SUA_ARATH
ID SUA_ARATH Reviewed; 1007 AA.
AC F4JCU0; D5L2Y2; Q8VYR8; Q9M383;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 2.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=SUPPRESSOR OF ABI3-5 {ECO:0000312|EMBL:ADE44117.1};
DE AltName: Full=REQUIRED FOR SNC4-1D protein 1 {ECO:0000303|PubMed:25267732};
DE AltName: Full=Splicing factor SUA {ECO:0000305};
GN Name=SUA {ECO:0000312|EMBL:ADE44117.1};
GN Synonyms=RSN1 {ECO:0000303|PubMed:25267732};
GN OrderedLocusNames=At3g54230 {ECO:0000312|Araport:AT3G54230};
GN ORFNames=F24B22.190 {ECO:0000312|EMBL:CAB70997.1};
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), IDENTIFICATION, FUNCTION, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH U2AF65A.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=20525852; DOI=10.1105/tpc.110.074674;
RA Sugliani M., Brambilla V., Clerkx E.J., Koornneef M., Soppe W.J.;
RT "The conserved splicing factor SUA controls alternative splicing of the
RT developmental regulator ABI3 in Arabidopsis.";
RL Plant Cell 22:1936-1946(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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] (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 FUNCTION.
RX PubMed=25267732; DOI=10.1093/mp/ssu103;
RA Zhang Z., Liu Y., Ding P., Li Y., Kong Q., Zhang Y.;
RT "Splicing of receptor-like kinase-encoding SNC4 and CERK1 is regulated by
RT two conserved splicing factors that are required for plant immunity.";
RL Mol. Plant 7:1766-1775(2014).
CC -!- FUNCTION: Splicing factor that controls alternative splicing of the
CC developmental regulator ABI3. Reduces splicing of a cryptic intron in
CC ABI3, leading to a decreased in ABI3-beta transcript (PubMed:20525852).
CC Regulates the splicing of the receptor-like kinase SNC4/LRKL-2.6
CC (PubMed:25267732). {ECO:0000269|PubMed:20525852,
CC ECO:0000269|PubMed:25267732}.
CC -!- SUBUNIT: Interacts with the pre-spliceosomal component U2AF65A.
CC {ECO:0000269|PubMed:20525852}.
CC -!- INTERACTION:
CC F4JCU0; O23212: U2AF65A; NbExp=3; IntAct=EBI-4427912, EBI-4439005;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20525852}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4JCU0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4JCU0-2; Sequence=VSP_058194;
CC -!- TISSUE SPECIFICITY: Ubiquitous with highest expression in siliques
CC toward the end of seed maturation. {ECO:0000269|PubMed:20525852}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB70997.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; GU735482; ADE44117.1; -; mRNA.
DR EMBL; AL132957; CAB70997.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79201.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79202.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63793.1; -; Genomic_DNA.
DR EMBL; AY070066; AAL49823.1; -; mRNA.
DR EMBL; AY096433; AAM20073.1; -; mRNA.
DR PIR; T47582; T47582.
DR RefSeq; NP_001190084.1; NM_001203155.1. [F4JCU0-2]
DR RefSeq; NP_001325864.1; NM_001339655.1. [F4JCU0-1]
DR RefSeq; NP_190991.2; NM_115283.3. [F4JCU0-1]
DR AlphaFoldDB; F4JCU0; -.
DR IntAct; F4JCU0; 15.
DR STRING; 3702.AT3G54230.2; -.
DR iPTMnet; F4JCU0; -.
DR PaxDb; F4JCU0; -.
DR PRIDE; F4JCU0; -.
DR ProteomicsDB; 245226; -. [F4JCU0-1]
DR EnsemblPlants; AT3G54230.1; AT3G54230.1; AT3G54230. [F4JCU0-1]
DR EnsemblPlants; AT3G54230.2; AT3G54230.2; AT3G54230. [F4JCU0-2]
DR EnsemblPlants; AT3G54230.5; AT3G54230.5; AT3G54230. [F4JCU0-1]
DR GeneID; 824590; -.
DR Gramene; AT3G54230.1; AT3G54230.1; AT3G54230. [F4JCU0-1]
DR Gramene; AT3G54230.2; AT3G54230.2; AT3G54230. [F4JCU0-2]
DR Gramene; AT3G54230.5; AT3G54230.5; AT3G54230. [F4JCU0-1]
DR KEGG; ath:AT3G54230; -.
DR Araport; AT3G54230; -.
DR TAIR; locus:2080355; AT3G54230.
DR eggNOG; KOG0154; Eukaryota.
DR HOGENOM; CLU_012277_0_0_1; -.
DR InParanoid; F4JCU0; -.
DR OrthoDB; 786674at2759; -.
DR PhylomeDB; F4JCU0; -.
DR PRO; PR:F4JCU0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4JCU0; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IMP:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:TAIR.
DR GO; GO:0043484; P:regulation of RNA splicing; IMP:UniProtKB.
DR CDD; cd16166; OCRE_SUA_like; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR041591; OCRE.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR035623; SUA-like_OCRE.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR Pfam; PF01585; G-patch; 1.
DR Pfam; PF17780; OCRE; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00443; G_patch; 1.
DR SMART; SM00360; RRM; 2.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF54928; SSF54928; 2.
DR SUPFAM; SSF90209; SSF90209; 1.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS50102; RRM; 2.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Metal-binding; mRNA processing; mRNA splicing;
KW Nucleus; Reference proteome; Repeat; RNA-binding; Spliceosome; Zinc;
KW Zinc-finger.
FT CHAIN 1..1007
FT /note="SUPPRESSOR OF ABI3-5"
FT /id="PRO_0000435871"
FT DOMAIN 272..352
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 432..512
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 928..974
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT ZN_FING 378..407
FT /note="RanBP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT REGION 1..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..853
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..881
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 350
FT /note="S -> SS (in isoform 2)"
FT /id="VSP_058194"
FT CONFLICT 262
FT /note="N -> D (in Ref. 1; ADE44117)"
FT /evidence="ECO:0000305"
FT CONFLICT 495
FT /note="R -> G (in Ref. 1; ADE44117)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="A -> S (in Ref. 1; ADE44117)"
FT /evidence="ECO:0000305"
FT CONFLICT 889
FT /note="L -> F (in Ref. 1; ADE44117)"
FT /evidence="ECO:0000305"
FT CONFLICT 920
FT /note="I -> F (in Ref. 1; ADE44117)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1007 AA; 112567 MW; 63CE1EBCA8CF91B8 CRC64;
MDPSRYGRQQ EWDNNSAPEG YGTQHDPNHR FGVSYDDGYP DERLMRDDVY NYPPGHNTLG
DLPQSRKRNY EENYPSELRR QEKPYIDSNY AADYYHDSEA GSRNGHYRDH EHERSSRYDG
CDDYSCNDNN YRSKNYHHSR DDGREKDYDY TRRSYDSEYE RASVRDGSRK SRDPQDRERN
SRDREWDSRD REWDKRCYSR ERDESPHKRY EKSRSRSTGR GEFSRSRSPR GRSHGRSYRE
DSYEGDHWNE SERRREYEDR HNQDHFSATP SATVVVKGLS MKSTEEDLYQ ILAEWGPLHH
VRVIREQNSG ISRGFAFIDF PTVDAARTMM DRIEHDGIVL DGRKLMFHYS QPTGRAGVSR
RQEHASRRSY GGSRNMIVPT DWICTICGCI NFARRTSCFQ CNEPKTKDSP SADVGLSNSA
AGKRISETGP THVLVVRGLD EDADEEMLRY EFSKHAPIKD LRLVRDKFTH VSRGFAFVHF
YSVEDATKAL EATNRTALER NGKILRVAYA KSVHGSGTGI SAPSHSNNLA AAAIEAATFS
QQYDGVGWAP KEYNTGEKQN TGGQAQGVGE IESQKGTSAP QSGYVWDEAS GYYYDAASGY
YYDGNSGLYY DSNSGLWYSY DQQTQQYVPC PDQNNESKVT ENQPDSAKKE KSSQQKVIIS
AATTPNVEKV LSLPDAVQAA AAAAIASEKR EKERVKEIKL ASKTSLLASK KKMSNVLTMW
KQRSHETQIQ RPSPSLGDNP PTVSAEARSS FSTGQSMGKL KSDVIIAKER STSNHGVSAL
TTAESSSSST TGGTLMGVMR GSFGGTLGGA SSSASVQMPP ILPSASPASV SVSGSGRRRF
SETPTAGPTH REQPQTSYRD RAAERRNLYG SSTSSGNDVI DSSEDLMGLR KGSSDPTPFP
PGVGGRGITT STEVSSFDVI TEERAIDESN VGNRMLRNMG WHEGSGLGKD GSGMKEPVQA
QGVDRRAGLG SQQKKVDAEF EVQPGDTYRT LLHKKALARF RDMSDNN
