SR30_ARATH
ID SR30_ARATH Reviewed; 268 AA.
AC Q9XFR5; Q949S8; Q9XFR6;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 165.
DE RecName: Full=Serine/arginine-rich splicing factor SR30;
DE Short=At-SR30;
DE Short=At-SRp30;
DE Short=AtSR30;
DE AltName: Full=SF2/ASF-like splicing modulator Srp30;
DE AltName: Full=Serine-arginine rich RNA binding protein 30;
GN Name=SR30; Synonyms=SRP30; OrderedLocusNames=At1g09140; ORFNames=T12M4.19;
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 [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), FUNCTION,
RP ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND PHOSPHORYLATION.
RX PubMed=10215626; DOI=10.1101/gad.13.8.987;
RA Lopato S., Kalyna M., Dorner S., Kobayashi R., Krainer A.R., Barta A.;
RT "atSRp30, one of two SF2/ASF-like proteins from Arabidopsis thaliana,
RT regulates splicing of specific plant genes.";
RL Genes Dev. 13:987-1001(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] (ISOFORM 1).
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 INTERACTION WITH CYP63.
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 [6]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=15034145; DOI=10.1091/mbc.e04-02-0100;
RA Fang Y., Hearn S., Spector D.L.;
RT "Tissue-specific expression and dynamic organization of SR splicing factors
RT in Arabidopsis.";
RL Mol. Biol. Cell 15:2664-2673(2004).
RN [7]
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 [8]
RP INTERACTION WITH SNRNP35.
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 [9]
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 [10]
RP ALTERNATIVE SPLICING, AND INDUCTION BY HIGH-LIGHT; PARAQUAT; COLD AND SALT
RP STRESS.
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 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 [12]
RP ALTERNATIVE SPLICING.
RX PubMed=19734266; DOI=10.1104/pp.109.141705;
RA Chung T., Wang D., Kim C.S., Yadegari R., Larkins B.A.;
RT "Plant SMU-1 and SMU-2 homologues regulate pre-mRNA splicing and multiple
RT aspects of development.";
RL Plant Physiol. 151:1498-1512(2009).
RN [13]
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 [14]
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 [15]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=23132568; DOI=10.1271/bbb.120425;
RA Mori T., Yoshimura K., Nosaka R., Sakuyama H., Koike Y., Tanabe N.,
RA Maruta T., Tamoi M., Shigeoka S.;
RT "Subcellular and subnuclear distribution of high-light responsive
RT serine/arginine-rich proteins, atSR45a and atSR30, in Arabidopsis
RT thaliana.";
RL Biosci. Biotechnol. Biochem. 76:2075-2081(2012).
RN [16]
RP INDUCTION.
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: Regulatory splicing factor that modulates alternative
CC splicing and gene expression in specific cell types. Autoregulates its
CC own expression. Probably involved in intron recognition and spliceosome
CC assembly. {ECO:0000269|PubMed:10215626}.
CC -!- SUBUNIT: Component of the spliceosome. Interacts with SNRNP35, CYP59
CC and CYP63. {ECO:0000269|PubMed:15166240, ECO:0000269|PubMed:15987817,
CC ECO:0000269|PubMed:16497658}.
CC -!- INTERACTION:
CC Q9XFR5; Q9LY75: CYP63; NbExp=4; IntAct=EBI-1540237, EBI-2360522;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:15034145,
CC ECO:0000269|PubMed:15133128, ECO:0000269|PubMed:23132568}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:15034145, ECO:0000269|PubMed:15133128,
CC ECO:0000269|PubMed:23132568}. Cytoplasm {ECO:0000269|PubMed:23132568}.
CC Note=Inhibition of phosphorylation causes suppression of nuclear
CC localization. {ECO:0000269|PubMed:23132568}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9XFR5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9XFR5-2; Sequence=VSP_054988, VSP_054989;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10215626,
CC ECO:0000269|PubMed:15034145}.
CC -!- INDUCTION: Up-regulated by paraquat, high salt and early after high-
CC light irradiation. Down-regulated by cold.
CC {ECO:0000269|PubMed:17319848, ECO:0000269|PubMed:17556373,
CC ECO:0000269|PubMed:24763593}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:10215626,
CC ECO:0000269|PubMed:23132568}.
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 stress treatment (PubMed:10215626, PubMed:17556373,
CC PubMed:17319848) or light regimes (PubMed:24763593).
CC {ECO:0000305|PubMed:10215626, ECO:0000305|PubMed:17319848,
CC ECO:0000305|PubMed:17556373, 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. SR subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ131214; CAB42557.1; -; Genomic_DNA.
DR EMBL; AJ131214; CAB42558.1; -; Genomic_DNA.
DR EMBL; AC003114; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE28400.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28401.1; -; Genomic_DNA.
DR EMBL; AY150486; AAN13011.1; -; mRNA.
DR EMBL; AY050912; AAK93589.2; -; mRNA.
DR RefSeq; NP_172386.3; NM_100783.6. [Q9XFR5-1]
DR RefSeq; NP_683288.2; NM_148447.4. [Q9XFR5-2]
DR AlphaFoldDB; Q9XFR5; -.
DR SMR; Q9XFR5; -.
DR BioGRID; 22674; 14.
DR IntAct; Q9XFR5; 13.
DR STRING; 3702.AT1G09140.1; -.
DR iPTMnet; Q9XFR5; -.
DR PaxDb; Q9XFR5; -.
DR PRIDE; Q9XFR5; -.
DR ProteomicsDB; 226765; -. [Q9XFR5-1]
DR EnsemblPlants; AT1G09140.1; AT1G09140.1; AT1G09140. [Q9XFR5-1]
DR EnsemblPlants; AT1G09140.2; AT1G09140.2; AT1G09140. [Q9XFR5-2]
DR GeneID; 837433; -.
DR Gramene; AT1G09140.1; AT1G09140.1; AT1G09140. [Q9XFR5-1]
DR Gramene; AT1G09140.2; AT1G09140.2; AT1G09140. [Q9XFR5-2]
DR KEGG; ath:AT1G09140; -.
DR Araport; AT1G09140; -.
DR TAIR; locus:2195346; AT1G09140.
DR eggNOG; KOG0105; Eukaryota.
DR InParanoid; Q9XFR5; -.
DR OMA; DHSGGDR; -.
DR OrthoDB; 1321443at2759; -.
DR PhylomeDB; Q9XFR5; -.
DR PRO; PR:Q9XFR5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9XFR5; baseline and differential.
DR Genevisible; Q9XFR5; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
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; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Spliceosome.
FT CHAIN 1..268
FT /note="Serine/arginine-rich splicing factor SR30"
FT /id="PRO_0000429595"
FT DOMAIN 7..82
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 109..187
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 186..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P92964"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P92965"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VYA5"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VYA5"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P92964"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FYB7"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P92966"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9SJA6"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P92965"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FYB7"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P92966"
FT VAR_SEQ 247..256
FT /note="QSRSKSRSRS -> GSLLRAGDWI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10215626"
FT /id="VSP_054988"
FT VAR_SEQ 257..268
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10215626"
FT /id="VSP_054989"
FT CONFLICT 110
FT /note="R -> H (in Ref. 4; AAK93589)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="S -> T (in Ref. 4; AAK93589)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 268 AA; 30386 MW; 73BDC3534A8F9AC4 CRC64;
MSSRWNRTIY VGNLPGDIRK CEVEDLFYKY GPIVDIDLKI PPRPPGYAFV EFEDPRDADD
AIYGRDGYDF DGCRLRVEIA HGGRRFSPSV DRYSSSYSAS RAPSRRSDYR VLVTGLPPSA
SWQDLKDHMR KAGDVCFSEV FPDRKGMSGV VDYSNYDDMK YAIRKLDATE FRNAFSSAYI
RVREYESRSV SRSPDDSKSY RSRSRSRGPS CSYSSKSRSV SPARSISPRS RPLSRSRSLY
SSVSRSQSRS KSRSRSRSNS PVSPVISG
