RSZ33_ARATH
ID RSZ33_ARATH Reviewed; 290 AA.
AC Q8VYA5; F4IQ37; Q67Y02; Q9FYA7; Q9ZUT2;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 145.
DE RecName: Full=Serine/arginine-rich splicing factor RS2Z33;
DE AltName: Full=RS-containing zinc finger protein 33;
DE Short=At-RS2Z33;
DE Short=At-RSZ33;
DE Short=AtRSZ33;
GN Name=RS2Z33; Synonyms=RSZ33; OrderedLocusNames=At2g37340; ORFNames=F3G5.13;
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), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, PHOSPHORYLATION, AND INTERACTION WITH SR34; RSZ21; RSZ22;
RP SCL28; SCL30; SCL33; SCL30A AND SC35.
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INTERACTION WITH SR33.
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 FUNCTION, ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=12972547; DOI=10.1091/mbc.e03-02-0109;
RA Kalyna M., Lopato S., Barta A.;
RT "Ectopic expression of atRSZ33 reveals its function in splicing and causes
RT pleiotropic changes in development.";
RL Mol. Biol. Cell 14:3565-3577(2003).
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 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202; SER-204; SER-211;
RP SER-219; SER-226 AND SER-256, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [13]
RP FUNCTION.
RX PubMed=16936312; DOI=10.1093/nar/gkl570;
RA Kalyna M., Lopato S., Voronin V., Barta A.;
RT "Evolutionary conservation and regulation of particular alternative
RT splicing events in plant SR proteins.";
RL Nucleic Acids Res. 34:4395-4405(2006).
RN [14]
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 [15]
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 [16]
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 [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211; SER-219 AND SER-256, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211; SER-219; SER-226;
RP SER-230; SER-239; SER-245 AND SER-256, AND IDENTIFICATION BY MASS
RP 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 [20]
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 [21]
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 [22]
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 [23]
RP FUNCTION, AND INTERACTION WITH CDKG1.
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).
RN [24]
RP INDUCTION.
RX PubMed=24763593; DOI=10.1126/science.1250322;
RA Petrillo E., Herz M.A., Fuchs A., Reifer D., Fuller J., Yanovsky M.J.,
RA Simpson C., Brown J.W., Barta A., Kalyna M., Kornblihtt A.R.;
RT "A chloroplast retrograde signal regulates nuclear alternative splicing.";
RL Science 344:427-430(2014).
CC -!- FUNCTION: Splicing factor involved in constitutive and/or alternative
CC splicing. Regulates the splicing of its own pre-mRNA and the
CC alternative splicing of RS30, RS31 and RS34. Associates the cyclin-
CC dependent kinase G1 (CDKG1) with the spliceosome and recruits it to U1
CC snRNP to facilitate splicing. {ECO:0000269|PubMed:12972547,
CC ECO:0000269|PubMed:16936312, ECO:0000269|PubMed:23404887}.
CC -!- SUBUNIT: Component of the spliceosome. Interacts with SNRNP35, CDKG1,
CC cyp59, SR33, SR34, RSZ21, RSZ22, SCL28, SCL30, SCL30A, SCL33 and SC35
CC (PubMed:10593939, PubMed:12176998, PubMed:15987817, PubMed:16497658,
CC PubMed:23404887). Interacts with MOS14 (PubMed:21738492).
CC {ECO:0000269|PubMed:10593939, ECO:0000269|PubMed:12176998,
CC ECO:0000269|PubMed:15987817, ECO:0000269|PubMed:16497658,
CC ECO:0000269|PubMed:21738492, ECO:0000269|PubMed:23404887}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:12176998,
CC ECO:0000269|PubMed:15133128, ECO:0000269|PubMed:15686520,
CC ECO:0000269|PubMed:18674533}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8VYA5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VYA5-2; Sequence=VSP_043112;
CC Name=3;
CC IsoId=Q8VYA5-3; Sequence=VSP_043113;
CC -!- TISSUE SPECIFICITY: Expressed in roots, flowers, anthers, pollen,
CC ovules, style and developing seeds. Not detected in stems or leaves.
CC {ECO:0000269|PubMed:12176998, ECO:0000269|PubMed:12972547}.
CC -!- PTM: Extensively phosphorylated on serine residues in the RS domain.
CC {ECO:0000269|PubMed:12176998}.
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 (PubMed:17319848), but is not
CC affected by the light/dark regimes (PubMed:24763593).
CC {ECO:0000305|PubMed:17319848, ECO:0000305|PubMed:24763593}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. RS2Z subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BX842467; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ293801; CAC03605.1; -; mRNA.
DR EMBL; AC005896; AAC98054.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09385.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09386.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09387.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM63217.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM63218.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM63219.1; -; Genomic_DNA.
DR EMBL; AY072315; AAL61922.1; -; mRNA.
DR EMBL; AY114563; AAM47882.1; -; mRNA.
DR EMBL; AK176551; BAD44314.1; -; mRNA.
DR EMBL; BX842463; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BX842467; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK176666; BAD44429.1; -; mRNA.
DR PIR; F84791; F84791.
DR RefSeq; NP_001325321.1; NM_001336655.1. [Q8VYA5-2]
DR RefSeq; NP_001325322.1; NM_001336653.1. [Q8VYA5-2]
DR RefSeq; NP_001325323.1; NM_001336654.1. [Q8VYA5-3]
DR RefSeq; NP_850280.1; NM_179949.3. [Q8VYA5-1]
DR RefSeq; NP_973619.1; NM_201890.2. [Q8VYA5-2]
DR RefSeq; NP_973620.1; NM_201891.2. [Q8VYA5-3]
DR AlphaFoldDB; Q8VYA5; -.
DR SMR; Q8VYA5; -.
DR BioGRID; 3655; 16.
DR IntAct; Q8VYA5; 11.
DR STRING; 3702.AT2G37340.1; -.
DR iPTMnet; Q8VYA5; -.
DR MetOSite; Q8VYA5; -.
DR PaxDb; Q8VYA5; -.
DR PRIDE; Q8VYA5; -.
DR ProteomicsDB; 226631; -. [Q8VYA5-1]
DR EnsemblPlants; AT2G37340.1; AT2G37340.1; AT2G37340. [Q8VYA5-1]
DR EnsemblPlants; AT2G37340.2; AT2G37340.2; AT2G37340. [Q8VYA5-2]
DR EnsemblPlants; AT2G37340.3; AT2G37340.3; AT2G37340. [Q8VYA5-3]
DR EnsemblPlants; AT2G37340.4; AT2G37340.4; AT2G37340. [Q8VYA5-2]
DR EnsemblPlants; AT2G37340.5; AT2G37340.5; AT2G37340. [Q8VYA5-3]
DR EnsemblPlants; AT2G37340.6; AT2G37340.6; AT2G37340. [Q8VYA5-2]
DR GeneID; 818311; -.
DR Gramene; AT2G37340.1; AT2G37340.1; AT2G37340. [Q8VYA5-1]
DR Gramene; AT2G37340.2; AT2G37340.2; AT2G37340. [Q8VYA5-2]
DR Gramene; AT2G37340.3; AT2G37340.3; AT2G37340. [Q8VYA5-3]
DR Gramene; AT2G37340.4; AT2G37340.4; AT2G37340. [Q8VYA5-2]
DR Gramene; AT2G37340.5; AT2G37340.5; AT2G37340. [Q8VYA5-3]
DR Gramene; AT2G37340.6; AT2G37340.6; AT2G37340. [Q8VYA5-2]
DR KEGG; ath:AT2G37340; -.
DR Araport; AT2G37340; -.
DR TAIR; locus:2049766; AT2G37340.
DR eggNOG; KOG0107; Eukaryota.
DR HOGENOM; CLU_047187_3_0_1; -.
DR InParanoid; Q8VYA5; -.
DR OMA; CWVCEVL; -.
DR PhylomeDB; Q8VYA5; -.
DR PRO; PR:Q8VYA5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8VYA5; baseline and differential.
DR Genevisible; Q8VYA5; AT.
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: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 GO; GO:0000245; P:spliceosomal complex assembly; TAS: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; 2.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50158; ZF_CCHC; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Metal-binding; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Spliceosome; Zinc;
KW Zinc-finger.
FT CHAIN 1..290
FT /note="Serine/arginine-rich splicing factor RS2Z33"
FT /id="PRO_0000416998"
FT DOMAIN 11..81
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 99..116
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 121..138
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 135..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P92964"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P92964"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P92965"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16807317"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16807317"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16807317,
FT ECO:0007744|PubMed:19245862, ECO:0007744|PubMed:19376835"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16807317,
FT ECO:0007744|PubMed:19245862, ECO:0007744|PubMed:19376835"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16807317,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16807317,
FT ECO:0007744|PubMed:19245862, ECO:0007744|PubMed:19376835"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FYB7"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P92966"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P92966"
FT VAR_SEQ 1..49
FT /note="MPRYDDRYGNTRLYVGRLSSRTRTRDLERLFSRYGRVRDVDMKRDYAFV ->
FT MWENTPCMWSLLSSHFRNQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_043112"
FT VAR_SEQ 1..41
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_043113"
FT CONFLICT 50
FT /note="E -> V (in Ref. 6; BAD44429)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="S -> Q (in Ref. 1; CAC03605)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="R -> G (in Ref. 1; CAC03605)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 290 AA; 32893 MW; 4B0407A7E106EFA2 CRC64;
MPRYDDRYGN TRLYVGRLSS RTRTRDLERL FSRYGRVRDV DMKRDYAFVE FGDPRDADDA
RHYLDGRDFD GSRITVEFSR GAPRGSRDFD SRGPPPGAGR CFNCGVDGHW ARDCTAGDWK
NKCYRCGERG HIERNCKNSP KKLRRSGSYS RSPVRSRSPR RRRSPSRSLS RSRSYSRSRS
PVRRRERSVE ERSRSPKRMD DSLSPRARDR SPVLDDEGSP KIIDGSPPPS PKLQKEVGSD
RDGGSPQDNG RNSVVSPVVG AGGDSSKEDR SPVDDDYEPN RTSPRGSESP
