SL30A_ARATH
ID SL30A_ARATH Reviewed; 262 AA.
AC Q9LHP2; Q9FYA8;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=Serine/arginine-rich SC35-like splicing factor SCL30A;
DE Short=At-SCL30A;
DE Short=AtSCL30A;
DE AltName: Full=SC35-like splicing factor 30A;
DE AltName: Full=Serine/arginine-rich splicing factor 30A;
GN Name=SCL30A; OrderedLocusNames=At3g13570; ORFNames=K20M4.1;
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], 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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].
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 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 [6]
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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174; SER-176 AND SER-178, AND
RP IDENTIFICATION BY 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 [9]
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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, AND IDENTIFICATION BY
RP 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 [12]
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 [13]
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 [14]
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 probably to multiple 5'-GAAG-3' repeats found in its third
CC intron, suggesting autoregulation of alternative splicing
CC (PubMed:22913769). May be necessary for accurate splicing of the 3'
CC region of introns. {ECO:0000269|PubMed:22913769}.
CC -!- SUBUNIT: Component of the spliceosome. Interacts with SNRNP35, CYP59
CC and RS2Z33. {ECO:0000269|PubMed:12176998, ECO:0000269|PubMed:15987817,
CC ECO:0000269|PubMed:16497658}.
CC -!- INTERACTION:
CC Q9LHP2; Q1PDV2: SCL28; NbExp=2; IntAct=EBI-927082, EBI-927052;
CC Q9LHP2; Q8L3X8: SCL30; NbExp=3; IntAct=EBI-927082, EBI-927061;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:15133128}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LHP2-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: No effect on alternative splicing, due to the
CC redundancy with SCL33. 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. {ECO:0000305|PubMed:17319848}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. SCL subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ293800; CAC03604.1; -; mRNA.
DR EMBL; AP002038; BAB02599.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75375.1; -; Genomic_DNA.
DR EMBL; AF370268; AAK44083.1; -; mRNA.
DR EMBL; AY063026; AAL34200.1; -; mRNA.
DR RefSeq; NP_187966.1; NM_112203.4. [Q9LHP2-1]
DR AlphaFoldDB; Q9LHP2; -.
DR SMR; Q9LHP2; -.
DR BioGRID; 5893; 14.
DR IntAct; Q9LHP2; 10.
DR STRING; 3702.AT3G13570.1; -.
DR iPTMnet; Q9LHP2; -.
DR PaxDb; Q9LHP2; -.
DR PRIDE; Q9LHP2; -.
DR ProteomicsDB; 232590; -. [Q9LHP2-1]
DR EnsemblPlants; AT3G13570.1; AT3G13570.1; AT3G13570. [Q9LHP2-1]
DR GeneID; 820559; -.
DR Gramene; AT3G13570.1; AT3G13570.1; AT3G13570. [Q9LHP2-1]
DR KEGG; ath:AT3G13570; -.
DR Araport; AT3G13570; -.
DR TAIR; locus:2086804; AT3G13570.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_012062_10_1_1; -.
DR InParanoid; Q9LHP2; -.
DR OMA; NVEWARN; -.
DR OrthoDB; 1524134at2759; -.
DR PhylomeDB; Q9LHP2; -.
DR PRO; PR:Q9LHP2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LHP2; baseline and differential.
DR Genevisible; Q9LHP2; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016607; C:nuclear speck; IDA: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; IGI: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; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Spliceosome.
FT CHAIN 1..262
FT /note="Serine/arginine-rich SC35-like splicing factor
FT SCL30A"
FT /id="PRO_0000429601"
FT DOMAIN 37..115
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..160
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..262
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 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16807317"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16807317"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16807317"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8L3X8"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8L3X8"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8L3X8"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FMG4"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FMG4"
FT CONFLICT 149
FT /note="Missing (in Ref. 1; CAC03604)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="R -> C (in Ref. 1; CAC03604)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 262 AA; 30227 MW; A77DDEF4E9ECD7B2 CRC64;
MRGRSYTPSP PRGYGRRGRS PSPRGRFGGS RDSDLPTSLL VRNLRHDCRQ EDLRRPFEQF
GPVKDIYLPR DYYTGDPRGF GFIQFMDPAD AAEAKHQMDG YLLLGRELTV VFAEENRKKP
TEMRTRDRGG RSNRFQDRRR SPPRYSRSPP PRRGRRSRSR SRGYNSPPAK RHQSRSVSPQ
DRRYEKERSY SRSPPHNGSR VRSGSPGRVK SHSRSPRRSV SPRKNRSYTP EQARSQSPVP
RQSRSPTPVP RGAQNGDRSP SQ
