SR45A_ARATH
ID SR45A_ARATH Reviewed; 382 AA.
AC Q84TH4; Q940S1; Q949Y9; Q9LNV4;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Serine/arginine-rich splicing factor SR45a;
DE Short=At-SR45A;
DE Short=AtSR45a;
DE AltName: Full=Protein TRANSFORMER2-like;
DE Short=atTra2;
GN Name=SR45A; Synonyms=TRA2; OrderedLocusNames=At1g07350; ORFNames=F22G5.31;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1A; 2 AND 2B).
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [5]
RP ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, INTERACTION WITH RNU1, TISSUE
RP SPECIFICITY, AND INDUCTION BY HIGH-LIGHT; PARAQUAT AND SALT STRESS.
RX PubMed=17556373; DOI=10.1093/pcp/pcm069;
RA Tanabe N., Yoshimura K., Kimura A., Yabuta Y., Shigeoka S.;
RT "Differential expression of alternatively spliced mRNAs of Arabidopsis SR
RT protein homologs, atSR30 and atSR45a, in response to environmental
RT stress.";
RL Plant Cell Physiol. 48:1036-1049(2007).
RN [6]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH SR45; RNU1; PRP38; SCL28 AND
RP U2AF35B.
RC STRAIN=cv. Columbia;
RX PubMed=19238562; DOI=10.1007/s11103-009-9469-y;
RA Tanabe N., Kimura A., Yoshimura K., Shigeoka S.;
RT "Plant-specific SR-related protein atSR45a interacts with spliceosomal
RT proteins in plant nucleus.";
RL Plant Mol. Biol. 70:241-252(2009).
RN [7]
RP ALTERNATIVE SPLICING.
RX PubMed=19734266; DOI=10.1104/pp.109.141705;
RA Chung T., Wang D., Kim C.S., Yadegari R., Larkins B.A.;
RT "Plant SMU-1 and SMU-2 homologues regulate pre-mRNA splicing and multiple
RT aspects of development.";
RL Plant Physiol. 151:1498-1512(2009).
RN [8]
RP GENE FAMILY.
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 [9]
RP ALTERNATIVE SPLICING, AND INDUCTION BY ABIOTIC STRESS.
RX PubMed=22291167; DOI=10.3732/ajb.1100355;
RA Gulledge A.A., Roberts A.D., Vora H., Patel K., Loraine A.E.;
RT "Mining Arabidopsis thaliana RNA-seq data with Integrated Genome Browser
RT reveals stress-induced alternative splicing of the putative splicing
RT regulator SR45a.";
RL Am. J. Bot. 99:219-231(2012).
RN [10]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=23132568; DOI=10.1271/bbb.120425;
RA Mori T., Yoshimura K., Nosaka R., Sakuyama H., Koike Y., Tanabe N.,
RA Maruta T., Tamoi M., Shigeoka S.;
RT "Subcellular and subnuclear distribution of high-light responsive
RT serine/arginine-rich proteins, atSR45a and atSR30, in Arabidopsis
RT thaliana.";
RL Biosci. Biotechnol. Biochem. 76:2075-2081(2012).
CC -!- FUNCTION: Probable splicing factor involved in constitutive and/or
CC alternative splicing events. May bridge the 5' and 3' components of the
CC spliceosome. {ECO:0000269|PubMed:19238562}.
CC -!- SUBUNIT: Component of the spliceosome. Homodimer. Interacts with PRP38,
CC SCL28, SR45, RNU1 and U2AF35B. {ECO:0000269|PubMed:17556373,
CC ECO:0000269|PubMed:19238562}.
CC -!- INTERACTION:
CC Q84TH4; P92964: RS31; NbExp=3; IntAct=EBI-25519389, EBI-927132;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:17556373,
CC ECO:0000269|PubMed:23132568}. Note=The phosphorylation status has no
CC effect on the localization.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1a;
CC IsoId=Q84TH4-1; Sequence=Displayed;
CC Name=2b;
CC IsoId=Q84TH4-2; Sequence=VSP_054993, VSP_054994, VSP_054995;
CC Name=2;
CC IsoId=Q84TH4-3; Sequence=VSP_054993;
CC Name=1b;
CC IsoId=Q84TH4-4; Sequence=VSP_054994, VSP_054995;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems and roots.
CC {ECO:0000269|PubMed:17556373}.
CC -!- INDUCTION: Up-regulated early after high-light irradiation, but not by
CC paraquat or high salt. {ECO:0000269|PubMed:17556373,
CC ECO:0000269|PubMed:22291167}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:23132568}.
CC -!- MISCELLANEOUS: The splicing patterns of the pre-mRNA are similar
CC throughout the developmental period, but change in response to various
CC types of stress treatment (PubMed:17556373, PubMed:22291167).
CC {ECO:0000305|PubMed:17556373, ECO:0000305|PubMed:22291167}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. SR45 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: According to PubMed:20884799, this protein should not be
CC regarded as a classical SR protein. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79558.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC022464; AAF79558.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28112.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28113.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60737.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60738.1; -; Genomic_DNA.
DR EMBL; BT005797; AAO64199.1; -; mRNA.
DR EMBL; AY053418; AAK96648.1; -; mRNA.
DR EMBL; AY050800; AAK92735.1; -; mRNA.
DR RefSeq; NP_001323001.1; NM_001331692.1. [Q84TH4-2]
DR RefSeq; NP_001323002.1; NM_001331694.1. [Q84TH4-4]
DR RefSeq; NP_563787.2; NM_100609.4. [Q84TH4-1]
DR RefSeq; NP_849605.1; NM_179274.2. [Q84TH4-2]
DR AlphaFoldDB; Q84TH4; -.
DR SMR; Q84TH4; -.
DR BioGRID; 22487; 7.
DR IntAct; Q84TH4; 1.
DR STRING; 3702.AT1G07350.1; -.
DR iPTMnet; Q84TH4; -.
DR PaxDb; Q84TH4; -.
DR PRIDE; Q84TH4; -.
DR ProteomicsDB; 226860; -. [Q84TH4-1]
DR EnsemblPlants; AT1G07350.1; AT1G07350.1; AT1G07350. [Q84TH4-1]
DR EnsemblPlants; AT1G07350.2; AT1G07350.2; AT1G07350. [Q84TH4-2]
DR EnsemblPlants; AT1G07350.3; AT1G07350.3; AT1G07350. [Q84TH4-2]
DR EnsemblPlants; AT1G07350.5; AT1G07350.5; AT1G07350. [Q84TH4-4]
DR GeneID; 837246; -.
DR Gramene; AT1G07350.1; AT1G07350.1; AT1G07350. [Q84TH4-1]
DR Gramene; AT1G07350.2; AT1G07350.2; AT1G07350. [Q84TH4-2]
DR Gramene; AT1G07350.3; AT1G07350.3; AT1G07350. [Q84TH4-2]
DR Gramene; AT1G07350.5; AT1G07350.5; AT1G07350. [Q84TH4-4]
DR KEGG; ath:AT1G07350; -.
DR Araport; AT1G07350; -.
DR TAIR; locus:2025092; AT1G07350.
DR eggNOG; KOG4661; Eukaryota.
DR HOGENOM; CLU_050438_0_0_1; -.
DR InParanoid; Q84TH4; -.
DR OMA; YSERKPS; -.
DR OrthoDB; 1524134at2759; -.
DR PRO; PR:Q84TH4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q84TH4; baseline and differential.
DR Genevisible; Q84TH4; AT.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0043484; P:regulation of RNA splicing; IMP:TAIR.
DR GO; GO:0009644; P:response to high light intensity; IMP:TAIR.
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 Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Ribonucleoprotein; Spliceosome.
FT CHAIN 1..382
FT /note="Serine/arginine-rich splicing factor SR45a"
FT /id="PRO_0000429598"
FT REGION 30..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..30
FT /note="Missing (in isoform 2b and isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_054993"
FT VAR_SEQ 150..159
FT /note="KARRRRGRTP -> KFLWQQVCCL (in isoform 2b and isoform
FT 1b)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_054994"
FT VAR_SEQ 160..382
FT /note="Missing (in isoform 2b and isoform 1b)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_054995"
SQ SEQUENCE 382 AA; 44978 MW; FFD7E9C734D89D19 CRC64;
MGKREIHFTP VGRQVQRVLE YPLRLENRSP MSYSRRSRYS PSLSPYDKRR GRSVSRSLSR
SPTRSVSSDA ENPGNSLYVT GLSHRVTERD LEDHFAKEGK VTDVHLVLDP WTRESRGFGF
ISMKSVGDAN RCIRSLDHSV LQGRVITVEK ARRRRGRTPT PGKYLGLRTA RGRHKSPSYS
PRRSVSCSRS RSRSYSSDRG RSYSPSYGRR GRSSSYSPFY RRRRFYSPSR SPSPDDRYNR
RRDRSYSPYY RRRDRSRSYS RNCRARDRSP YYMRRYRSRS RSYSPRYRAR DRSCSPYYRG
RDRSYSPHYQ GRDRSYSPES RYYRRHRSVS GSVSPGGRSM SRSISPRKGR KESRSKSRRH
DRQSSMCHSR SARSSTSRSV SP
