SR45_ARATH
ID SR45_ARATH Reviewed; 414 AA.
AC Q9SEE9; F4I4H8; Q5E925; Q94AS1;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 161.
DE RecName: Full=Serine/arginine-rich splicing factor SR45 {ECO:0000303|PubMed:10593939};
DE Short=At-SR45 {ECO:0000303|PubMed:10593939};
DE Short=AtSR45 {ECO:0000303|PubMed:10593939};
DE AltName: Full=Serine/arginine-rich ribonucleoprotein 1 {ECO:0000303|PubMed:19435936};
GN Name=SR45 {ECO:0000303|PubMed:10593939};
GN Synonyms=RNPS1 {ECO:0000303|PubMed:19435936};
GN OrderedLocusNames=At1g16610 {ECO:0000312|Araport:AT1G16610};
GN ORFNames=F19K19.9 {ECO:0000312|EMBL:AAG10821.1};
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), INTERACTION WITH AFC2; RNU1 AND
RP SCL33, PHOSPHORYLATION BY AFC2, AND TISSUE SPECIFICITY.
RX PubMed=10593939; DOI=10.1074/jbc.274.51.36428;
RA Golovkin M., Reddy A.S.N.;
RT "An SC35-like protein and a novel serine/arginine-rich protein interact
RT with Arabidopsis U1-70K protein.";
RL J. Biol. Chem. 274:36428-36438(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION, TISSUE SPECIFICITY, AND INTERACTION
RP WITH RNU1.
RX PubMed=14675452; DOI=10.1046/j.1365-313x.2003.01932.x;
RA Ali G.S., Golovkin M., Reddy A.S.N.;
RT "Nuclear localization and in vivo dynamics of a plant-specific
RT serine/arginine-rich protein.";
RL Plant J. 36:883-893(2003).
RN [7]
RP REVIEW.
RX PubMed=15270675; DOI=10.1042/bst0320561;
RA Kalyna M., Barta A.;
RT "A plethora of plant serine/arginine-rich proteins: redundancy or evolution
RT of novel gene functions?";
RL Biochem. Soc. Trans. 32:561-564(2004).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [10]
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 [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=17534421; DOI=10.1371/journal.pone.0000471;
RA Ali G.S., Palusa S.G., Golovkin M., Prasad J., Manley J.L., Reddy A.S.;
RT "Regulation of plant developmental processes by a novel splicing factor.";
RL PLoS ONE 2:E471-E471(2007).
RN [12]
RP ALTERNATIVE SPLICING.
RX PubMed=18402682; DOI=10.1186/1471-2164-9-159;
RA Schindler S., Szafranski K., Hiller M., Ali G.S., Palusa S.G., Backofen R.,
RA Platzer M., Reddy A.S.N.;
RT "Alternative splicing at NAGNAG acceptors in Arabidopsis thaliana SR and
RT SR-related protein-coding genes.";
RL BMC Genomics 9:159-159(2008).
RN [13]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH RNU1.
RX PubMed=18414657; DOI=10.1371/journal.pone.0001953;
RA Ali G.S., Prasad K.V., Hanumappa M., Reddy A.S.;
RT "Analyses of in vivo interaction and mobility of two spliceosomal proteins
RT using FRAP and BiFC.";
RL PLoS ONE 3:E1953-E1953(2008).
RN [14]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=19435936; DOI=10.1105/tpc.108.060434;
RA Koroleva O.A., Calder G., Pendle A.F., Kim S.H., Lewandowska D.,
RA Simpson C.G., Jones I.M., Brown J.W.S., Shaw P.J.;
RT "Dynamic behavior of Arabidopsis eIF4A-III, putative core protein of exon
RT junction complex: fast relocation to nucleolus and splicing speckles under
RT hypoxia.";
RL Plant Cell 21:1592-1606(2009).
RN [15]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF 218-THR-SER-219, TISSUE
RP SPECIFICITY, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, AND INDUCTION BY
RP ABIOTIC STRESSES.
RX PubMed=19403727; DOI=10.1104/pp.109.138180;
RA Zhang X.-N., Mount S.M.;
RT "Two alternatively spliced isoforms of the Arabidopsis SR45 protein have
RT distinct roles during normal plant development.";
RL Plant Physiol. 150:1450-1458(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-256, 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 [17]
RP GENE FAMILY.
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 [18]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=20699397; DOI=10.1104/pp.110.155523;
RA Carvalho R.F., Carvalho S.D., Duque P.;
RT "The plant-specific SR45 protein negatively regulates glucose and ABA
RT signaling during early seedling development in Arabidopsis.";
RL Plant Physiol. 154:772-783(2010).
RN [19]
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 [20]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22274613; DOI=10.4161/epi.7.1.18782;
RA Ausin I., Greenberg M.V., Li C.F., Jacobsen S.E.;
RT "The splicing factor SR45 affects the RNA-directed DNA methylation pathway
RT in Arabidopsis.";
RL Epigenetics 7:29-33(2012).
RN [21]
RP INTERACTION WITH SKIP.
RX PubMed=22942380; DOI=10.1105/tpc.112.100081;
RA Wang X., Wu F., Xie Q., Wang H., Wang Y., Yue Y., Gahura O., Ma S., Liu L.,
RA Cao Y., Jiao Y., Puta F., McClung C.R., Xu X., Ma L.;
RT "SKIP is a component of the spliceosome linking alternative splicing and
RT the circadian clock in Arabidopsis.";
RL Plant Cell 24:3278-3295(2012).
RN [22]
RP FUNCTION, AND INTERACTION WITH RNU1; U2AF35A AND U2AF35B.
RX PubMed=22563826; DOI=10.1111/j.1365-313x.2012.05042.x;
RA Day I.S., Golovkin M., Palusa S.G., Link A., Ali G.S., Thomas J.,
RA Richardson D.N., Reddy A.S.;
RT "Interactions of SR45, an SR-like protein, with spliceosomal proteins and
RT an intronic sequence: insights into regulated splicing.";
RL Plant J. 71:936-947(2012).
RN [23]
RP SUBCELLULAR LOCATION.
RX PubMed=23454656; DOI=10.1016/j.febslet.2013.02.041;
RA Baldwin K.L., Dinh E.M., Hart B.M., Masson P.H.;
RT "CACTIN is an essential nuclear protein in Arabidopsis and may be
RT associated with the eukaryotic spliceosome.";
RL FEBS Lett. 587:873-879(2013).
RN [24]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27436712; DOI=10.1105/tpc.16.00301;
RA Carvalho R.F., Szakonyi D., Simpson C.G., Barbosa I.C., Brown J.W.,
RA Baena-Gonzalez E., Duque P.;
RT "The Arabidopsis SR45 splicing factor, a negative regulator of sugar
RT signaling, modulates SNF1-related protein kinase 1 stability.";
RL Plant Cell 28:1910-1925(2016).
CC -!- FUNCTION: Involved in 5' and 3' splicing site selection of introns, and
CC may bridge the 5' and 3' components of the spliceosome. Isoform 1 is
CC required during flower petal development and isoform 2 is involved in
CC root growth. Regulates negatively glucose and abscisic acid (ABA)
CC signaling during early seedling development. Involved in the RNA-
CC directed DNA methylation pathway (PubMed:22274613). Modulates KIN10
CC stability in response to sugars, probably through the splicing
CC regulation of 5PTASE13, a protein implicated in the proteasomal
CC degradation of KIN10 (PubMed:27436712). {ECO:0000269|PubMed:17534421,
CC ECO:0000269|PubMed:19403727, ECO:0000269|PubMed:20699397,
CC ECO:0000269|PubMed:22274613, ECO:0000269|PubMed:22563826,
CC ECO:0000269|PubMed:27436712}.
CC -!- SUBUNIT: Component of the spliceosome. Interacts with AFC2, U2AF35A,
CC U2AF35B, RNU1, SCL33 and SKIP. The interaction with AFC2 depends on
CC phosphorylation status. Interaction with RNU1 defines initial 5' splice
CC sites and interaction with U2AF35B 3' splice sites in the early stage
CC of spliceosome assembly. {ECO:0000269|PubMed:10593939,
CC ECO:0000269|PubMed:14675452, ECO:0000269|PubMed:18414657,
CC ECO:0000269|PubMed:22563826, ECO:0000269|PubMed:22942380}.
CC -!- INTERACTION:
CC Q9SEE9; Q9LY75: CYP63; NbExp=2; IntAct=EBI-1792008, EBI-2360522;
CC Q9SEE9; Q42404: RNU1; NbExp=4; IntAct=EBI-1792008, EBI-1633812;
CC Q9SEE9; Q9SEU4: SCL33; NbExp=3; IntAct=EBI-1792008, EBI-927103;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:14675452,
CC ECO:0000269|PubMed:16895966, ECO:0000269|PubMed:18414657,
CC ECO:0000269|PubMed:19435936}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:14675452, ECO:0000269|PubMed:16895966}.
CC Note=Colocalizes with spliceosome components. During interphase,
CC present in both nuclear speckles and nucleoplasm. Nucleoplasm-speckle
CC shuttling protein. The intranuclear distribution and mobility depend on
CC the phosphorylation status, ATP and transcription activity.
CC {ECO:0000269|PubMed:14675452, ECO:0000269|PubMed:16895966}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=SR45.1;
CC IsoId=Q9SEE9-1; Sequence=Displayed;
CC Name=2; Synonyms=SR45.2;
CC IsoId=Q9SEE9-2; Sequence=VSP_044313;
CC Name=3;
CC IsoId=Q9SEE9-3; Sequence=VSP_044314;
CC -!- TISSUE SPECIFICITY: Especially present in actively growing regions and
CC dividing cells. Mostly expressed in roots (primary and secondary root
CC meristem), shoot apical meristem (SAM), leaf primordia, pollen and
CC inflorescence, and, to a lower extent, in leaves, vascular tissue,
CC hydathode and fruits. {ECO:0000269|PubMed:10593939,
CC ECO:0000269|PubMed:14675452, ECO:0000269|PubMed:19403727}.
CC -!- INDUCTION: Levels of the isoform 2 are altered in response to sucrose
CC depletion (Suc) and temperature changes; reduced in cold but increased
CC in warm temperatures. {ECO:0000269|PubMed:17319848,
CC ECO:0000269|PubMed:19403727}.
CC -!- PTM: Phosphorylated by AFC2. The phosphorylation status regulates
CC intranuclear distribution. {ECO:0000269|PubMed:10593939,
CC ECO:0000269|PubMed:14675452}.
CC -!- DISRUPTION PHENOTYPE: Several developmental defects, including defects
CC in flower and leaf morphology (petal development), delayed flowering
CC time and root growth. Hypersensitivity to glucose (Glc) and to abscisic
CC acid (ABA) during early seedling growth, accompanied with an enhanced
CC ability to accumulate ABA in response to Glc. DNA methylation
CC establishment and maintenance defects. Altered alternative splicing
CC pattern of several related SR genes. {ECO:0000269|PubMed:17534421,
CC ECO:0000269|PubMed:19403727, ECO:0000269|PubMed:20699397,
CC ECO:0000269|PubMed:22274613, ECO:0000269|PubMed:27436712}.
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. SR45 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: According to PubMed:20884799, this protein should not be
CC regarded as a classical SR protein although it could complement an
CC animal in vitro splicing extract deficient in SR proteins.
CC {ECO:0000305|PubMed:17534421}.
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DR EMBL; AF151366; AAF19004.1; -; mRNA.
DR EMBL; AC011808; AAG10821.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29475.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29476.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29477.1; -; Genomic_DNA.
DR EMBL; AY045835; AAK76509.1; -; mRNA.
DR EMBL; BT020372; AAV85727.1; -; mRNA.
DR EMBL; BT021095; AAX12865.1; -; mRNA.
DR PIR; C86301; C86301.
DR RefSeq; NP_001185014.1; NM_001198085.1. [Q9SEE9-3]
DR RefSeq; NP_173107.1; NM_101523.4. [Q9SEE9-1]
DR RefSeq; NP_973844.1; NM_202115.3. [Q9SEE9-2]
DR AlphaFoldDB; Q9SEE9; -.
DR SMR; Q9SEE9; -.
DR BioGRID; 23470; 17.
DR IntAct; Q9SEE9; 8.
DR MINT; Q9SEE9; -.
DR STRING; 3702.AT1G16610.3; -.
DR iPTMnet; Q9SEE9; -.
DR PaxDb; Q9SEE9; -.
DR PRIDE; Q9SEE9; -.
DR ProteomicsDB; 226709; -. [Q9SEE9-1]
DR EnsemblPlants; AT1G16610.1; AT1G16610.1; AT1G16610. [Q9SEE9-1]
DR EnsemblPlants; AT1G16610.2; AT1G16610.2; AT1G16610. [Q9SEE9-2]
DR EnsemblPlants; AT1G16610.3; AT1G16610.3; AT1G16610. [Q9SEE9-3]
DR GeneID; 838230; -.
DR Gramene; AT1G16610.1; AT1G16610.1; AT1G16610. [Q9SEE9-1]
DR Gramene; AT1G16610.2; AT1G16610.2; AT1G16610. [Q9SEE9-2]
DR Gramene; AT1G16610.3; AT1G16610.3; AT1G16610. [Q9SEE9-3]
DR KEGG; ath:AT1G16610; -.
DR Araport; AT1G16610; -.
DR TAIR; locus:2017948; AT1G16610.
DR eggNOG; KOG0118; Eukaryota.
DR InParanoid; Q9SEE9; -.
DR OMA; PIRRRND; -.
DR OrthoDB; 1524222at2759; -.
DR PRO; PR:Q9SEE9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SEE9; baseline and differential.
DR Genevisible; Q9SEE9; AT.
DR GO; GO:0061574; C:ASAP complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016607; C:nuclear speck; IDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005654; C:nucleoplasm; 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:0000398; P:mRNA splicing, via spliceosome; IPI:TAIR.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; NAS:TAIR.
DR GO; GO:0010182; P:sugar mediated signaling pathway; IMP:UniProtKB.
DR CDD; cd12365; RRM_RNPS1; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034201; RNPS1_RRM.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
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..414
FT /note="Serine/arginine-rich splicing factor SR45"
FT /id="PRO_0000419679"
FT DOMAIN 98..176
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..219
FT /note="Required for isoform 1 function in petal
FT development"
FT /evidence="ECO:0000269|PubMed:19403727"
FT MOTIF 62..69
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 229..236
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 284..291
FT /note="Nuclear localization signal 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 318..325
FT /note="Nuclear localization signal 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 338..345
FT /note="Nuclear localization signal 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 373..380
FT /note="Nuclear localization signal 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 9..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..340
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..391
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16807317,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT VAR_SEQ 218..225
FT /note="TSPQRKTG -> R (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_044313"
FT VAR_SEQ 353
FT /note="K -> KYVGTHLNFFLG (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_044314"
FT MUTAGEN 218..219
FT /note="TS->AA: Mimics isoform 2 function in roots."
FT /evidence="ECO:0000269|PubMed:19403727"
FT CONFLICT 361
FT /note="R -> P (in Ref. 4; AAK76509)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 414 AA; 45348 MW; C3457F2319D8C983 CRC64;
MAKPSRGRRS PSVSGSSSRS SSRSRSGSSP SRSISRSRSR SRSLSSSSSP SRSVSSGSRS
PPRRGKSPAG PARRGRSPPP PPSKGASSPS KKAVQESLVL HVDSLSRNVN EAHLKEIFGN
FGEVIHVEIA MDRAVNLPRG HGYVEFKARA DAEKAQLYMD GAQIDGKVVK ATFTLPPRQK
VSSPPKPVSA APKRDAPKSD NAAADAEKDG GPRRPRETSP QRKTGLSPRR RSPLPRRGLS
PRRRSPDSPH RRRPGSPIRR RGDTPPRRRP ASPSRGRSPS SPPPRRYRSP PRGSPRRIRG
SPVRRRSPLP LRRRSPPPRR LRSPPRRSPI RRRSRSPIRR PGRSRSSSIS PRKGRGPAGR
RGRSSSYSSS PSPRRIPRKI SRSRSPKRPL RGKRSSSNSS SSSSPPPPPP PRKT
