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Protein

Serine/arginine-rich splicing factor RSZ22

Gene

RSZ22

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Sequence-specific RNA-binding protein probably involved in pre-mRNA splicing. In vitro, can complement efficiently splicing-deficient mammalian SRSF7-depleted HeLa cell extract.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri99 – 11618CCHC-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • mRNA splicing, via spliceosome Source: TAIR
  • RNA splicing Source: TAIR
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-ATH-72163. mRNA Splicing - Major Pathway.
R-ATH-72165. mRNA Splicing - Minor Pathway.
R-ATH-72187. mRNA 3'-end processing.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/arginine-rich splicing factor RSZ22
Alternative name(s):
RS-containing zinc finger protein 22
Short name:
At-RSZ22
Short name:
At-RSZp22
Short name:
AtRSZ22
Gene namesi
Name:RSZ22
Synonyms:RSZP22, SRZ22
Ordered Locus Names:At4g31580
ORF Names:F28M20.230
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G31580.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • nuclear speck Source: TAIR
  • nucleolus Source: TAIR
  • spliceosomal complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi101 – 1011C → S: No effect on cellular localization. 1 Publication
Mutagenesisi104 – 1041C → S: No effect on cellular localization. 1 Publication
Mutagenesisi109 – 1091H → S: No effect on cellular localization. 1 Publication
Mutagenesisi114 – 1141C → S: No effect on cellular localization. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 200200Serine/arginine-rich splicing factor RSZ22PRO_0000416992Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei138 – 1381PhosphoserineBy similarity
Modified residuei147 – 1471PhosphoserineBy similarity
Modified residuei152 – 1521PhosphoserineBy similarity
Modified residuei160 – 1601PhosphoserineBy similarity
Modified residuei162 – 1621PhosphoserineBy similarity
Modified residuei174 – 1741PhosphoserineBy similarity
Modified residuei200 – 2001PhosphoserineBy similarity

Post-translational modificationi

Extensively phosphorylated on serine residues in the RS domain. Phosphorylated by AFC2.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO81126.
PRIDEiO81126.

PTM databases

iPTMnetiO81126.

Expressioni

Tissue specificityi

Expressed in primary and lateral roots, stems, petioles, abaxial and adaxial epidermis cells, trichomes, unopened flowers, anther filaments, anthers, stigma, pollen, pollen tube, ovule funiculi, integuments, embryo sac and developing seeds.3 Publications

Gene expression databases

GenevisibleiO81126. AT.

Interactioni

Subunit structurei

Component of the spliceosome. Interacts with AFC2, RS2Z33 and RNU1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RNU1Q424044EBI-1633829,EBI-1633812

Protein-protein interaction databases

BioGridi14571. 6 interactions.
IntActiO81126. 4 interactions.
STRINGi3702.AT4G31580.1.

Structurei

3D structure databases

ProteinModelPortaliO81126.
SMRiO81126. Positions 3-61.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 7170RRMPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi76 – 9621Poly-GlyAdd
BLAST
Compositional biasi122 – 17756Arg/Ser-rich (RS domain)Add
BLAST

Sequence similaritiesi

Contains 1 CCHC-type zinc finger.PROSITE-ProRule annotation
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri99 – 11618CCHC-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0107. Eukaryota.
ENOG4111N8Y. LUCA.
HOGENOMiHOG000276234.
InParanoidiO81126.
KOiK12896.
OMAiSHNRGER.
PhylomeDBiO81126.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
4.10.60.10. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR001878. Znf_CCHC.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
PF00098. zf-CCHC. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
SM00343. ZnF_C2HC. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
SSF57756. SSF57756. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
PS50158. ZF_CCHC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O81126-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRVYVGNLD PRVTERELED EFRAFGVVRS VWVARRPPGY AFLDFEDPRD
60 70 80 90 100
ARDAIRALDG KNGWRVEQSH NRGERGGGGR GGDRGGGGGG RGGRGGSDLK
110 120 130 140 150
CYECGETGHF ARECRNRGGT GRRRSKSRSR TPPRYRRSPS YGRRSYSPRA
160 170 180 190 200
RSPPPPRRRS PSPPPARGRS YSRSPPPYRA REEVPYANGN GLKERRRSRS
Length:200
Mass (Da):22,458
Last modified:November 1, 1998 - v1
Checksum:iBDA0E941F763D741
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti67 – 671E → A in CAA05352 (PubMed:10350090).Curated
Sequence conflicti89 – 891G → A in CAA05352 (PubMed:10350090).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF033586 mRNA. Translation: AAD12769.1.
AJ002378 mRNA. Translation: CAA05352.1.
AL031004 Genomic DNA. Translation: CAA19765.1.
AL161579 Genomic DNA. Translation: CAB79876.1.
CP002687 Genomic DNA. Translation: AEE85931.1.
CP002687 Genomic DNA. Translation: AEE85932.1.
AY065387 mRNA. Translation: AAL38828.1.
AY117206 mRNA. Translation: AAM51281.1.
AY086525 mRNA. Translation: AAM63524.1.
PIRiT05112.
T52627.
RefSeqiNP_001078474.1. NM_001085005.1.
NP_194886.1. NM_119307.3.
UniGeneiAt.23104.

Genome annotation databases

EnsemblPlantsiAT4G31580.1; AT4G31580.1; AT4G31580.
AT4G31580.2; AT4G31580.2; AT4G31580.
GeneIDi829285.
GrameneiAT4G31580.1; AT4G31580.1; AT4G31580.
AT4G31580.2; AT4G31580.2; AT4G31580.
KEGGiath:AT4G31580.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF033586 mRNA. Translation: AAD12769.1.
AJ002378 mRNA. Translation: CAA05352.1.
AL031004 Genomic DNA. Translation: CAA19765.1.
AL161579 Genomic DNA. Translation: CAB79876.1.
CP002687 Genomic DNA. Translation: AEE85931.1.
CP002687 Genomic DNA. Translation: AEE85932.1.
AY065387 mRNA. Translation: AAL38828.1.
AY117206 mRNA. Translation: AAM51281.1.
AY086525 mRNA. Translation: AAM63524.1.
PIRiT05112.
T52627.
RefSeqiNP_001078474.1. NM_001085005.1.
NP_194886.1. NM_119307.3.
UniGeneiAt.23104.

3D structure databases

ProteinModelPortaliO81126.
SMRiO81126. Positions 3-61.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi14571. 6 interactions.
IntActiO81126. 4 interactions.
STRINGi3702.AT4G31580.1.

PTM databases

iPTMnetiO81126.

Proteomic databases

PaxDbiO81126.
PRIDEiO81126.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G31580.1; AT4G31580.1; AT4G31580.
AT4G31580.2; AT4G31580.2; AT4G31580.
GeneIDi829285.
GrameneiAT4G31580.1; AT4G31580.1; AT4G31580.
AT4G31580.2; AT4G31580.2; AT4G31580.
KEGGiath:AT4G31580.

Organism-specific databases

TAIRiAT4G31580.

Phylogenomic databases

eggNOGiKOG0107. Eukaryota.
ENOG4111N8Y. LUCA.
HOGENOMiHOG000276234.
InParanoidiO81126.
KOiK12896.
OMAiSHNRGER.
PhylomeDBiO81126.

Enzyme and pathway databases

ReactomeiR-ATH-72163. mRNA Splicing - Major Pathway.
R-ATH-72165. mRNA Splicing - Minor Pathway.
R-ATH-72187. mRNA 3'-end processing.

Miscellaneous databases

PROiO81126.

Gene expression databases

GenevisibleiO81126. AT.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
4.10.60.10. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR001878. Znf_CCHC.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
PF00098. zf-CCHC. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
SM00343. ZnF_C2HC. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
SSF57756. SSF57756. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
PS50158. ZF_CCHC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The plant U1 small nuclear ribonucleoprotein particle 70K protein interacts with two novel serine/arginine-rich proteins."
    Golovkin M., Reddy A.S.
    Plant Cell 10:1637-1648(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH RNU1, TISSUE SPECIFICITY.
  2. "A novel family of plant splicing factors with a Zn knuckle motif: examination of RNA binding and splicing activities."
    Lopato S., Gattoni R., Fabini G., Stevenin J., Barta A.
    Plant Mol. Biol. 39:761-773(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Strain: cv. Columbia.
  3. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. "An SC35-like protein and a novel serine/arginine-rich protein interact with Arabidopsis U1-70K protein."
    Golovkin M., Reddy A.S.N.
    J. Biol. Chem. 274:36428-36438(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AFC2.
  8. "Network of interactions of a novel plant-specific Arg/Ser-rich protein, atRSZ33, with atSC35-like splicing factors."
    Lopato S., Forstner C., Kalyna M., Hilscher J., Langhammer U., Korakod L., Zdravko J., Barta A.
    J. Biol. Chem. 277:39989-39998(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH RS2Z33.
  9. "Use of fluorescent protein tags to study nuclear organization of the spliceosomal machinery in transiently transformed living plant cells."
    Lorkovic Z.J., Hilscher J., Barta A.
    Mol. Biol. Cell 15:3233-3243(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. "Functional distribution and dynamics of Arabidopsis SR splicing factors in living plant cells."
    Tillemans V., Dispa L., Remacle C., Collinge M., Motte P.
    Plant J. 41:567-582(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. "Insights into nuclear organization in plants as revealed by the dynamic distribution of Arabidopsis SR splicing factors."
    Tillemans V., Leponce I., Rausin G., Dispa L., Motte P.
    Plant Cell 18:3218-3234(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  12. "Co-localisation studies of Arabidopsis SR splicing factors reveal different types of speckles in plant cell nuclei."
    Lorkovic Z.J., Hilscher J., Barta A.
    Exp. Cell Res. 314:3175-3186(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  13. "Implementing a rational and consistent nomenclature for serine/arginine-rich protein splicing factors (SR proteins) in plants."
    Barta A., Kalyna M., Reddy A.S.
    Plant Cell 22:2926-2929(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  14. "Dynamic nucleocytoplasmic shuttling of an Arabidopsis SR splicing factor: role of the RNA-binding domains."
    Rausin G., Tillemans V., Stankovic N., Hanikenne M., Motte P.
    Plant Physiol. 153:273-284(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-101; CYS-104; HIS-109 AND CYS-114.
  15. "Comparative analysis of serine/arginine-rich proteins across 27 eukaryotes: insights into sub-family classification and extent of alternative splicing."
    Richardson D.N., Rogers M.F., Labadorf A., Ben-Hur A., Guo H., Paterson A.H., Reddy A.S.N.
    PLoS ONE 6:E24542-E24542(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY.
  16. "CYCLIN-DEPENDENT KINASE G1 is associated with the spliceosome to regulate CALLOSE SYNTHASE5 splicing and pollen wall formation in Arabidopsis."
    Huang X.Y., Niu J., Sun M.X., Zhu J., Gao J.F., Yang J., Zhou Q., Yang Z.N.
    Plant Cell 25:637-648(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION THE SPLICEOSOME COMPLEX.

Entry informationi

Entry nameiRSZ22_ARATH
AccessioniPrimary (citable) accession number: O81126
Secondary accession number(s): O23646
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2012
Last sequence update: November 1, 1998
Last modified: February 17, 2016
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.