SRS41_ARATH
ID SRS41_ARATH Reviewed; 356 AA.
AC P92966; C0Z344; F4KES0; F4KES2; F4KES3; Q9FJ88;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Serine/arginine-rich splicing factor RS41;
DE Short=At-RSp41;
DE Short=AtRS41;
GN Name=RS41; Synonyms=RSP41; OrderedLocusNames=At5g52040; ORFNames=MSG15.12;
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 1).
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=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239; SER-324; SER-342;
RP SER-347 AND SER-351, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239 AND SER-254, 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 [10]
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 [11]
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 [12]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH RCF3 AND
RP CPL1, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=24146632; DOI=10.1371/journal.pgen.1003875;
RA Chen T., Cui P., Chen H., Ali S., Zhang S., Xiong L.;
RT "A KH-domain RNA-binding protein interacts with FIERY2/CTD phosphatase-like
RT 1 and splicing factors and is important for pre-mRNA splicing in
RT Arabidopsis.";
RL PLoS Genet. 9:E1003875-E1003875(2013).
RN [13]
RP FUNCTION, INTERACTION WITH DRB1/HYL1 AND SE, AND SUBCELLULAR LOCATION.
RX PubMed=26227967; DOI=10.1093/nar/gkv751;
RA Chen T., Cui P., Xiong L.;
RT "The RNA-binding protein HOS5 and serine/arginine-rich proteins RS40 and
RT RS41 participate in miRNA biogenesis in Arabidopsis.";
RL Nucleic Acids Res. 43:8283-8298(2015).
CC -!- FUNCTION: Required for constitutive and alternative pre-mRNA splicing
CC (Probable). Involved in primary miRNA processing and pri-miRNA
CC biogenesis. Binds both intronless and intron-containing pri-miRNAs
CC (PubMed:26227967). {ECO:0000269|PubMed:26227967,
CC ECO:0000305|PubMed:24146632}.
CC -!- SUBUNIT: Component of the spliceosome (Probable). Interacts with RCF3
CC and CPL1 (PubMed:24146632). Interacts with DRB1/HYL1 and SE
CC (PubMed:26227967). {ECO:0000269|PubMed:24146632,
CC ECO:0000269|PubMed:26227967, ECO:0000305}.
CC -!- INTERACTION:
CC P92966; O81127: RSZ21; NbExp=3; IntAct=EBI-4474477, EBI-927172;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24146632,
CC ECO:0000269|PubMed:26227967}. Nucleus speckle
CC {ECO:0000269|PubMed:24146632, ECO:0000269|PubMed:26227967}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P92966-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P92966-2; Sequence=VSP_054983;
CC Name=3;
CC IsoId=P92966-3; Sequence=VSP_054982;
CC Name=4;
CC IsoId=P92966-4; Sequence=VSP_054982, VSP_054983;
CC Name=5;
CC IsoId=P92966-5; Sequence=VSP_054981;
CC -!- TISSUE SPECIFICITY: Leaves, stem, roots and flowers.
CC -!- DISRUPTION PHENOTYPE: Mutant seedlings show increased sensitivity to
CC salt stress and abscisic acid (ABA). {ECO:0000269|PubMed:24146632}.
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. {ECO:0000305|PubMed:17319848}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. RS subfamily.
CC {ECO:0000305}.
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DR EMBL; X99436; CAA67799.1; -; mRNA.
DR EMBL; AB015478; BAB11052.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96162.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96163.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96164.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96165.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68613.1; -; Genomic_DNA.
DR EMBL; AY059133; AAL15239.1; -; mRNA.
DR EMBL; AF370171; AAK43986.1; -; mRNA.
DR EMBL; AK319008; BAH57123.1; -; mRNA.
DR RefSeq; NP_001154773.1; NM_001161301.1. [P92966-5]
DR RefSeq; NP_001154774.1; NM_001161302.1. [P92966-4]
DR RefSeq; NP_001330349.1; NM_001344975.1. [P92966-3]
DR RefSeq; NP_200017.2; NM_124583.4. [P92966-2]
DR RefSeq; NP_851174.1; NM_180843.3. [P92966-1]
DR AlphaFoldDB; P92966; -.
DR SMR; P92966; -.
DR BioGRID; 20524; 16.
DR IntAct; P92966; 2.
DR STRING; 3702.AT5G52040.2; -.
DR iPTMnet; P92966; -.
DR PaxDb; P92966; -.
DR PRIDE; P92966; -.
DR ProteomicsDB; 226740; -. [P92966-1]
DR EnsemblPlants; AT5G52040.1; AT5G52040.1; AT5G52040. [P92966-1]
DR EnsemblPlants; AT5G52040.2; AT5G52040.2; AT5G52040. [P92966-2]
DR EnsemblPlants; AT5G52040.3; AT5G52040.3; AT5G52040. [P92966-5]
DR EnsemblPlants; AT5G52040.4; AT5G52040.4; AT5G52040. [P92966-4]
DR EnsemblPlants; AT5G52040.6; AT5G52040.6; AT5G52040. [P92966-3]
DR GeneID; 835279; -.
DR Gramene; AT5G52040.1; AT5G52040.1; AT5G52040. [P92966-1]
DR Gramene; AT5G52040.2; AT5G52040.2; AT5G52040. [P92966-2]
DR Gramene; AT5G52040.3; AT5G52040.3; AT5G52040. [P92966-5]
DR Gramene; AT5G52040.4; AT5G52040.4; AT5G52040. [P92966-4]
DR Gramene; AT5G52040.6; AT5G52040.6; AT5G52040. [P92966-3]
DR KEGG; ath:AT5G52040; -.
DR Araport; AT5G52040; -.
DR TAIR; locus:2173088; AT5G52040.
DR eggNOG; KOG0106; Eukaryota.
DR InParanoid; P92966; -.
DR OMA; GHRKERT; -.
DR OrthoDB; 1563362at2759; -.
DR PhylomeDB; P92966; -.
DR PRO; PR:P92966; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P92966; baseline and differential.
DR Genevisible; P92966; AT.
DR GO; GO:0010445; C:nuclear dicing body; IDA:TAIR.
DR GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; ISS: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; ISS:TAIR.
DR GO; GO:0031053; P:primary miRNA processing; IGI: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 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..356
FT /note="Serine/arginine-rich splicing factor RS41"
FT /id="PRO_0000081879"
FT DOMAIN 2..74
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 96..167
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REPEAT 267..278
FT /note="1"
FT REPEAT 279..290
FT /note="2"
FT REPEAT 291..302
FT /note="3"
FT REPEAT 303..307
FT /note="4; truncated"
FT REGION 73..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..307
FT /note="4 X 12 AA tandem repeats of [KE]-[GK]-R -[GR]-E-S-R-
FT S-P-P-P-Y"
FT COMPBIAS 168..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P92964"
FT MOD_RES 194
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 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16807317,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9SJA6"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FYB7"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16807317"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16807317"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16807317"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16807317"
FT VAR_SEQ 1..36
FT /note="MKPVFCGNFEYDARESDLERLFRKYGKVERVDMKAG -> MEFAPPRFW
FT (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_054981"
FT VAR_SEQ 1..35
FT /note="MKPVFCGNFEYDARESDLERLFRKYGKVERVDMKA -> MQ (in
FT isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_054982"
FT VAR_SEQ 346
FT /note="E -> ES (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_054983"
FT CONFLICT 132
FT /note="F -> Y (in Ref. 1; CAA67799)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 356 AA; 41282 MW; 36DBBCDFFE42F362 CRC64;
MKPVFCGNFE YDARESDLER LFRKYGKVER VDMKAGFAFV YMEDERDAED AIRALDRFEY
GRTGRRLRVE WTKNDRGGAG RSGGSRRSSS GLRPSKTLFV INFDAQNTRT RDLERHFEPY
GKIVNVRIRR NFAFIQYEAQ EDATRALDAT NSSKLMDKVI SVEYAVKDDD SRGNGYSPER
RRDRSPDRRR RSPSPYRRER GSPDYGRGAS PVAHKRERTS PDYGRGRRSP SPYKRARLSP
DYKRDDRRRE RVASPENGAV RNRSPRKGRG ESRSPPPYEK RRESRSPPPY EKRRESRSPP
PYEKRRERSR SRSKSSPENG QVESPGQIME VEAGRGYDGA DSPIRESPSR SPPAEE
