RSZ21_ARATH
ID RSZ21_ARATH Reviewed; 187 AA.
AC O81127; B3H6W9; F4I7M9; O23645; Q9LRA8;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 158.
DE RecName: Full=Serine/arginine-rich splicing factor RSZ21;
DE AltName: Full=RS-containing zinc finger protein 21;
DE Short=At-RSZ21;
DE Short=At-RSZp21;
DE Short=AtRSZ21;
GN Name=RSZ21; Synonyms=RSZP21, SRZ21; OrderedLocusNames=At1g23860;
GN ORFNames=T23E23.2;
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 RNU1, AND TISSUE
RP SPECIFICITY.
RX PubMed=9761791; DOI=10.2307/3870762;
RA Golovkin M., Reddy A.S.;
RT "The plant U1 small nuclear ribonucleoprotein particle 70K protein
RT interacts with two novel serine/arginine-rich proteins.";
RL Plant Cell 10:1637-1648(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=10350090; DOI=10.1023/a:1006129615846;
RA Lopato S., Gattoni R., Fabini G., Stevenin J., Barta A.;
RT "A novel family of plant splicing factors with a Zn knuckle motif:
RT examination of RNA binding and splicing activities.";
RL Plant Mol. Biol. 39:761-773(1999).
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=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 [6]
RP INTERACTION WITH AFC2.
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 [7]
RP 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 [8]
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 [9]
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 [10]
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 [11]
RP SUBCELLULAR LOCATION.
RX PubMed=18674533; DOI=10.1016/j.yexcr.2008.06.020;
RA Lorkovic Z.J., Hilscher J., Barta A.;
RT "Co-localisation studies of Arabidopsis SR splicing factors reveal
RT different types of speckles in plant cell nuclei.";
RL Exp. Cell Res. 314:3175-3186(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, 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 [13]
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 [14]
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 [15]
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. Interacts with SNRNP35, AFC2,
CC CYP59, RS2Z33 and RNU1 (PubMed:10593939, PubMed:12176998,
CC PubMed:15987817, PubMed:16497658, PubMed:9761791). Interacts with MOS14
CC (PubMed:21738492). {ECO:0000269|PubMed:10593939,
CC ECO:0000269|PubMed:12176998, ECO:0000269|PubMed:15987817,
CC ECO:0000269|PubMed:16497658, ECO:0000269|PubMed:21738492,
CC ECO:0000269|PubMed:9761791}.
CC -!- INTERACTION:
CC O81127; P51568: AFC3; NbExp=3; IntAct=EBI-927172, EBI-25519318;
CC O81127; Q8L9Y3: ARR14; NbExp=3; IntAct=EBI-927172, EBI-1100737;
CC O81127; Q9FIU6: ORRM2; NbExp=3; IntAct=EBI-927172, EBI-4449084;
CC O81127; Q42404: RNU1; NbExp=4; IntAct=EBI-927172, EBI-1633812;
CC O81127; P92964: RS31; NbExp=5; IntAct=EBI-927172, EBI-927132;
CC O81127; P92966: RS41; NbExp=3; IntAct=EBI-927172, EBI-4474477;
CC O81127; O81127: RSZ21; NbExp=3; IntAct=EBI-927172, EBI-927172;
CC O81127; Q9SJA6: RSZ22A; NbExp=3; IntAct=EBI-927172, EBI-4433459;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:15133128,
CC ECO:0000269|PubMed:18674533}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O81127-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O81127-2; Sequence=VSP_054986;
CC Name=3;
CC IsoId=O81127-3; Sequence=VSP_054987;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, flowers and siliques.
CC {ECO:0000269|PubMed:9761791}.
CC -!- PTM: Extensively phosphorylated on serine residues in the RS domain (By
CC similarity). Phosphorylated by AFC2. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. RSZ subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF87159.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF033587; AAD12770.1; -; mRNA.
DR EMBL; AJ002377; CAA05351.1; -; mRNA.
DR EMBL; AC002423; AAF87159.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30440.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30441.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30442.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30443.1; -; Genomic_DNA.
DR EMBL; AK317576; BAH20240.1; -; mRNA.
DR PIR; A86373; A86373.
DR PIR; T51584; T51584.
DR PIR; T52628; T52628.
DR RefSeq; NP_001117342.1; NM_001123870.4. [O81127-3]
DR RefSeq; NP_001185074.1; NM_001198145.1. [O81127-2]
DR RefSeq; NP_564208.1; NM_102234.4. [O81127-1]
DR RefSeq; NP_973901.1; NM_202172.1. [O81127-1]
DR AlphaFoldDB; O81127; -.
DR SMR; O81127; -.
DR BioGRID; 24235; 23.
DR IntAct; O81127; 16.
DR STRING; 3702.AT1G23860.1; -.
DR iPTMnet; O81127; -.
DR PaxDb; O81127; -.
DR PRIDE; O81127; -.
DR ProteomicsDB; 228056; -. [O81127-1]
DR EnsemblPlants; AT1G23860.1; AT1G23860.1; AT1G23860. [O81127-1]
DR EnsemblPlants; AT1G23860.2; AT1G23860.2; AT1G23860. [O81127-1]
DR EnsemblPlants; AT1G23860.3; AT1G23860.3; AT1G23860. [O81127-3]
DR EnsemblPlants; AT1G23860.4; AT1G23860.4; AT1G23860. [O81127-2]
DR GeneID; 838997; -.
DR Gramene; AT1G23860.1; AT1G23860.1; AT1G23860. [O81127-1]
DR Gramene; AT1G23860.2; AT1G23860.2; AT1G23860. [O81127-1]
DR Gramene; AT1G23860.3; AT1G23860.3; AT1G23860. [O81127-3]
DR Gramene; AT1G23860.4; AT1G23860.4; AT1G23860. [O81127-2]
DR KEGG; ath:AT1G23860; -.
DR Araport; AT1G23860; -.
DR TAIR; locus:2199837; AT1G23860.
DR eggNOG; KOG0107; Eukaryota.
DR InParanoid; O81127; -.
DR OMA; ELDGTMC; -.
DR PhylomeDB; O81127; -.
DR PRO; PR:O81127; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O81127; baseline and differential.
DR Genevisible; O81127; AT.
DR GO; GO:0016607; C:nuclear speck; IDA:TAIR.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
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 InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Metal-binding; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Spliceosome; Zinc;
KW Zinc-finger.
FT CHAIN 1..187
FT /note="Serine/arginine-rich splicing factor RSZ21"
FT /id="PRO_0000416991"
FT DOMAIN 2..73
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 89..106
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 68..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..151
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VYA5"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VYA5"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P92964"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P92966"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9SJA6"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FYB7"
FT VAR_SEQ 128..131
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_054986"
FT VAR_SEQ 131..153
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_054987"
FT CONFLICT 136
FT /note="R -> S (in Ref. 2; CAA05351)"
FT /evidence="ECO:0000305"
FT CONFLICT 153..155
FT /note="Missing (in Ref. 2; CAA05351)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 187 AA; 21537 MW; D8706B45A8E78F72 CRC64;
MTRVYVGNLD PRVTERELED EFKAFGVLRN VWVARRPPGY AFLEFDDERD ALDAISALDR
KNGWRVELSH KDKGGRGGGG GRRGGIEDSK CYECGELGHF ARECRRGRGS VRRRSPSPRR
RRSPDYGYAR RSISPRGRRS PPRRRSVTPP RRGRSYSRSP PYRGSRRDSP RRRDSPYGRR
SPYANGV
