SRS31_ARATH
ID SRS31_ARATH Reviewed; 264 AA.
AC P92964; Q944A4; Q9M278;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 25-MAY-2022, entry version 163.
DE RecName: Full=Serine/arginine-rich splicing factor RS31;
DE Short=At-RSp31;
DE Short=AtRS31;
GN Name=RS31; Synonyms=RSP31; OrderedLocusNames=At3g61860; ORFNames=F21F14.30;
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].
RC STRAIN=cv. Columbia;
RX PubMed=8989882; DOI=10.2307/3870466;
RA Lopato S., Waigmann E., Barta A.;
RT "Characterization of a novel arginine/serine-rich splicing factor in
RT Arabidopsis.";
RL Plant Cell 8:2255-2264(1996).
RN [2]
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 [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 SUBCELLULAR LOCATION.
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 [6]
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 [7]
RP SUBCELLULAR LOCATION.
RX PubMed=15686520; DOI=10.1111/j.1365-313x.2004.02321.x;
RA Tillemans V., Dispa L., Remacle C., Collinge M., Motte P.;
RT "Functional distribution and dynamics of Arabidopsis SR splicing factors in
RT living plant cells.";
RL Plant J. 41:567-582(2005).
RN [8]
RP ALTERNATIVE SPLICING.
RX PubMed=16520337; DOI=10.1093/molbev/msj118;
RA Iida K., Go M.;
RT "Survey of conserved alternative splicing events of mRNAs encoding SR
RT proteins in land plants.";
RL Mol. Biol. Evol. 23:1085-1094(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16807317; DOI=10.1093/nar/gkl429;
RA de la Fuente van Bentem S., Anrather D., Roitinger E., Djamei A.,
RA Hufnagl T., Barta A., Csaszar E., Dohnal I., Lecourieux D., Hirt H.;
RT "Phosphoproteomics reveals extensive in vivo phosphorylation of Arabidopsis
RT proteins involved in RNA metabolism.";
RL Nucleic Acids Res. 34:3267-3278(2006).
RN [10]
RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=16936312; DOI=10.1093/nar/gkl570;
RA Kalyna M., Lopato S., Voronin V., Barta A.;
RT "Evolutionary conservation and regulation of particular alternative
RT splicing events in plant SR proteins.";
RL Nucleic Acids Res. 34:4395-4405(2006).
RN [11]
RP INTERACTION WITH CYP59.
RX PubMed=16497658; DOI=10.1261/rna.2226106;
RA Gullerova M., Barta A., Lorkovic Z.J.;
RT "AtCyp59 is a multidomain cyclophilin from Arabidopsis thaliana that
RT interacts with SR proteins and the C-terminal domain of the RNA polymerase
RT II.";
RL RNA 12:631-643(2006).
RN [12]
RP ALTERNATIVE SPLICING, AND INDUCTION.
RX PubMed=17319848; DOI=10.1111/j.1365-313x.2006.03020.x;
RA Palusa S.G., Ali G.S., Reddy A.S.;
RT "Alternative splicing of pre-mRNAs of Arabidopsis serine/arginine-rich
RT proteins: regulation by hormones and stresses.";
RL Plant J. 49:1091-1107(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181; SER-183 AND SER-215, AND
RP IDENTIFICATION BY 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 [14]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=20884799; DOI=10.1105/tpc.110.078352;
RA Barta A., Kalyna M., Reddy A.S.;
RT "Implementing a rational and consistent nomenclature for serine/arginine-
RT rich protein splicing factors (SR proteins) in plants.";
RL Plant Cell 22:2926-2929(2010).
RN [15]
RP GENE FAMILY.
RX PubMed=21935421; DOI=10.1371/journal.pone.0024542;
RA Richardson D.N., Rogers M.F., Labadorf A., Ben-Hur A., Guo H.,
RA Paterson A.H., Reddy A.S.N.;
RT "Comparative analysis of serine/arginine-rich proteins across 27
RT eukaryotes: insights into sub-family classification and extent of
RT alternative splicing.";
RL PLoS ONE 6:E24542-E24542(2011).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=23454656; DOI=10.1016/j.febslet.2013.02.041;
RA Baldwin K.L., Dinh E.M., Hart B.M., Masson P.H.;
RT "CACTIN is an essential nuclear protein in Arabidopsis and may be
RT associated with the eukaryotic spliceosome.";
RL FEBS Lett. 587:873-879(2013).
RN [17]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24763593; DOI=10.1126/science.1250322;
RA Petrillo E., Herz M.A., Fuchs A., Reifer D., Fuller J., Yanovsky M.J.,
RA Simpson C., Brown J.W., Barta A., Kalyna M., Kornblihtt A.R.;
RT "A chloroplast retrograde signal regulates nuclear alternative splicing.";
RL Science 344:427-430(2014).
CC -!- FUNCTION: Required for constitutive and alternative pre-mRNA splicing.
CC -!- SUBUNIT: Component of the spliceosome. Interacts with CYP59.
CC {ECO:0000269|PubMed:16497658}.
CC -!- INTERACTION:
CC P92964; P51568: AFC3; NbExp=3; IntAct=EBI-927132, EBI-25519318;
CC P92964; Q42404: RNU1; NbExp=3; IntAct=EBI-927132, EBI-1633812;
CC P92964; O81127: RSZ21; NbExp=5; IntAct=EBI-927132, EBI-927172;
CC P92964; Q8VY74: SNRNP35; NbExp=4; IntAct=EBI-927132, EBI-927038;
CC P92964; Q84TH4: SR45A; NbExp=3; IntAct=EBI-927132, EBI-25519389;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:14740228,
CC ECO:0000269|PubMed:15133128, ECO:0000269|PubMed:15686520,
CC ECO:0000269|PubMed:23454656}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:14740228, ECO:0000269|PubMed:15133128}. Note=In
CC meristematic cells, no apparent accumulation in foci.
CC {ECO:0000269|PubMed:14740228}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P92964-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Highly expressed in roots and flowers. A presumably
CC longer alternatively spliced form is found in leaves, stems and
CC flowers. {ECO:0000269|PubMed:16936312}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:24763593}.
CC -!- MISCELLANEOUS: The splicing pattern of the pre-mRNA is regulated in a
CC tissue-specific manner and by development, and changes in response to
CC various types of abiotic stresses (PubMed:17319848) or light regimes
CC (PubMed:24763593). This alternative splicing event is regulated by
CC RS2Z33 and is not autoregulated (PubMed:16936312).
CC {ECO:0000305|PubMed:16936312, ECO:0000305|PubMed:17319848,
CC ECO:0000305|PubMed:24763593}.
CC -!- MISCELLANEOUS: A mobile signal generated in the leaves triggers root
CC alternative splicing responses to light. {ECO:0000305|PubMed:24763593}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. RS subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB71893.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X99435; CAA67798.1; -; mRNA.
DR EMBL; AL138642; CAB71893.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE80270.1; -; Genomic_DNA.
DR EMBL; AF439831; AAL27502.1; -; mRNA.
DR EMBL; AY125565; AAM78075.1; -; mRNA.
DR PIR; T47978; T47978.
DR PIR; T51304; T51304.
DR RefSeq; NP_567120.1; NM_116051.4. [P92964-1]
DR AlphaFoldDB; P92964; -.
DR SMR; P92964; -.
DR BioGRID; 10673; 9.
DR IntAct; P92964; 10.
DR MINT; P92964; -.
DR STRING; 3702.AT3G61860.1; -.
DR iPTMnet; P92964; -.
DR PaxDb; P92964; -.
DR PRIDE; P92964; -.
DR ProteomicsDB; 226738; -. [P92964-1]
DR EnsemblPlants; AT3G61860.1; AT3G61860.1; AT3G61860. [P92964-1]
DR GeneID; 825359; -.
DR Gramene; AT3G61860.1; AT3G61860.1; AT3G61860. [P92964-1]
DR KEGG; ath:AT3G61860; -.
DR Araport; AT3G61860; -.
DR TAIR; locus:2079502; AT3G61860.
DR eggNOG; KOG0106; Eukaryota.
DR HOGENOM; CLU_043462_0_0_1; -.
DR InParanoid; P92964; -.
DR OMA; ECTHMSE; -.
DR PhylomeDB; P92964; -.
DR PRO; PR:P92964; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P92964; baseline and differential.
DR Genevisible; P92964; AT.
DR GO; GO:0016607; C:nuclear speck; IDA:TAIR.
DR GO; GO:0005681; C:spliceosomal complex; TAS:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:TAIR.
DR GO; GO:0008380; P:RNA splicing; NAS:TAIR.
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 InterPro; IPR029537; RSP31/31A.
DR PANTHER; PTHR23147:SF146; PTHR23147:SF146; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Spliceosome.
FT CHAIN 1..264
FT /note="Serine/arginine-rich splicing factor RS31"
FT /id="PRO_0000081877"
FT DOMAIN 2..74
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 93..164
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 166..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P92965"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9SJA6"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P92965"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FYB7"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P92966"
FT CONFLICT 66
FT /note="R -> K (in Ref. 1; CAA67798)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 264 AA; 31155 MW; 445FD2E4A5E0C203 CRC64;
MRPVFVGNFE YETRQSDLER LFDKYGRVDR VDMKSGYAFV YFEDERDAED AIRKLDNFPF
GYEKRRLSVE WAKGERGRPR GDAKAPSNLK PTKTLFVINF DPIRTKEHDI EKHFEPYGKV
TNVRIRRNFS FVQFETQEDA TKALEATQRS KILDRVVSVE YALKDDDERD DRNGGRSPRR
SLSPVYRRRP SPDYGRRPSP GQGRRPSPDY GRARSPEYDR YKGPAAYERR RSPDYGRRSS
DYGRQRSPGY DRYRSRSPVP RGRP
