RU2B1_ARATH
ID RU2B1_ARATH Reviewed; 232 AA.
AC O22922; Q8LB63;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=U2 small nuclear ribonucleoprotein B'';
DE Short=U2 snRNP B'';
GN Name=U2B''; OrderedLocusNames=At2g30260; ORFNames=T9D9;
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 [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 [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=9819359; DOI=10.1242/jcs.111.24.3687;
RA Boudonck K., Dolan L., Shaw P.J.;
RT "Coiled body numbers in the Arabidopsis root epidermis are regulated by
RT cell type, developmental stage and cell cycle parameters.";
RL J. Cell Sci. 111:3687-3694(1998).
RN [7]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=14740228; DOI=10.1007/s00412-003-0271-3;
RA Docquier S., Tillemans V., Deltour R., Motte P.;
RT "Nuclear bodies and compartmentalization of pre-mRNA splicing factors in
RT higher plants.";
RL Chromosoma 112:255-266(2004).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=15133128; DOI=10.1091/mbc.e04-01-0055;
RA Lorkovic Z.J., Hilscher J., Barta A.;
RT "Use of fluorescent protein tags to study nuclear organization of the
RT spliceosomal machinery in transiently transformed living plant cells.";
RL Mol. Biol. Cell 15:3233-3243(2004).
RN [9]
RP SUBUNIT, AND GENE FAMILY.
RX PubMed=15987817; DOI=10.1261/rna.2440305;
RA Lorkovic Z.J., Lehner R., Forstner C., Barta A.;
RT "Evolutionary conservation of minor U12-type spliceosome between plants and
RT humans.";
RL RNA 11:1095-1107(2005).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=16624863; DOI=10.1091/mbc.e05-12-1157;
RA Collier S., Pendle A., Boudonck K., van Rij T., Dolan L., Shaw P.;
RT "A distant coilin homologue is required for the formation of cajal bodies
RT in Arabidopsis.";
RL Mol. Biol. Cell 17:2942-2951(2006).
RN [11]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=19419533; DOI=10.1111/j.1365-313x.2009.03859.x;
RA Terzi L.C., Simpson G.G.;
RT "Arabidopsis RNA immunoprecipitation.";
RL Plant J. 59:163-168(2009).
CC -!- FUNCTION: Involved in nuclear pre-mRNA splicing. {ECO:0000250}.
CC -!- SUBUNIT: Component of the spliceosome where it is associated with snRNP
CC U2. {ECO:0000269|PubMed:15987817, ECO:0000269|PubMed:19419533}.
CC -!- SUBCELLULAR LOCATION: Nucleus, Cajal body {ECO:0000269|PubMed:14740228,
CC ECO:0000269|PubMed:15133128, ECO:0000269|PubMed:16624863}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:14740228, ECO:0000269|PubMed:15133128,
CC ECO:0000269|PubMed:16624863, ECO:0000269|PubMed:19419533,
CC ECO:0000269|PubMed:9819359}. Cytoplasm {ECO:0000269|PubMed:9819359}.
CC Note=Present in coiled bodies and an interchromatin network.
CC Redistributed throughout the cytoplasm upon entry into mitosis. Also
CC detected in central nucleolar vacuole. {ECO:0000269|PubMed:9819359}.
CC -!- SIMILARITY: Belongs to the RRM U1 A/B'' family. {ECO:0000305}.
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DR EMBL; AC002338; AAC16931.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08363.1; -; Genomic_DNA.
DR EMBL; BT003068; AAO23633.1; -; mRNA.
DR EMBL; AK227609; BAE99600.1; -; mRNA.
DR EMBL; AY087401; AAM64950.1; -; mRNA.
DR PIR; C84706; C84706.
DR RefSeq; NP_180585.1; NM_128579.4.
DR AlphaFoldDB; O22922; -.
DR SMR; O22922; -.
DR BioGRID; 2925; 18.
DR IntAct; O22922; 4.
DR MINT; O22922; -.
DR STRING; 3702.AT2G30260.1; -.
DR PaxDb; O22922; -.
DR PRIDE; O22922; -.
DR ProteomicsDB; 226613; -.
DR EnsemblPlants; AT2G30260.1; AT2G30260.1; AT2G30260.
DR GeneID; 817576; -.
DR Gramene; AT2G30260.1; AT2G30260.1; AT2G30260.
DR KEGG; ath:AT2G30260; -.
DR Araport; AT2G30260; -.
DR TAIR; locus:2065742; AT2G30260.
DR eggNOG; KOG4206; Eukaryota.
DR HOGENOM; CLU_041869_1_1_1; -.
DR OMA; NQTIYVN; -.
DR OrthoDB; 1608132at2759; -.
DR PhylomeDB; O22922; -.
DR PRO; PR:O22922; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22922; baseline and differential.
DR Genevisible; O22922; AT.
DR GO; GO:0015030; C:Cajal body; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0005686; C:U2 snRNP; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000354; P:cis assembly of pre-catalytic spliceosome; TAS:TAIR.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Repeat; Ribonucleoprotein; RNA-binding; Spliceosome.
FT CHAIN 1..232
FT /note="U2 small nuclear ribonucleoprotein B''"
FT /id="PRO_0000416929"
FT DOMAIN 10..89
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 158..232
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 100..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 10
FT /note="Q -> H (in Ref. 5; AAM64950)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="D -> E (in Ref. 5; AAM64950)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 232 AA; 26237 MW; A0066B07B3084E99 CRC64;
MLTADIPPNQ SIYIQNLNER IKKEELKRSL YCLFSQFGRI LDVVALKTPK LRGQAWVTFS
EVTAAGHAVR QMQNFPFYDK PMRLQYAKAK SDCLAKAEGT FVPKDKKRKQ EEKVERKRED
SQRPNTANGP SANGPSANNG VPAPSFQPSG QETMPPNNIL FIQNLPHETT SMMLQLLFEQ
YPGFKEIRMI DAKPGIAFVE YEDDVQASIA MQPLQGFKIT PQNPMVISFA KK
