RS31A_ARATH
ID RS31A_ARATH Reviewed; 250 AA.
AC Q9ZPX8; F4IJ76;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Serine/arginine-rich splicing factor RS31A;
DE Short=At-RS31A;
DE Short=At-RSp31A;
DE Short=AtRS31A;
DE AltName: Full=Arginine/serine-rich splicing factor RS32;
DE Short=At-RSp32;
GN Name=RS31A; Synonyms=RSP31A, RSP32; OrderedLocusNames=At2g46610;
GN ORFNames=F13A10.14;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
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 [6]
RP ALTERNATIVE SPLICING.
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 [7]
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 [8]
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 [9]
RP INTERACTION WITH MOS14.
RX PubMed=21738492; DOI=10.1371/journal.pgen.1002159;
RA Xu S., Zhang Z., Jing B., Gannon P., Ding J., Xu F., Li X., Zhang Y.;
RT "Transportin-SR is required for proper splicing of resistance genes and
RT plant immunity.";
RL PLoS Genet. 7:E1002159-E1002159(2011).
RN [10]
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).
CC -!- FUNCTION: Probably involved in intron recognition and spliceosome
CC assembly.
CC -!- SUBUNIT: Component of the spliceosome (Probable). Interacts with MOS14
CC (PubMed:21738492). {ECO:0000269|PubMed:21738492, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:P92964}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P92964}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ZPX8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ZPX8-2; Sequence=VSP_054996;
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; AC006418; AAD20171.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10728.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10729.1; -; Genomic_DNA.
DR EMBL; AY065237; AAL38713.1; -; mRNA.
DR EMBL; BT000995; AAN41395.1; -; mRNA.
DR EMBL; AK317202; BAH19886.1; -; mRNA.
DR PIR; A84905; A84905.
DR RefSeq; NP_182184.1; NM_130226.6. [Q9ZPX8-1]
DR RefSeq; NP_973702.1; NM_201973.6. [Q9ZPX8-2]
DR AlphaFoldDB; Q9ZPX8; -.
DR SMR; Q9ZPX8; -.
DR BioGRID; 4608; 2.
DR IntAct; Q9ZPX8; 1.
DR STRING; 3702.AT2G46610.1; -.
DR iPTMnet; Q9ZPX8; -.
DR PaxDb; Q9ZPX8; -.
DR PRIDE; Q9ZPX8; -.
DR ProteomicsDB; 228101; -. [Q9ZPX8-1]
DR EnsemblPlants; AT2G46610.1; AT2G46610.1; AT2G46610. [Q9ZPX8-1]
DR EnsemblPlants; AT2G46610.2; AT2G46610.2; AT2G46610. [Q9ZPX8-2]
DR GeneID; 819273; -.
DR Gramene; AT2G46610.1; AT2G46610.1; AT2G46610. [Q9ZPX8-1]
DR Gramene; AT2G46610.2; AT2G46610.2; AT2G46610. [Q9ZPX8-2]
DR KEGG; ath:AT2G46610; -.
DR Araport; AT2G46610; -.
DR TAIR; locus:2039975; AT2G46610.
DR eggNOG; KOG0106; Eukaryota.
DR HOGENOM; CLU_043462_0_0_1; -.
DR InParanoid; Q9ZPX8; -.
DR OMA; VRRSERC; -.
DR OrthoDB; 1563362at2759; -.
DR PhylomeDB; Q9ZPX8; -.
DR PRO; PR:Q9ZPX8; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZPX8; baseline and differential.
DR Genevisible; Q9ZPX8; AT.
DR GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
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 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..250
FT /note="Serine/arginine-rich splicing factor RS31A"
FT /id="PRO_0000429602"
FT DOMAIN 2..74
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 95..166
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 170..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P92964"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P92964"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P92965"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FYB7"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P92966"
FT VAR_SEQ 1..35
FT /note="MRHVYVGNFDYDTRHSDLERLFSKFGRVKRVDMKS -> MYTSLHIDA (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_054996"
SQ SEQUENCE 250 AA; 29681 MW; D844136FFD2686DA CRC64;
MRHVYVGNFD YDTRHSDLER LFSKFGRVKR VDMKSGYAFV YFEDERDAED AIRRTDNTTF
GYGRRKLSVE WAKDFQGERG KPRDGKAVSN QRPTKTLFVI NFDPIRTRER DMERHFEPYG
KVLNVRMRRN FAFVQFATQE DATKALDSTH NSKLLDKVVS VEYALREAGE REDRYAGSRR
RRSPSPVYRR RPSPDYTRRR SPEYDRYKGP APYERRKSPD YGRRSSDYGR ARARSPGYDR
SRSPIQRARG
