SMU2_ARATH
ID SMU2_ARATH Reviewed; 585 AA.
AC O48713;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Suppressor of mec-8 and unc-52 protein homolog 2;
DE Short=AtSMU-2;
DE AltName: Full=Protein RED-like;
DE AltName: Full=RNA splicing protein SMU2;
GN Name=SMU2; OrderedLocusNames=At2g26460; ORFNames=T9J22.13;
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 [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 [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].
RA Cheuk R., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kim C.J., Chen H., Cheuk R., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-579, AND IDENTIFICATION BY
RP MASS 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 [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND INTERACTION WITH SMU1.
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).
CC -!- FUNCTION: Auxiliary spliceosomal protein involved in splicing of
CC specific pre-mRNAs that affect multiple aspects of development.
CC {ECO:0000269|PubMed:19734266}.
CC -!- SUBUNIT: Component of the spliceosome. Interacts with SMU1.
CC {ECO:0000269|PubMed:19734266}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19734266}.
CC -!- TISSUE SPECIFICITY: Highly expressed in seedlings at 7 days after
CC germination, young flowers before anthesis and developing siliques.
CC Expressed at lower levels in roots, expanding leaves, open flowers, dry
CC seeds and inflorescences. Not detected in senescing leaves.
CC {ECO:0000269|PubMed:19734266}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, but slower growth.
CC {ECO:0000269|PubMed:19734266}.
CC -!- SIMILARITY: Belongs to the RED family. {ECO:0000305}.
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DR EMBL; AC002505; AAC14495.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07841.1; -; Genomic_DNA.
DR EMBL; BT011249; AAR92285.1; -; mRNA.
DR EMBL; BT012549; AAS99693.1; -; mRNA.
DR PIR; T00979; T00979.
DR RefSeq; NP_180214.1; NM_128203.2.
DR AlphaFoldDB; O48713; -.
DR BioGRID; 2539; 1.
DR STRING; 3702.AT2G26460.1; -.
DR iPTMnet; O48713; -.
DR PaxDb; O48713; -.
DR PRIDE; O48713; -.
DR ProteomicsDB; 234472; -.
DR EnsemblPlants; AT2G26460.1; AT2G26460.1; AT2G26460.
DR GeneID; 817187; -.
DR Gramene; AT2G26460.1; AT2G26460.1; AT2G26460.
DR KEGG; ath:AT2G26460; -.
DR Araport; AT2G26460; -.
DR TAIR; locus:2066221; AT2G26460.
DR eggNOG; KOG2498; Eukaryota.
DR HOGENOM; CLU_026814_1_0_1; -.
DR InParanoid; O48713; -.
DR OMA; EPEYKSA; -.
DR OrthoDB; 500537at2759; -.
DR PhylomeDB; O48713; -.
DR PRO; PR:O48713; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O48713; baseline and differential.
DR Genevisible; O48713; AT.
DR GO; GO:0016607; C:nuclear speck; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; IMP:TAIR.
DR InterPro; IPR039896; Red-like.
DR InterPro; IPR012492; RED_C.
DR InterPro; IPR012916; RED_N.
DR PANTHER; PTHR12765; PTHR12765; 1.
DR Pfam; PF07807; RED_C; 1.
DR Pfam; PF07808; RED_N; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..585
FT /note="Suppressor of mec-8 and unc-52 protein homolog 2"
FT /id="PRO_0000429842"
FT REPEAT 16..17
FT /note="R-[ED] 1"
FT REPEAT 29..30
FT /note="R-[ED] 2"
FT REPEAT 36..37
FT /note="R-[ED] 3"
FT REPEAT 258..259
FT /note="R-[ED] 4"
FT REPEAT 322..323
FT /note="R-[ED] 5"
FT REPEAT 436..437
FT /note="R-[ED] 6"
FT REPEAT 445..446
FT /note="R-[ED] 7"
FT REPEAT 450..451
FT /note="R-[ED] 8"
FT REPEAT 540..541
FT /note="R-[ED] 9"
FT REPEAT 542..543
FT /note="R-[ED] 10"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 579
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 585 AA; 66331 MW; 77AC4B56A6BE5227 CRC64;
MKPSKSHHKE KTARRREEKL EESDNPKYRD RAKERRENQN PDYDPSELSS FHAVAPPGAV
DIRAADALKI SIENSKYLGG DVEHTHLVKG LDYALLNKVR SEIVKKPDGE DGDGGKTSAP
KEDQRVTFRT IAAKSVYQWI VKPQTIIKSN EMFLPGRMTF VYDMEGGYTH DIPTTLYRSK
ADCPVPEEFV TVNVDGSVLD RIAKIMSYLR LGSSGKVLKK KKKEKDGKGK MSTIANDYDE
DDNKSKIENG SSVNISDREV LPPPPPLPPG INHLDLSTKQ EEPPVARTDD DDIFVGEGVD
YTVPGKDVTQ SPISEDMEES PRDKEKVSYF DEPAYGPVQE KVPYFAEPAY GPVQPSAGQE
WQDMSAYGAM QTQGLAPGYP GEWQEYQYAE QTGYQEQYLQ PGMEGYEVQP ETDVLLDPQL
MSQEEKDRGL GSVFKRDDQR LQQLRESDAR EKDPTFVSES YSECYPGYQE YNHEIVGSDE
EPDLSKMDMG GKAKGGLHRW DFETEEEWEK YNEQKEAMPK AAFQFGVKMQ DGRKTRKQNR
DRDQKLNNEL HQINKILTRK KMEKEGGDVA SLDAAEAQTP KRSKH
