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 27-MAR-2024, entry version 173. 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; GN 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.Q9XFR5; -. DR iPTMnet; Q9XFR5; -. DR PaxDb; 3702-AT1G09140-1; -. 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; AT1G09140; SR30. DR eggNOG; KOG0105; Eukaryota. DR InParanoid; Q9XFR5; -. DR OMA; PMLRHSP; -. DR OrthoDB; 132255at2759; -. DR PhylomeDB; Q9XFR5; -. DR PRO; PR:Q9XFR5; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; Q9XFR5; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:TAIR. DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell. 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; IEA:UniProtKB-KW. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. DR CDD; cd12602; RRM2_SF2_plant_like; 1. 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 PANTHER; PTHR23003:SF56; NUCLEOLAR PROTEIN 3-RELATED; 1. DR PANTHER; PTHR23003; RNA RECOGNITION MOTIF RRM DOMAIN CONTAINING PROTEIN; 1. DR Pfam; PF00076; RRM_1; 2. DR SMART; SM00360; RRM; 2. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1. DR PROSITE; PS50102; RRM; 2. DR Genevisible; Q9XFR5; AT. 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 //