SPF27_ARATH
ID SPF27_ARATH Reviewed; 253 AA.
AC Q949S9; Q9LV24;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Pre-mRNA-splicing factor SPF27 homolog;
DE AltName: Full=Modifier of SNC1 member 4;
DE AltName: Full=Protein BCAS2 homolog;
GN Name=MOS4; Synonyms=BCAS2, SPF27; OrderedLocusNames=At3g18165;
GN ORFNames=MRC8.16;
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], SUBCELLULAR LOCATION, INTERACTION WITH CDC5,
RP DISRUPTION PHENOTYPE, COMPONENT OF THE MAC COMPLEX, AND FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=17575050; DOI=10.1101/gad.1559607;
RA Palma K., Zhao Q., Cheng Y.T., Bi D., Monaghan J., Cheng W., Zhang Y.,
RA Li X.;
RT "Regulation of plant innate immunity by three proteins in a complex
RT conserved across the plant and animal kingdoms.";
RL Genes Dev. 21:1484-1493(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
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].
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND COMPONENT OF THE MAC COMPLEX.
RX PubMed=19629177; DOI=10.1371/journal.ppat.1000526;
RA Monaghan J., Xu F., Gao M., Zhao Q., Palma K., Long C., Chen S., Zhang Y.,
RA Li X.;
RT "Two Prp19-like U-box proteins in the MOS4-associated complex play
RT redundant roles in plant innate immunity.";
RL PLoS Pathog. 5:E1000526-E1000526(2009).
RN [7]
RP FUNCTION, AND INTERACTION WITH CYCL1-1.
RX PubMed=22248079; DOI=10.1111/j.1365-313x.2012.04906.x;
RA Xu F., Xu S., Wiermer M., Zhang Y., Li X.;
RT "The cyclin L homolog MOS12 and the MOS4-associated complex are required
RT for the proper splicing of plant resistance genes.";
RL Plant J. 70:916-928(2012).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ENY2, AND SUBCELLULAR
RP LOCATION.
RX PubMed=29588169; DOI=10.1016/j.jmb.2018.03.018;
RA Pfab A., Bruckmann A., Nazet J., Merkl R., Grasser K.D.;
RT "The adaptor protein ENY2 is a component of the deubiquitination module of
RT the Arabidopsis SAGA transcriptional co-activator complex but not of the
RT TREX-2 complex.";
RL J. Mol. Biol. 430:1479-1494(2018).
CC -!- FUNCTION: Component of the MAC complex that probably regulates defense
CC responses through transcriptional control and thereby is essential for
CC plant innate immunity. Involved in mRNA splicing.
CC {ECO:0000269|PubMed:17575050, ECO:0000269|PubMed:22248079}.
CC -!- SUBUNIT: Component of the multiprotein assembly MOS4-associated complex
CC (MAC) at least composed of MOS4, CDC5 and PRL1 (PubMed:19629177).
CC Interacts with CYCL1-1 and CDC5 (PubMed:22248079). Associated with the
CC spliceosome (PubMed:22248079). Interacts with ENY2 (PubMed:29588169).
CC {ECO:0000269|PubMed:19629177, ECO:0000269|PubMed:22248079,
CC ECO:0000269|PubMed:29588169}.
CC -!- INTERACTION:
CC Q949S9; P92948: CDC5; NbExp=3; IntAct=EBI-1382943, EBI-1382948;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17575050,
CC ECO:0000269|PubMed:29588169}.
CC -!- DISRUPTION PHENOTYPE: Enhanced susceptibility to virulent and avirulent
CC pathogens. {ECO:0000269|PubMed:17575050}.
CC -!- SIMILARITY: Belongs to the SPF27 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02029.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; EF688334; ABS20115.1; -; mRNA.
DR EMBL; AB020749; BAB02029.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76058.1; -; Genomic_DNA.
DR EMBL; AY050910; AAK93587.1; -; mRNA.
DR EMBL; AY091412; AAM14351.1; -; mRNA.
DR EMBL; AY088112; AAM65658.1; -; mRNA.
DR RefSeq; NP_566599.1; NM_112699.3.
DR AlphaFoldDB; Q949S9; -.
DR SMR; Q949S9; -.
DR BioGRID; 6676; 11.
DR IntAct; Q949S9; 24.
DR STRING; 3702.AT3G18165.1; -.
DR PaxDb; Q949S9; -.
DR PRIDE; Q949S9; -.
DR ProteomicsDB; 245335; -.
DR EnsemblPlants; AT3G18165.1; AT3G18165.1; AT3G18165.
DR GeneID; 821343; -.
DR Gramene; AT3G18165.1; AT3G18165.1; AT3G18165.
DR KEGG; ath:AT3G18165; -.
DR Araport; AT3G18165; -.
DR TAIR; locus:505006356; AT3G18165.
DR eggNOG; KOG3096; Eukaryota.
DR HOGENOM; CLU_082523_0_0_1; -.
DR InParanoid; Q949S9; -.
DR OMA; SHLSMRH; -.
DR OrthoDB; 1607056at2759; -.
DR PhylomeDB; Q949S9; -.
DR PRO; PR:Q949S9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q949S9; baseline and differential.
DR Genevisible; Q949S9; AT.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0000974; C:Prp19 complex; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR008409; SPF27.
DR PANTHER; PTHR13296; PTHR13296; 1.
DR Pfam; PF05700; BCAS2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Immunity; Innate immunity; mRNA processing; mRNA splicing;
KW Nucleus; Plant defense; Reference proteome; Spliceosome.
FT CHAIN 1..253
FT /note="Pre-mRNA-splicing factor SPF27 homolog"
FT /id="PRO_0000391631"
FT COILED 124..235
FT /evidence="ECO:0000255"
SQ SEQUENCE 253 AA; 29680 MW; 04323FBBFD7F92FD CRC64;
MATNNGDVLM LEATPEAARP WASAANAEVI DALPYIDDDY GNPLIKSEVD RLVEEEMRRS
SKKPADFLKD LPPLPKFDFK NCPVLGKEYE RVRAGKPPVR IDFESRYKLE MPPANKRNDD
AAWKQYLQKN QRSLQQKLIE LENLELMSKL GPELWRQNNH RLEVFLTRMQ RLAQEQNEEI
EKVNRERKYH QQTTSYELNA LSQEWRQLCV KNMEIQSACA MLETQIDSFK KEAAERGWNL
EEKLENVEPL QMQ
