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Serine/arginine-rich splicing factor SR45 (At-SR45) (AtSR45)

 SR45_ARATH              Reviewed;         414 AA.
Q9SEE9; F4I4H8; Q5E925; Q94AS1;
03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
23-MAY-2018, entry version 144.
RecName: Full=Serine/arginine-rich splicing factor SR45;
Short=At-SR45;
Short=AtSR45;
Name=SR45; Synonyms=RNPS1; OrderedLocusNames=At1g16610;
ORFNames=F19K19.9;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH AFC2; RNU1
AND SCL33, PHOSPHORYLATION BY AFC2, AND TISSUE SPECIFICITY.
PubMed=10593939; DOI=10.1074/jbc.274.51.36428;
Golovkin M., Reddy A.S.N.;
"An SC35-like protein and a novel serine/arginine-rich protein
interact with Arabidopsis U1-70K protein.";
J. Biol. Chem. 274:36428-36438(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=cv. Columbia;
Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
[6]
SUBCELLULAR LOCATION, PHOSPHORYLATION, TISSUE SPECIFICITY, AND
INTERACTION WITH RNU1.
PubMed=14675452; DOI=10.1046/j.1365-313X.2003.01932.x;
Ali G.S., Golovkin M., Reddy A.S.N.;
"Nuclear localization and in vivo dynamics of a plant-specific
serine/arginine-rich protein.";
Plant J. 36:883-893(2003).
[7]
REVIEW.
PubMed=15270675; DOI=10.1042/BST0320561;
Kalyna M., Barta A.;
"A plethora of plant serine/arginine-rich proteins: redundancy or
evolution of novel gene functions?";
Biochem. Soc. Trans. 32:561-564(2004).
[8]
SUBCELLULAR LOCATION.
PubMed=16895966; DOI=10.1242/jcs.03144;
Ali G.S., Reddy A.S.;
"ATP, phosphorylation and transcription regulate the mobility of plant
splicing factors.";
J. Cell Sci. 119:3527-3538(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=16807317; DOI=10.1093/nar/gkl429;
de la Fuente van Bentem S., Anrather D., Roitinger E., Djamei A.,
Hufnagl T., Barta A., Csaszar E., Dohnal I., Lecourieux D., Hirt H.;
"Phosphoproteomics reveals extensive in vivo phosphorylation of
Arabidopsis proteins involved in RNA metabolism.";
Nucleic Acids Res. 34:3267-3278(2006).
[10]
ALTERNATIVE SPLICING, AND INDUCTION.
PubMed=17319848; DOI=10.1111/j.1365-313X.2006.03020.x;
Palusa S.G., Ali G.S., Reddy A.S.;
"Alternative splicing of pre-mRNAs of Arabidopsis serine/arginine-rich
proteins: regulation by hormones and stresses.";
Plant J. 49:1091-1107(2007).
[11]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=17534421; DOI=10.1371/journal.pone.0000471;
Ali G.S., Palusa S.G., Golovkin M., Prasad J., Manley J.L.,
Reddy A.S.;
"Regulation of plant developmental processes by a novel splicing
factor.";
PLoS ONE 2:E471-E471(2007).
[12]
ALTERNATIVE SPLICING.
PubMed=18402682; DOI=10.1186/1471-2164-9-159;
Schindler S., Szafranski K., Hiller M., Ali G.S., Palusa S.G.,
Backofen R., Platzer M., Reddy A.S.N.;
"Alternative splicing at NAGNAG acceptors in Arabidopsis thaliana SR
and SR-related protein-coding genes.";
BMC Genomics 9:159-159(2008).
[13]
SUBCELLULAR LOCATION, AND INTERACTION WITH RNU1.
PubMed=18414657; DOI=10.1371/journal.pone.0001953;
Ali G.S., Prasad K.V., Hanumappa M., Reddy A.S.;
"Analyses of in vivo interaction and mobility of two spliceosomal
proteins using FRAP and BiFC.";
PLoS ONE 3:E1953-E1953(2008).
[14]
SUBCELLULAR LOCATION.
STRAIN=cv. Columbia;
PubMed=19435936; DOI=10.1105/tpc.108.060434;
Koroleva O.A., Calder G., Pendle A.F., Kim S.H., Lewandowska D.,
Simpson C.G., Jones I.M., Brown J.W.S., Shaw P.J.;
"Dynamic behavior of Arabidopsis eIF4A-III, putative core protein of
exon junction complex: fast relocation to nucleolus and splicing
speckles under hypoxia.";
Plant Cell 21:1592-1606(2009).
[15]
FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF 218-THR-SER-219, TISSUE
SPECIFICITY, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, AND INDUCTION
BY ABIOTIC STRESSES.
PubMed=19403727; DOI=10.1104/pp.109.138180;
Zhang X.-N., Mount S.M.;
"Two alternatively spliced isoforms of the Arabidopsis SR45 protein
have distinct roles during normal plant development.";
Plant Physiol. 150:1450-1458(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-256, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[17]
GENE FAMILY.
PubMed=20884799; DOI=10.1105/tpc.110.078352;
Barta A., Kalyna M., Reddy A.S.;
"Implementing a rational and consistent nomenclature for
serine/arginine-rich protein splicing factors (SR proteins) in
plants.";
Plant Cell 22:2926-2929(2010).
[18]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=20699397; DOI=10.1104/pp.110.155523;
Carvalho R.F., Carvalho S.D., Duque P.;
"The plant-specific SR45 protein negatively regulates glucose and ABA
signaling during early seedling development in Arabidopsis.";
Plant Physiol. 154:772-783(2010).
[19]
GENE FAMILY.
PubMed=21935421; DOI=10.1371/journal.pone.0024542;
Richardson D.N., Rogers M.F., Labadorf A., Ben-Hur A., Guo H.,
Paterson A.H., Reddy A.S.N.;
"Comparative analysis of serine/arginine-rich proteins across 27
eukaryotes: insights into sub-family classification and extent of
alternative splicing.";
PLoS ONE 6:E24542-E24542(2011).
[20]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=22274613; DOI=10.4161/epi.7.1.18782;
Ausin I., Greenberg M.V., Li C.F., Jacobsen S.E.;
"The splicing factor SR45 affects the RNA-directed DNA methylation
pathway in Arabidopsis.";
Epigenetics 7:29-33(2012).
[21]
INTERACTION WITH SKIP.
PubMed=22942380; DOI=10.1105/tpc.112.100081;
Wang X., Wu F., Xie Q., Wang H., Wang Y., Yue Y., Gahura O., Ma S.,
Liu L., Cao Y., Jiao Y., Puta F., McClung C.R., Xu X., Ma L.;
"SKIP is a component of the spliceosome linking alternative splicing
and the circadian clock in Arabidopsis.";
Plant Cell 24:3278-3295(2012).
[22]
FUNCTION, AND INTERACTION WITH RNU1; U2AF35A AND U2AF35B.
PubMed=22563826; DOI=10.1111/j.1365-313X.2012.05042.x;
Day I.S., Golovkin M., Palusa S.G., Link A., Ali G.S., Thomas J.,
Richardson D.N., Reddy A.S.;
"Interactions of SR45, an SR-like protein, with spliceosomal proteins
and an intronic sequence: insights into regulated splicing.";
Plant J. 71:936-947(2012).
[23]
SUBCELLULAR LOCATION.
PubMed=23454656; DOI=10.1016/j.febslet.2013.02.041;
Baldwin K.L., Dinh E.M., Hart B.M., Masson P.H.;
"CACTIN is an essential nuclear protein in Arabidopsis and may be
associated with the eukaryotic spliceosome.";
FEBS Lett. 587:873-879(2013).
-!- FUNCTION: Involved in 5' and 3' splicing site selection of
introns, and may bridge the 5' and 3' components of the
spliceosome. Isoform 1 is required during flower petal development
and isoform 2 is involved in root growth. Regulates negatively
glucose and abscisic acid (ABA) signaling during early seedling
development. Involved in the RNA-directed DNA methylation pathway
(PubMed:22274613). {ECO:0000269|PubMed:17534421,
ECO:0000269|PubMed:19403727, ECO:0000269|PubMed:20699397,
ECO:0000269|PubMed:22274613, ECO:0000269|PubMed:22563826}.
-!- SUBUNIT: Component of the spliceosome. Interacts with AFC2,
U2AF35A, U2AF35B, RNU1, SCL33 and SKIP. The interaction with AFC2
depends on phosphorylation status. Interaction with RNU1 defines
initial 5' splice sites and interaction with U2AF35B 3' splice
sites in the early stage of spliceosome assembly.
{ECO:0000269|PubMed:10593939, ECO:0000269|PubMed:14675452,
ECO:0000269|PubMed:18414657, ECO:0000269|PubMed:22563826,
ECO:0000269|PubMed:22942380}.
-!- INTERACTION:
Q9LY75:CYP63; NbExp=2; IntAct=EBI-1792008, EBI-2360522;
Q42404:RNU1; NbExp=4; IntAct=EBI-1792008, EBI-1633812;
Q9SEU4:SCL33; NbExp=3; IntAct=EBI-1792008, EBI-927103;
-!- SUBCELLULAR LOCATION: Nucleus speckle
{ECO:0000269|PubMed:14675452, ECO:0000269|PubMed:16895966,
ECO:0000269|PubMed:18414657, ECO:0000269|PubMed:19435936}.
Nucleus, nucleoplasm {ECO:0000269|PubMed:14675452,
ECO:0000269|PubMed:16895966}. Note=Colocalizes with spliceosome
components. During interphase, present in both nuclear speckles
and nucleoplasm. Nucleoplasm-speckle shuttling protein. The
intranuclear distribution and mobility depend on the
phosphorylation status, ATP and transcription activity.
{ECO:0000269|PubMed:14675452, ECO:0000269|PubMed:16895966}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=SR45.1;
IsoId=Q9SEE9-1; Sequence=Displayed;
Name=2; Synonyms=SR45.2;
IsoId=Q9SEE9-2; Sequence=VSP_044313;
Name=3;
IsoId=Q9SEE9-3; Sequence=VSP_044314;
Note=Derived from EST data. No experimental confirmation
available.;
-!- TISSUE SPECIFICITY: Especially present in actively growing regions
and dividing cells. Mostly expressed in roots (primary and
secondary root meristem), shoot apical meristem (SAM), leaf
primordia, pollen and inflorescence, and, to a lower extent, in
leaves, vascular tissue, hydathode and fruits.
{ECO:0000269|PubMed:10593939, ECO:0000269|PubMed:14675452,
ECO:0000269|PubMed:19403727}.
-!- INDUCTION: Levels of the isoform 2 are altered in response to
sucrose depletion (Suc) and temperature changes; reduced in cold
but increased in warm temperatures. {ECO:0000269|PubMed:17319848,
ECO:0000269|PubMed:19403727}.
-!- PTM: Phosphorylated by AFC2. The phosphorylation status regulates
intranuclear distribution. {ECO:0000269|PubMed:10593939,
ECO:0000269|PubMed:14675452}.
-!- DISRUPTION PHENOTYPE: Several developmental defects, including
defects in flower and leaf morphology (petal development), delayed
flowering time and root growth. Hypersensitivity to glucose (Glc)
and to abscisic acid (ABA) during early seedling growth,
accompanied with an enhanced ability to accumulate ABA in response
to Glc. DNA methylation establishment and maintenance defects.
Altered alternative splicing pattern of several related SR genes.
{ECO:0000269|PubMed:17534421, ECO:0000269|PubMed:19403727,
ECO:0000269|PubMed:20699397, ECO:0000269|PubMed:22274613}.
-!- MISCELLANEOUS: The splicing pattern of the pre-mRNA is regulated
in a tissue-specific manner and by development, and changes in
response to various types of abiotic stresses.
{ECO:0000305|PubMed:17319848}.
-!- SIMILARITY: Belongs to the splicing factor SR family. SR45
subfamily. {ECO:0000305}.
-!- CAUTION: According to PubMed:20884799, this protein should not be
regarded as a classical SR protein although it could complement an
animal in vitro splicing extract deficient in SR proteins.
{ECO:0000305|PubMed:17534421}.
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EMBL; AF151366; AAF19004.1; -; mRNA.
EMBL; AC011808; AAG10821.1; -; Genomic_DNA.
EMBL; CP002684; AEE29475.1; -; Genomic_DNA.
EMBL; CP002684; AEE29476.1; -; Genomic_DNA.
EMBL; CP002684; AEE29477.1; -; Genomic_DNA.
EMBL; AY045835; AAK76509.1; -; mRNA.
EMBL; BT020372; AAV85727.1; -; mRNA.
EMBL; BT021095; AAX12865.1; -; mRNA.
PIR; C86301; C86301.
RefSeq; NP_001185014.1; NM_001198085.1. [Q9SEE9-3]
RefSeq; NP_173107.1; NM_101523.4. [Q9SEE9-1]
RefSeq; NP_973844.1; NM_202115.3. [Q9SEE9-2]
UniGene; At.11865; -.
ProteinModelPortal; Q9SEE9; -.
SMR; Q9SEE9; -.
BioGrid; 23470; 16.
IntAct; Q9SEE9; 7.
MINT; Q9SEE9; -.
STRING; 3702.AT1G16610.3; -.
iPTMnet; Q9SEE9; -.
PaxDb; Q9SEE9; -.
PRIDE; Q9SEE9; -.
EnsemblPlants; AT1G16610.1; AT1G16610.1; AT1G16610. [Q9SEE9-1]
EnsemblPlants; AT1G16610.2; AT1G16610.2; AT1G16610. [Q9SEE9-2]
EnsemblPlants; AT1G16610.3; AT1G16610.3; AT1G16610. [Q9SEE9-3]
EnsemblPlants; AT1G16610.7; AT1G16610.7; AT1G16610.
GeneID; 838230; -.
Gramene; AT1G16610.1; AT1G16610.1; AT1G16610. [Q9SEE9-1]
Gramene; AT1G16610.2; AT1G16610.2; AT1G16610. [Q9SEE9-2]
Gramene; AT1G16610.3; AT1G16610.3; AT1G16610. [Q9SEE9-3]
Gramene; AT1G16610.7; AT1G16610.7; AT1G16610.
KEGG; ath:AT1G16610; -.
Araport; AT1G16610; -.
TAIR; locus:2017948; AT1G16610.
eggNOG; KOG0118; Eukaryota.
eggNOG; COG0724; LUCA.
InParanoid; Q9SEE9; -.
KO; K14325; -.
OMA; PNFGRGV; -.
Reactome; R-ATH-72163; mRNA Splicing - Major Pathway.
Reactome; R-ATH-72187; mRNA 3'-end processing.
Reactome; R-ATH-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
PRO; PR:Q9SEE9; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9SEE9; baseline and differential.
Genevisible; Q9SEE9; AT.
GO; GO:0016607; C:nuclear speck; IDA:TAIR.
GO; GO:0005730; C:nucleolus; IDA:TAIR.
GO; GO:0005654; C:nucleoplasm; IDA:TAIR.
GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0000398; P:mRNA splicing, via spliceosome; IPI:TAIR.
GO; GO:0008380; P:RNA splicing; NAS:TAIR.
GO; GO:0010182; P:sugar mediated signaling pathway; IMP:TAIR.
CDD; cd12365; RRM_RNPS1; 1.
Gene3D; 3.30.70.330; -; 1.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR034201; RNPS1_RRM.
InterPro; IPR000504; RRM_dom.
Pfam; PF00076; RRM_1; 1.
SMART; SM00360; RRM; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50102; RRM; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; mRNA processing;
mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
RNA-binding; Spliceosome.
CHAIN 1 414 Serine/arginine-rich splicing factor
SR45.
/FTId=PRO_0000419679.
DOMAIN 98 176 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
MOTIF 62 69 Nuclear localization signal 1.
{ECO:0000250}.
MOTIF 229 236 Nuclear localization signal 2.
{ECO:0000250}.
MOTIF 284 291 Nuclear localization signal 3.
{ECO:0000250}.
MOTIF 318 325 Nuclear localization signal 4.
{ECO:0000250}.
MOTIF 338 345 Nuclear localization signal 5.
{ECO:0000250}.
MOTIF 373 380 Nuclear localization signal 6.
{ECO:0000250}.
COMPBIAS 10 60 Ser-rich.
COMPBIAS 78 82 Poly-Pro.
COMPBIAS 176 411 Pro-rich.
COMPBIAS 344 404 Ser-rich.
SITE 218 219 Required for isoform 1 function in petal
development.
MOD_RES 77 77 Phosphoserine.
{ECO:0000244|PubMed:16807317,
ECO:0000244|PubMed:19376835}.
MOD_RES 256 256 Phosphoserine.
{ECO:0000244|PubMed:19376835}.
VAR_SEQ 218 225 TSPQRKTG -> R (in isoform 2).
{ECO:0000303|Ref.5}.
/FTId=VSP_044313.
VAR_SEQ 353 353 K -> KYVGTHLNFFLG (in isoform 3).
{ECO:0000305}.
/FTId=VSP_044314.
MUTAGEN 218 219 TS->AA: Mimics isoform 2 function in
roots. {ECO:0000269|PubMed:19403727}.
CONFLICT 361 361 R -> P (in Ref. 4; AAK76509).
{ECO:0000305}.
SEQUENCE 414 AA; 45348 MW; C3457F2319D8C983 CRC64;
MAKPSRGRRS PSVSGSSSRS SSRSRSGSSP SRSISRSRSR SRSLSSSSSP SRSVSSGSRS
PPRRGKSPAG PARRGRSPPP PPSKGASSPS KKAVQESLVL HVDSLSRNVN EAHLKEIFGN
FGEVIHVEIA MDRAVNLPRG HGYVEFKARA DAEKAQLYMD GAQIDGKVVK ATFTLPPRQK
VSSPPKPVSA APKRDAPKSD NAAADAEKDG GPRRPRETSP QRKTGLSPRR RSPLPRRGLS
PRRRSPDSPH RRRPGSPIRR RGDTPPRRRP ASPSRGRSPS SPPPRRYRSP PRGSPRRIRG
SPVRRRSPLP LRRRSPPPRR LRSPPRRSPI RRRSRSPIRR PGRSRSSSIS PRKGRGPAGR
RGRSSSYSSS PSPRRIPRKI SRSRSPKRPL RGKRSSSNSS SSSSPPPPPP PRKT


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CNTLN_HUMAN Mouse ELISA Kit FOR Serine per arginine-rich splicing factor 12 96T
pro-1352 Recombinant Human Serine per arginine-Rich Splicing Factor 1 20
E1213r Human ELISA Kit FOR Serine per arginine-rich splicing factor 8 96T


 

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