; NbExp=7; IntAct=EBI-2359412, EBI-2354070;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12427994}. Cytoplasm
CC {ECO:0000269|PubMed:12427994}. 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: Stomatal closing and reduced wilting during
CC drought due to abscisic acid-hypersensitivity in early abscisic acid
CC signaling. Abscisic acid-hypersensitive cytosolic calcium increases in
CC guard cells. {ECO:0000269|PubMed:11525733}.
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 NCBP1 family. {ECO:0000305}.
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DR EMBL; AF272891; AAK91588.1; -; mRNA.
DR EMBL; AF268377; AAF76167.1; -; mRNA.
DR EMBL; AC007063; AAD22677.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC06238.1; -; Genomic_DNA.
DR EMBL; AY064960; AAL38378.1; -; mRNA.
DR EMBL; BT000650; AAN18216.1; -; mRNA.
DR PIR; C84508; C84508.
DR RefSeq; NP_565356.1; NM_126934.4.
DR AlphaFoldDB; Q9SIU2; -.
DR SMR; Q9SIU2; -.
DR BioGRID; 1201; 13.
DR ComplexPortal; CPX-1334; Nuclear cap-binding complex.
DR IntAct; Q9SIU2; 1.
DR STRING; 3702.AT2G13540.1; -.
DR iPTMnet; Q9SIU2; -.
DR PaxDb; Q9SIU2; -.
DR PRIDE; Q9SIU2; -.
DR ProteomicsDB; 251141; -.
DR EnsemblPlants; AT2G13540.1; AT2G13540.1; AT2G13540.
DR GeneID; 815840; -.
DR Gramene; AT2G13540.1; AT2G13540.1; AT2G13540.
DR KEGG; ath:AT2G13540; -.
DR Araport; AT2G13540; -.
DR TAIR; locus:2054137; AT2G13540.
DR eggNOG; KOG1104; Eukaryota.
DR HOGENOM; CLU_013207_1_0_1; -.
DR InParanoid; Q9SIU2; -.
DR OMA; QPFKIPF; -.
DR OrthoDB; 270650at2759; -.
DR PhylomeDB; Q9SIU2; -.
DR PRO; PR:Q9SIU2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SIU2; baseline and differential.
DR Genevisible; Q9SIU2; AT.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
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:TAIR.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0000339; F:RNA cap binding; IDA:TAIR.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW.
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:0048574; P:long-day photoperiodism, flowering; IMP:TAIR.
DR GO; GO:0035195; P:miRNA-mediated gene silencing; IC:ComplexPortal.
DR GO; GO:0006406; P:mRNA export from nucleus; IC:ComplexPortal.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:ComplexPortal.
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:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IBA:GO_Central.
DR GO; GO:0031053; P:primary miRNA processing; IMP:ComplexPortal.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0000394; P:RNA splicing, via endonucleolytic cleavage and ligation; IMP:TAIR.
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 Cytoplasm; mRNA capping; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; RNA-mediated gene silencing.
FT CHAIN 1..848
FT /note="Nuclear cap-binding protein subunit 1"
FT /id="PRO_0000385246"
FT DOMAIN 8..228
FT /note="MIF4G"
FT REGION 767..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 625
FT /note="V -> M (in Ref. 5; AAN18216/AAL38378)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 848 AA; 96548 MW; 1E583391F4BAE1A8 CRC64;
MSNWKTLLLR IGEKGPEYGT SSDYKDHIET CFGVIRREIE RSGDQVLPFL LQCAEQLPHK
IPLYGTLIGL LNLENEDFVQ KLVESVHANF QVALDSGNCN SIRILLRFMT SLLCSKVIQP
ASLIVVFETL LSSAATTVDE EKGNPSWQPQ ADFYVICILS SLPWGGSELA EQVPDEIERV
LVGIQAYLSI RKNSSTSGLN FFHNGEFESS LAEKDFVEDL LDRIQSLASN GWKLESVPRP
HLSFEAQLVA GKFHELRPIK CMEQPSPPSD HSRAYSGKQK HDALTRYPQR IRRLNIFPAN
KMEDVQPIDR FVVEEYLLDV LFYLNGCRKE CASYMANLPV TFRYEYLMAE TLFSQILLLP
QPPFKTLYYT LVIMDLCKAL PGAFPAVVAG AVRALFEKIS DLDMESRTRL ILWFSHHLSN
FQFIWPWEEW AFVLDLPKWA PKRVFVQEIL QREVRLSYWD KIKQSIENAT ALEELLPPKA
GPNFMYSLEE GKEKTEEQQL SAELSRKVKE KQTARDMIVW IEETIYPVHG FEVTLTIVVQ
TLLDIGSKSF THLVTVLERY GQVFSKLCPD NDKQVMLLSQ VSTYWKNNVQ MTAVAIDRMM
GYRLVSNQAI VRWVFSPENV DQFHVSDQPW EILGNALNKT YNRISDLRKD ISNITKNVLV
AEKASANARV ELEAAESKLS LVEGEPVLGE NPAKMKRLKS TVEKTGEAEL SLRESLEAKE
ALLNRALSET EVLLLLLFQS FLGVLKERLP DPTKVRSVQD LKSIGAEDDK PSAMDVDSEN
GNPKKSCEVG EREQWCLSTL GYLTAFTRQY ASEIWPHMEK LESEVFSGED VHPLFLQAIS
SALQFPLH
