SRC33_ARATH
ID SRC33_ARATH Reviewed; 287 AA.
AC Q9SEU4; C0Z312; F4I090; F4I092; Q949P4; Q9C8A1;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 148.
DE RecName: Full=Serine/arginine-rich SC35-like splicing factor SCL33;
DE Short=At-SCL33;
DE Short=AtSCL33;
DE AltName: Full=SC35-like splicing factor 33;
DE AltName: Full=Serine/arginine-rich splicing factor 33;
GN Name=SCL33; Synonyms=SR33; OrderedLocusNames=At1g55310; ORFNames=F7A10.15;
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 SR45, HOMODIMER, PHOSPHORYLATION BY AFC2, ALTERNATIVE SPLICING, AND TISSUE
RP 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 [MRNA] (ISOFORM 1), AND INTERACTION WITH RS2Z33.
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 [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 2).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 85-287 (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 [8]
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 [9]
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 [10]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
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 [11]
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 [12]
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 [13]
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 [14]
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 [15]
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 [16]
RP ALTERNATIVE SPLICING, AND 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 [17]
RP FUNCTION, ALTERNATIVE SPLICING, AND DISRUPTION PHENOTYPE.
RX PubMed=22913769; DOI=10.1111/tpj.12004;
RA Thomas J., Palusa S.G., Prasad K.V., Ali G.S., Surabhi G.K., Ben-Hur A.,
RA Abdel-Ghany S.E., Reddy A.S.;
RT "Identification of an intronic splicing regulatory element involved in
RT auto-regulation of alternative splicing of SCL33 pre-mRNA.";
RL Plant J. 72:935-946(2012).
CC -!- FUNCTION: Involved in intron recognition and spliceosome assembly.
CC Binds to multiple 5'-GAAG-3' repeats found in its third intron,
CC suggesting autoregulation of alternative splicing (PubMed:22913769).
CC May be necessary for accurate splicing of the 3' region of introns.
CC {ECO:0000269|PubMed:22913769}.
CC -!- SUBUNIT: Component of the spliceosome. Homodimer. Interacts with AFC2,
CC CYP59, RS2Z33, RNU1 and SR45. The interaction with AFC2 depends on
CC phosphorylation status. {ECO:0000269|PubMed:10593939,
CC ECO:0000269|PubMed:12176998, ECO:0000269|PubMed:16497658}.
CC -!- INTERACTION:
CC Q9SEU4; P51567: AFC2; NbExp=2; IntAct=EBI-927103, EBI-1792180;
CC Q9SEU4; Q6Q151: CYP59; NbExp=3; IntAct=EBI-927103, EBI-1625989;
CC Q9SEU4; Q42404: RNU1; NbExp=3; IntAct=EBI-927103, EBI-1633812;
CC Q9SEU4; Q9SEU4: SCL33; NbExp=3; IntAct=EBI-927103, EBI-927103;
CC Q9SEU4; Q9SEE9: SR45; NbExp=3; IntAct=EBI-927103, EBI-1792008;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:15034145,
CC ECO:0000269|PubMed:15133128}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:15034145}. Cytoplasm {ECO:0000269|PubMed:15034145}.
CC Note=Colocalizes with spliceosome components. Follows a dynamic
CC subcellular location during the cell cycle. Distributed throughout the
CC cell on entry into mitosis, as the nuclear envelope breaks down. In
CC metaphase, diffusely present throughout the cytoplasm. In later
CC telophase, as the nuclear envelope is reformed, reenters into the
CC daughter nuclei where speckles are observed. Daughter nuclei acquire
CC later a typical interphase spherical shape and the nucleolus gradually
CC forms. {ECO:0000269|PubMed:15034145}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9SEU4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SEU4-2; Sequence=VSP_044317;
CC Name=3;
CC IsoId=Q9SEU4-3; Sequence=VSP_044315, VSP_044316;
CC Name=4;
CC IsoId=Q9SEU4-4; Sequence=VSP_044318, VSP_044319;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Mostly expressed in roots, fruits and
CC flowers, and, to a lower extent, in leaves.
CC {ECO:0000269|PubMed:10593939, ECO:0000269|PubMed:15034145}.
CC -!- DEVELOPMENTAL STAGE: Near the primary root tip, expressed in the
CC vascular bundle, endodermis, cortex, epidermis, and lateral root cap.
CC In leaves, present in guard cells leaf epidermal pavement cells and
CC trichomes. In flowers, high expression in the pollen grains, mostly in
CC vegetative nuclei. Also present in sepals, petals, and young siliques.
CC After flowering, the expression level decreases gradually.
CC {ECO:0000269|PubMed:15034145}.
CC -!- PTM: Phosphorylated by AFC2. {ECO:0000269|PubMed:10593939}.
CC -!- DISRUPTION PHENOTYPE: No effect on alternative splicing, due to the
CC redundancy with SCL30A. Scl33 and scl30a double mutant shows altered
CC splicing. {ECO:0000269|PubMed:22913769}.
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.
CC {ECO:0000305|PubMed:17319848}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. SCL subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51556.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF099940; AAF17288.1; -; mRNA.
DR EMBL; AJ293799; CAC03603.1; -; mRNA.
DR EMBL; AC027034; AAG51556.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33222.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33223.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58649.1; -; Genomic_DNA.
DR EMBL; AY050974; AAK93651.1; -; mRNA.
DR EMBL; BT020420; AAW28547.1; -; mRNA.
DR EMBL; AK318976; BAH57091.1; -; mRNA.
DR PIR; B96595; B96595.
DR PIR; T50647; T50647.
DR RefSeq; NP_001031195.4; NM_001036118.4. [Q9SEU4-4]
DR RefSeq; NP_001319238.1; NM_001333699.1. [Q9SEU4-4]
DR RefSeq; NP_001321067.1; NM_001333701.1.
DR RefSeq; NP_564685.4; NM_104406.6. [Q9SEU4-1]
DR AlphaFoldDB; Q9SEU4; -.
DR SMR; Q9SEU4; -.
DR BioGRID; 27201; 10.
DR IntAct; Q9SEU4; 8.
DR STRING; 3702.AT1G55310.3; -.
DR iPTMnet; Q9SEU4; -.
DR PaxDb; Q9SEU4; -.
DR PRIDE; Q9SEU4; -.
DR ProteomicsDB; 226721; -. [Q9SEU4-1]
DR EnsemblPlants; AT1G55310.1; AT1G55310.1; AT1G55310. [Q9SEU4-1]
DR EnsemblPlants; AT1G55310.2; AT1G55310.2; AT1G55310. [Q9SEU4-4]
DR EnsemblPlants; AT1G55310.5; AT1G55310.5; AT1G55310. [Q9SEU4-4]
DR GeneID; 841976; -.
DR Gramene; AT1G55310.1; AT1G55310.1; AT1G55310. [Q9SEU4-1]
DR Gramene; AT1G55310.2; AT1G55310.2; AT1G55310. [Q9SEU4-4]
DR Gramene; AT1G55310.5; AT1G55310.5; AT1G55310. [Q9SEU4-4]
DR KEGG; ath:AT1G55310; -.
DR Araport; AT1G55310; -.
DR TAIR; locus:2035651; AT1G55310.
DR eggNOG; KOG0118; Eukaryota.
DR InParanoid; Q9SEU4; -.
DR OMA; CSPADHR; -.
DR PhylomeDB; Q9SEU4; -.
DR PRO; PR:Q9SEU4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SEU4; baseline and differential.
DR Genevisible; Q9SEU4; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0035061; C:interchromatin granule; IDA:TAIR.
DR GO; GO:0016607; C:nuclear speck; IDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; ISS:TAIR.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IPI:TAIR.
DR GO; GO:0008380; P:RNA splicing; NAS:TAIR.
DR Gene3D; 3.30.70.330; -; 1.
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; 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; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Spliceosome.
FT CHAIN 1..287
FT /note="Serine/arginine-rich SC35-like splicing factor
FT SCL33"
FT /id="PRO_0000419680"
FT DOMAIN 36..114
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..257
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8L3X8"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8L3X8"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LHP2"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LHP2"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LHP2"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8L3X8"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8L3X8"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8L3X8"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8L3X8"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FMG4"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FMG4"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FMG4"
FT VAR_SEQ 74
FT /note="G -> GSHLCTDTCKASR (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_044315"
FT VAR_SEQ 130
FT /note="G -> GS (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_044316"
FT VAR_SEQ 216..239
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_044317"
FT VAR_SEQ 216..220
FT /note="SPRRS -> TQEEA (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_044318"
FT VAR_SEQ 221..287
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_044319"
SQ SEQUENCE 287 AA; 33337 MW; 8964F965DF8ACFDD CRC64;
MRGRSYTPSP PRGYGRRGRS PSPRGRYGGR SRDLPTSLLV RNLRHDCRQE DLRKSFEQFG
PVKDIYLPRD YYTGDPRGFG FVQFMDPADA ADAKHHMDGY LLLGRELTVV FAEENRKKPT
EMRARERGGG RFRDRRRTPP RYYSRSRSPP PRRGRSRSRS GDYYSPPPRR HHPRSISPRE
ERYDGRRSYS RSPASDGSRG RSLTPVRGKS RSLSPSPRRS ISRSPRRSRS PSPKRNRSVS
PRRSISRSPR RSRSPRRSRR SYTPEPARSR SQSPHGGQYD EDRSPSQ
