RU17_ARATH
ID RU17_ARATH Reviewed; 427 AA.
AC Q42404; Q42378;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 170.
DE RecName: Full=U1 small nuclear ribonucleoprotein 70 kDa;
DE Short=U1 snRNP 70 kDa;
DE Short=U1-70K;
DE Short=snRNP70;
GN Name=RNU1; OrderedLocusNames=At3g50670; ORFNames=T3A5.50;
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] (ISOFORM LONG).
RC STRAIN=cv. Columbia; TISSUE=Leaf, and Stem;
RX PubMed=1420366; DOI=10.1016/0167-4781(92)90143-n;
RA Reddy A.S., Czernik A.J., An G., Poovaiah B.W.;
RT "Cloning of the cDNA for U1 small nuclear ribonucleoprotein particle 70K
RT protein from Arabidopsis thaliana.";
RL Biochim. Biophys. Acta 1171:88-92(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS LONG AND SHORT).
RC STRAIN=cv. Columbia; TISSUE=Leaf, and Stem;
RX PubMed=8776903; DOI=10.2307/3870311;
RA Golovkin M., Reddy A.S.;
RT "Structure and expression of a plant U1 snRNP 70K gene: alternative
RT splicing of U1 snRNP 70K pre-mRNAs produces two different transcripts.";
RL Plant Cell 8:1421-1435(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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] (ISOFORM LONG).
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 INTERACTION WITH RSZ21 AND RSZ22.
RX PubMed=9761791; DOI=10.2307/3870762;
RA Golovkin M., Reddy A.S.;
RT "The plant U1 small nuclear ribonucleoprotein particle 70K protein
RT interacts with two novel serine/arginine-rich proteins.";
RL Plant Cell 10:1637-1648(1998).
RN [7]
RP INTERACTION WITH SR45 AND SCL33.
RX PubMed=10593939; DOI=10.1074/jbc.274.51.36428;
RA Golovkin M., Reddy A.S.N.;
RT "An SC35-like protein and a novel serine/arginine-rich protein interact
RT with Arabidopsis U1-70K protein.";
RL J. Biol. Chem. 274:36428-36438(1999).
RN [8]
RP INTERACTION WITH SR34; CYP63 AND CYP95.
RX PubMed=15166240; DOI=10.1074/jbc.m400270200;
RA Lorkovic Z.J., Lopato S., Pexa M., Lehner R., Barta A.;
RT "Interactions of Arabidopsis RS domain containing cyclophilins with SR
RT proteins and U1 and U11 small nuclear ribonucleoprotein-specific proteins
RT suggest their involvement in pre-mRNA Splicing.";
RL J. Biol. Chem. 279:33890-33898(2004).
RN [9]
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 [10]
RP INTERACTION WITH SR45A.
RX PubMed=17556373; DOI=10.1093/pcp/pcm069;
RA Tanabe N., Yoshimura K., Kimura A., Yabuta Y., Shigeoka S.;
RT "Differential expression of alternatively spliced mRNAs of Arabidopsis SR
RT protein homologs, atSR30 and atSR45a, in response to environmental
RT stress.";
RL Plant Cell Physiol. 48:1036-1049(2007).
RN [11]
RP SUBCELLULAR LOCATION, INTERACTION WITH SR45, AND PHOSPHORYLATION.
RX PubMed=18414657; DOI=10.1371/journal.pone.0001953;
RA Ali G.S., Prasad K.V., Hanumappa M., Reddy A.S.;
RT "Analyses of in vivo interaction and mobility of two spliceosomal proteins
RT using FRAP and BiFC.";
RL PLoS ONE 3:E1953-E1953(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, 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).
RN [13]
RP INTERACTION WITH SR45; U2AF35A AND U2AF35B.
RX PubMed=22563826; DOI=10.1111/j.1365-313x.2012.05042.x;
RA Day I.S., Golovkin M., Palusa S.G., Link A., Ali G.S., Thomas J.,
RA Richardson D.N., Reddy A.S.;
RT "Interactions of SR45, an SR-like protein, with spliceosomal proteins and
RT an intronic sequence: insights into regulated splicing.";
RL Plant J. 71:936-947(2012).
CC -!- FUNCTION: Mediates the splicing of pre-mRNA by binding to the loop I
CC region of U1-snRNA.
CC -!- SUBUNIT: Component of the spliceosome. Interacts with CYP63, U2AF35A,
CC U2AF35B, SRZ21, RSZ22, SR34, SR45, SR45A and SCL33.
CC {ECO:0000269|PubMed:10593939, ECO:0000269|PubMed:15166240,
CC ECO:0000269|PubMed:17556373, ECO:0000269|PubMed:18414657,
CC ECO:0000269|PubMed:22563826, ECO:0000269|PubMed:9761791}.
CC -!- INTERACTION:
CC Q42404; O80575: At2g44050; NbExp=3; IntAct=EBI-1633812, EBI-4473692;
CC Q42404; O23160: MYB73; NbExp=3; IntAct=EBI-1633812, EBI-25506855;
CC Q42404; P92964: RS31; NbExp=3; IntAct=EBI-1633812, EBI-927132;
CC Q42404; O81127: RSZ21; NbExp=4; IntAct=EBI-1633812, EBI-927172;
CC Q42404; O81126: RSZ22; NbExp=4; IntAct=EBI-1633812, EBI-1633829;
CC Q42404; Q9SEU4: SCL33; NbExp=3; IntAct=EBI-1633812, EBI-927103;
CC Q42404; Q9SEE9: SR45; NbExp=4; IntAct=EBI-1633812, EBI-1792008;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:15133128,
CC ECO:0000269|PubMed:18414657}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:18414657}. Note=The exchange between speckles and
CC nucleoplasm is sensitive to ongoing transcription and phosphorylation.
CC {ECO:0000269|PubMed:18414657}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=Q42404-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q42404-2; Sequence=VSP_005853, VSP_005854;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Phosphorylated. The association and dissociation with SR45 is not
CC affected by the phosphorylation status (PubMed:18414657).
CC {ECO:0000269|PubMed:18414657}.
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DR EMBL; M93439; AAD12773.1; -; mRNA.
DR EMBL; U52909; AAD12774.1; -; Genomic_DNA.
DR EMBL; U52909; AAD12775.1; -; Genomic_DNA.
DR EMBL; U52910; AAD12776.1; -; mRNA.
DR EMBL; AL132979; CAB62436.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78692.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78693.1; -; Genomic_DNA.
DR EMBL; AY039874; AAK63978.1; -; mRNA.
DR EMBL; AY094003; AAM16264.1; -; mRNA.
DR PIR; S71367; S71367.
DR RefSeq; NP_190636.1; NM_114927.4. [Q42404-1]
DR RefSeq; NP_850676.1; NM_180345.1. [Q42404-2]
DR AlphaFoldDB; Q42404; -.
DR SMR; Q42404; -.
DR BioGRID; 9548; 19.
DR IntAct; Q42404; 12.
DR MINT; Q42404; -.
DR STRING; 3702.AT3G50670.1; -.
DR iPTMnet; Q42404; -.
DR PaxDb; Q42404; -.
DR PRIDE; Q42404; -.
DR ProteomicsDB; 228036; -. [Q42404-1]
DR EnsemblPlants; AT3G50670.1; AT3G50670.1; AT3G50670. [Q42404-1]
DR EnsemblPlants; AT3G50670.2; AT3G50670.2; AT3G50670. [Q42404-2]
DR GeneID; 824230; -.
DR Gramene; AT3G50670.1; AT3G50670.1; AT3G50670. [Q42404-1]
DR Gramene; AT3G50670.2; AT3G50670.2; AT3G50670. [Q42404-2]
DR KEGG; ath:AT3G50670; -.
DR Araport; AT3G50670; -.
DR TAIR; locus:2101714; AT3G50670.
DR eggNOG; KOG0113; Eukaryota.
DR HOGENOM; CLU_045151_2_1_1; -.
DR InParanoid; Q42404; -.
DR OMA; GVAKFMA; -.
DR PhylomeDB; Q42404; -.
DR PRO; PR:Q42404; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q42404; baseline and differential.
DR Genevisible; Q42404; AT.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005685; C:U1 snRNP; IBA:GO_Central.
DR GO; GO:0071004; C:U2-type prespliceosome; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0017069; F:snRNA binding; IBA:GO_Central.
DR GO; GO:0030619; F:U1 snRNA binding; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:TAIR.
DR CDD; cd12236; RRM_snRNP70; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034143; snRNP70_RRM.
DR InterPro; IPR022023; U1snRNP70_N.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF12220; U1snRNP70_N; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; RNA-binding;
KW Spliceosome.
FT CHAIN 1..427
FT /note="U1 small nuclear ribonucleoprotein 70 kDa"
FT /id="PRO_0000081885"
FT DOMAIN 138..216
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 82..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT VAR_SEQ 168..204
FT /note="HLVTDQLTNKPKGYAFIEYMHTRDMKAAYKQADGQKI -> GYSEHSLAGSV
FT RICVMASLSRALCSICFILSTKVFQG (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:8776903"
FT /id="VSP_005853"
FT VAR_SEQ 205..427
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:8776903"
FT /id="VSP_005854"
SQ SEQUENCE 427 AA; 50388 MW; 2B35E824EF35A341 CRC64;
MGDSGDPFLR NPNAAVQARA KVQNRANVLQ LKLMGQSHPT GLTNNLLKLF EPRPPLEYKP
PPEKRKCPPY TGMAQFVSNF AEPGDPEYAP PKPEVELPSQ KRERIHKLRL EKGVEKAAED
LKKYDPNNDP NATGDPYKTL FVSRLNYESS ESKIKREFES YGPIKRVHLV TDQLTNKPKG
YAFIEYMHTR DMKAAYKQAD GQKIDGRRVL VDVERGRTVP NWRPRRLGGG LGTSRVGGGE
EIVGEQQPQG RTSQSEEPSR PREEREKSRE KGKERERSRE LSHEQPRERS RDRPREDKHH
RDRDQGGRDR DRDSRRDRDR TRDRGDRDRR DRDRGRDRTS RDHDRDRSRK KERDYEGGEY
EHEGGGRSRE RDAEYRGEPE ETRGYYEDDQ GDTDRYSHRY DKMEEDDFRY EREYKRSKRS
ESREYVR
