RSZ22_ARATH
ID RSZ22_ARATH Reviewed; 200 AA.
AC O81126; O23646;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 170.
DE RecName: Full=Serine/arginine-rich splicing factor RSZ22;
DE AltName: Full=RS-containing zinc finger protein 22;
DE Short=At-RSZ22;
DE Short=At-RSZp22;
DE Short=AtRSZ22;
GN Name=RSZ22; Synonyms=RSZP22, SRZ22; OrderedLocusNames=At4g31580;
GN ORFNames=F28M20.230;
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], INTERACTION WITH RNU1, AND TISSUE 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], AND FUNCTION.
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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].
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].
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 [7]
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 [8]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, 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 [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.
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 [11]
RP SUBCELLULAR LOCATION.
RX PubMed=17114353; DOI=10.1105/tpc.106.044529;
RA Tillemans V., Leponce I., Rausin G., Dispa L., Motte P.;
RT "Insights into nuclear organization in plants as revealed by the dynamic
RT distribution of Arabidopsis SR splicing factors.";
RL Plant Cell 18:3218-3234(2006).
RN [12]
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 [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 SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF CYS-101;
RP CYS-104; HIS-109 AND CYS-114.
RX PubMed=20237019; DOI=10.1104/pp.110.154740;
RA Rausin G., Tillemans V., Stankovic N., Hanikenne M., Motte P.;
RT "Dynamic nucleocytoplasmic shuttling of an Arabidopsis SR splicing factor:
RT role of the RNA-binding domains.";
RL Plant Physiol. 153:273-284(2010).
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).
RN [16]
RP IDENTIFICATION OF THE SPLICEOSOME COMPLEX.
RX PubMed=23404887; DOI=10.1105/tpc.112.107896;
RA Huang X.Y., Niu J., Sun M.X., Zhu J., Gao J.F., Yang J., Zhou Q.,
RA Yang Z.N.;
RT "CYCLIN-DEPENDENT KINASE G1 is associated with the spliceosome to regulate
RT CALLOSE SYNTHASE5 splicing and pollen wall formation in Arabidopsis.";
RL Plant Cell 25:637-648(2013).
CC -!- FUNCTION: Sequence-specific RNA-binding protein probably involved in
CC pre-mRNA splicing. In vitro, can complement efficiently splicing-
CC deficient mammalian SRSF7-depleted HeLa cell extract.
CC {ECO:0000269|PubMed:10350090}.
CC -!- SUBUNIT: Component of the spliceosome. Interacts with AFC2, RS2Z33 and
CC RNU1. {ECO:0000269|PubMed:10593939, ECO:0000269|PubMed:12176998,
CC ECO:0000269|PubMed:9761791}.
CC -!- INTERACTION:
CC O81126; Q42404: RNU1; NbExp=4; IntAct=EBI-1633829, EBI-1633812;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:15133128,
CC ECO:0000269|PubMed:15686520, ECO:0000269|PubMed:17114353,
CC ECO:0000269|PubMed:18674533, ECO:0000305|PubMed:12176998}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:15133128, ECO:0000269|PubMed:15686520,
CC ECO:0000269|PubMed:17114353, ECO:0000269|PubMed:20237019}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:15686520, ECO:0000269|PubMed:17114353}.
CC Cytoplasm {ECO:0000269|PubMed:17114353, ECO:0000269|PubMed:20237019}.
CC Note=Shuttling between nucleolus, nucleoplasm and cytoplasm surrounding
CC the nucleus. Nucleolus localization is dependent on phosphorylation
CC state. {ECO:0000269|PubMed:15686520, ECO:0000269|PubMed:17114353,
CC ECO:0000269|PubMed:20237019}.
CC -!- TISSUE SPECIFICITY: Expressed in primary and lateral roots, stems,
CC petioles, abaxial and adaxial epidermis cells, trichomes, unopened
CC flowers, anther filaments, anthers, stigma, pollen, pollen tube, ovule
CC funiculi, integuments, embryo sac and developing seeds.
CC {ECO:0000269|PubMed:12176998, ECO:0000269|PubMed:20237019,
CC ECO:0000269|PubMed:9761791}.
CC -!- PTM: Extensively phosphorylated on serine residues in the RS domain.
CC Phosphorylated by AFC2.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. RSZ subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF033586; AAD12769.1; -; mRNA.
DR EMBL; AJ002378; CAA05352.1; -; mRNA.
DR EMBL; AL031004; CAA19765.1; -; Genomic_DNA.
DR EMBL; AL161579; CAB79876.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85931.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85932.1; -; Genomic_DNA.
DR EMBL; AY065387; AAL38828.1; -; mRNA.
DR EMBL; AY117206; AAM51281.1; -; mRNA.
DR EMBL; AY086525; AAM63524.1; -; mRNA.
DR PIR; T05112; T05112.
DR PIR; T52627; T52627.
DR RefSeq; NP_001078474.1; NM_001085005.1.
DR RefSeq; NP_194886.1; NM_119307.4.
DR AlphaFoldDB; O81126; -.
DR SMR; O81126; -.
DR BioGRID; 14571; 19.
DR IntAct; O81126; 13.
DR STRING; 3702.AT4G31580.1; -.
DR iPTMnet; O81126; -.
DR PaxDb; O81126; -.
DR PRIDE; O81126; -.
DR ProteomicsDB; 226656; -.
DR EnsemblPlants; AT4G31580.1; AT4G31580.1; AT4G31580.
DR EnsemblPlants; AT4G31580.2; AT4G31580.2; AT4G31580.
DR GeneID; 829285; -.
DR Gramene; AT4G31580.1; AT4G31580.1; AT4G31580.
DR Gramene; AT4G31580.2; AT4G31580.2; AT4G31580.
DR KEGG; ath:AT4G31580; -.
DR Araport; AT4G31580; -.
DR TAIR; locus:2124799; AT4G31580.
DR eggNOG; KOG0107; Eukaryota.
DR HOGENOM; CLU_012062_20_1_1; -.
DR InParanoid; O81126; -.
DR OMA; EMHRDSC; -.
DR OrthoDB; 1533297at2759; -.
DR PhylomeDB; O81126; -.
DR PRO; PR:O81126; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O81126; baseline and differential.
DR Genevisible; O81126; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IDA:TAIR.
DR GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA: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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
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 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 Cytoplasm; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Spliceosome; Zinc; Zinc-finger.
FT CHAIN 1..200
FT /note="Serine/arginine-rich splicing factor RSZ22"
FT /id="PRO_0000416992"
FT DOMAIN 2..71
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 99..116
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 62..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..171
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P92964"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VYA5"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P92964"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P92966"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VYA5"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9SJA6"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P92966"
FT MUTAGEN 101
FT /note="C->S: No effect on cellular localization."
FT /evidence="ECO:0000269|PubMed:20237019"
FT MUTAGEN 104
FT /note="C->S: No effect on cellular localization."
FT /evidence="ECO:0000269|PubMed:20237019"
FT MUTAGEN 109
FT /note="H->S: No effect on cellular localization."
FT /evidence="ECO:0000269|PubMed:20237019"
FT MUTAGEN 114
FT /note="C->S: No effect on cellular localization."
FT /evidence="ECO:0000269|PubMed:20237019"
FT CONFLICT 67
FT /note="E -> A (in Ref. 2; CAA05352)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="G -> A (in Ref. 2; CAA05352)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 200 AA; 22458 MW; BDA0E941F763D741 CRC64;
MSRVYVGNLD PRVTERELED EFRAFGVVRS VWVARRPPGY AFLDFEDPRD ARDAIRALDG
KNGWRVEQSH NRGERGGGGR GGDRGGGGGG RGGRGGSDLK CYECGETGHF ARECRNRGGT
GRRRSKSRSR TPPRYRRSPS YGRRSYSPRA RSPPPPRRRS PSPPPARGRS YSRSPPPYRA
REEVPYANGN GLKERRRSRS
