SR34_ARATH
ID SR34_ARATH Reviewed; 303 AA.
AC O22315; O22314; Q39201; Q564E1; Q8L7P1;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 157.
DE RecName: Full=Serine/arginine-rich-splicing factor SR34;
DE Short=At-SR34;
DE Short=At-SRp34;
DE Short=AtSR34;
DE AltName: Full=Pre-mRNA-splicing factor SF2;
DE AltName: Full=SR1 protein;
GN Name=SR34; Synonyms=SF2, SR1, SRP34; OrderedLocusNames=At1g02840;
GN ORFNames=F22D16.16, F22D16_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] (ISOFORM 1).
RX PubMed=7644475; DOI=10.1073/pnas.92.17.7672;
RA Lazar G., Schaal T., Maniatis T., Goodman H.M.;
RT "Identification of a plant serine-arginine-rich protein similar to the
RT mammalian splicing factor SF2/ASF.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:7672-7676(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Su C.-L., Schuler M.A.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, 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 [9]
RP PHOSPHORYLATION.
RX PubMed=10652154; DOI=10.1046/j.1365-313x.2000.00657.x;
RA Savaldi-Goldstein S., Sessa G., Fluhr R.;
RT "The ethylene-inducible PK12 kinase mediates the phosphorylation of SR
RT splicing factors.";
RL Plant J. 21:91-96(2000).
RN [10]
RP ALTERNATIVE SPLICING.
RX PubMed=10809003; DOI=10.1023/a:1006394207479;
RA Lazar G., Goodman H.M.;
RT "The Arabidopsis splicing factor SR1 is regulated by alternative
RT splicing.";
RL Plant Mol. Biol. 42:571-581(2000).
RN [11]
RP INTERACTION WITH RS2Z33, AND TISSUE SPECIFICITY.
RX PubMed=12176998; DOI=10.1074/jbc.m206455200;
RA Lopato S., Forstner C., Kalyna M., Hilscher J., Langhammer U., Korakod L.,
RA Zdravko J., Barta A.;
RT "Network of interactions of a novel plant-specific Arg/Ser-rich protein,
RT atRSZ33, with atSC35-like splicing factors.";
RL J. Biol. Chem. 277:39989-39998(2002).
RN [12]
RP INTERACTION WITH SR34; CYP63 AND CYP95, AND PHOSPHORYLATION.
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 [13]
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 [14]
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 [15]
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 [16]
RP SUBCELLULAR LOCATION.
RX PubMed=16895966; DOI=10.1242/jcs.03144;
RA Ali G.S., Reddy A.S.;
RT "ATP, phosphorylation and transcription regulate the mobility of plant
RT splicing factors.";
RL J. Cell Sci. 119:3527-3538(2006).
RN [17]
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 [18]
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 [19]
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 [20]
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 [21]
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: General splicing factor. Can promote splice site selection in
CC vitro presumably by antagonizing the effects of the A1 heterogeneous
CC nuclear ribonucleoprotein. May have an essential function during early
CC plant development. {ECO:0000269|PubMed:10215626}.
CC -!- SUBUNIT: Component of the spliceosome. Interacts with SNRNP35, RS2Z33,
CC SR34, CYP59, CYP63 and CYP95. The binding to CYP63 is phosphorylation-
CC dependent (PubMed:15166240). Interacts with MOS14 (PubMed:21738492).
CC {ECO:0000269|PubMed:12176998, ECO:0000269|PubMed:15166240,
CC ECO:0000269|PubMed:15987817, ECO:0000269|PubMed:16497658,
CC ECO:0000269|PubMed:21738492}.
CC -!- INTERACTION:
CC O22315; Q9LY75: CYP63; NbExp=3; IntAct=EBI-927464, EBI-2360522;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:15034145,
CC ECO:0000269|PubMed:15686520, ECO:0000269|PubMed:16895966}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:15034145, ECO:0000269|PubMed:15686520,
CC ECO:0000269|PubMed:16895966}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=SF2A;
CC IsoId=O22315-1; Sequence=Displayed;
CC Name=2; Synonyms=SF2B;
CC IsoId=O22315-2; Sequence=VSP_005859, VSP_005860;
CC Name=3;
CC IsoId=O22315-3; Sequence=VSP_054984, VSP_054985;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10215626,
CC ECO:0000269|PubMed:12176998, ECO:0000269|PubMed:15034145}.
CC -!- PTM: Extensively phosphorylated on serine residues in the RS domain.
CC {ECO:0000269|PubMed:10215626, ECO:0000269|PubMed:10652154,
CC ECO:0000269|PubMed:15166240}.
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 and hormones (PubMed:10215626,
CC PubMed:17319848). {ECO:0000305|PubMed:10215626,
CC ECO:0000305|PubMed:17319848}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. SR subfamily.
CC {ECO:0000305}.
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DR EMBL; M98340; AAA32856.1; -; mRNA.
DR EMBL; AF001035; AAB71385.1; -; Genomic_DNA.
DR EMBL; AF001035; AAB71386.1; -; Genomic_DNA.
DR EMBL; AC009525; AAF02881.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27477.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27478.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27479.2; -; Genomic_DNA.
DR EMBL; CP002684; ANM58907.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58908.1; -; Genomic_DNA.
DR EMBL; AK118379; BAC42991.1; -; mRNA.
DR EMBL; AY128338; AAM91541.1; -; mRNA.
DR EMBL; BT006316; AAP13424.1; -; mRNA.
DR EMBL; AY085920; AAM63132.1; -; mRNA.
DR PIR; F86158; F86158.
DR PIR; S71185; S71185.
DR RefSeq; NP_001318908.1; NM_001331357.1. [O22315-2]
DR RefSeq; NP_001321307.1; NM_001331358.1. [O22315-2]
DR RefSeq; NP_001321308.1; NM_001331359.1. [O22315-2]
DR RefSeq; NP_850933.1; NM_180602.2. [O22315-1]
DR RefSeq; NP_850934.1; NM_180603.1. [O22315-3]
DR AlphaFoldDB; O22315; -.
DR SMR; O22315; -.
DR BioGRID; 24497; 15.
DR IntAct; O22315; 11.
DR STRING; 3702.AT1G02840.1; -.
DR iPTMnet; O22315; -.
DR PaxDb; O22315; -.
DR PRIDE; O22315; -.
DR ProteomicsDB; 226858; -. [O22315-1]
DR EnsemblPlants; AT1G02840.1; AT1G02840.1; AT1G02840. [O22315-1]
DR EnsemblPlants; AT1G02840.2; AT1G02840.2; AT1G02840. [O22315-3]
DR EnsemblPlants; AT1G02840.3; AT1G02840.3; AT1G02840. [O22315-2]
DR EnsemblPlants; AT1G02840.4; AT1G02840.4; AT1G02840. [O22315-2]
DR EnsemblPlants; AT1G02840.5; AT1G02840.5; AT1G02840. [O22315-2]
DR GeneID; 839262; -.
DR Gramene; AT1G02840.1; AT1G02840.1; AT1G02840. [O22315-1]
DR Gramene; AT1G02840.2; AT1G02840.2; AT1G02840. [O22315-3]
DR Gramene; AT1G02840.3; AT1G02840.3; AT1G02840. [O22315-2]
DR Gramene; AT1G02840.4; AT1G02840.4; AT1G02840. [O22315-2]
DR Gramene; AT1G02840.5; AT1G02840.5; AT1G02840. [O22315-2]
DR KEGG; ath:AT1G02840; -.
DR Araport; AT1G02840; -.
DR TAIR; locus:2024770; AT1G02840.
DR eggNOG; KOG0105; Eukaryota.
DR HOGENOM; CLU_012062_34_0_1; -.
DR InParanoid; O22315; -.
DR OMA; YGMSSFR; -.
DR OrthoDB; 1321443at2759; -.
DR PhylomeDB; O22315; -.
DR PRO; PR:O22315; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O22315; baseline and differential.
DR Genevisible; O22315; AT.
DR GO; GO:0035061; C:interchromatin granule; IDA:TAIR.
DR GO; GO:0016607; C:nuclear speck; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; ISS:TAIR.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
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; 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; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Spliceosome.
FT CHAIN 1..303
FT /note="Serine/arginine-rich-splicing factor SR34"
FT /id="PRO_0000081917"
FT DOMAIN 7..82
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 119..197
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 81..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..241
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 267..285
FT /note="SRSRSRSPLPSVQKEGSKS -> WITVETLDHLDHNIISGFL (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_054984"
FT VAR_SEQ 267..272
FT /note="SRSRSR -> YGFTYD (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005859"
FT VAR_SEQ 273..303
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005860"
FT VAR_SEQ 286..303
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_054985"
FT CONFLICT 125
FT /note="G -> W (in Ref. 1; AAA32856)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="P -> A (in Ref. 1; AAA32856)"
FT /evidence="ECO:0000305"
FT CONFLICT 139..140
FT /note="MR -> IA (in Ref. 1; AAA32856)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 303 AA; 33729 MW; 6530F9CB628B8EFA CRC64;
MSSRSSRTVY VGNLPGDIRE REVEDLFSKY GPVVQIDLKV PPRPPGYAFV EFDDARDAED
AIHGRDGYDF DGHRLRVELA HGGRRSSDDT RGSFNGGGRG GGRGRGDGGS RGPSRRSEFR
VLVTGLPSSA SWQDLKDHMR KGGDVCFSQV YRDARGTTGV VDYTCYEDMK YALKKLDDTE
FRNAFSNGYV RVREYDSRKD SRSPSRGRSY SKSRSRSRGR SVSRSRSRSR SRSRSPKAKS
SRRSPAKSTS RSPGPRSKSR SPSPRRSRSR SRSPLPSVQK EGSKSPSKPS PAKSPIHTRS
PSR
