SIB1_ARATH
ID SIB1_ARATH Reviewed; 151 AA.
AC Q9LDH1;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Sigma factor binding protein 1, chloroplastic;
DE Short=AtsibI;
DE Short=Sigma factor binding protein I;
DE AltName: Full=SigA binding protein;
DE AltName: Full=VQ motif-containing protein 23 {ECO:0000303|PubMed:22535423};
DE Short=AtVQ23 {ECO:0000303|PubMed:22535423};
DE Flags: Precursor;
GN Name=SIB1; Synonyms=VQ23 {ECO:0000303|PubMed:22535423};
GN OrderedLocusNames=At3g56710; ORFNames=T8M16.40;
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], INTERACTION WITH SIGA, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND INDUCTION BY LIGHT.
RX PubMed=11943170; DOI=10.1016/s0014-5793(02)02388-8;
RA Morikawa K., Shiina T., Murakami S., Toyoshima Y.;
RT "Novel nuclear-encoded proteins interacting with a plastid sigma factor,
RT Sig1, in Arabidopsis thaliana.";
RL FEBS Lett. 514:300-304(2002).
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].
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, DISRUPTION PHENOTYPE, AND INDUCTION BY PSEUDOMONAS SYRINGAE.
RC STRAIN=cv. Columbia;
RX PubMed=20040062; DOI=10.1111/j.1365-3040.2009.02109.x;
RA Xie Y.-D., Li W., Guo D., Dong J., Zhang Q., Fu Y., Ren D., Peng M.,
RA Xia Y.;
RT "The Arabidopsis gene SIGMA FACTOR-BINDING PROTEIN 1 plays a role in the
RT salicylate- and jasmonate-mediated defence responses.";
RL Plant Cell Environ. 33:828-839(2010).
RN [6]
RP FUNCTION, INTERACTION WITH WRKY25 AND WRKY33, SUBCELLULAR LOCATION,
RP INDUCTION, MUTAGENESIS OF 62-VAL-GLN-63, AND DISRUPTION PHENOTYPE.
RX PubMed=21990940; DOI=10.1105/tpc.111.090571;
RA Lai Z., Li Y., Wang F., Cheng Y., Fan B., Yu J.Q., Chen Z.;
RT "Arabidopsis sigma factor binding proteins are activators of the WRKY33
RT transcription factor in plant defense.";
RL Plant Cell 23:3824-3841(2011).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=22535423; DOI=10.1104/pp.112.196816;
RA Cheng Y., Zhou Y., Yang Y., Chi Y.J., Zhou J., Chen J.Y., Wang F., Fan B.,
RA Shi K., Zhou Y.H., Yu J.Q., Chen Z.;
RT "Structural and functional analysis of VQ motif-containing proteins in
RT Arabidopsis as interacting proteins of WRKY transcription factors.";
RL Plant Physiol. 159:810-825(2012).
CC -!- FUNCTION: Contributes to plant defense. May regulate chloroplast
CC metabolism upon infection with pathogens such as Pseudomonas syringae
CC (PubMed:20040062). Functions as activator of WRKY33 in plant defense
CC against necrotrophic pathogens by stimulating the DNA-binding activity
CC of WRKY33 (PubMed:21990940). {ECO:0000269|PubMed:20040062,
CC ECO:0000269|PubMed:21990940}.
CC -!- SUBUNIT: Interacts with the sigma factor SIGA in chloroplast
CC (PubMed:11943170). Interacts with WRKY25 and WRKY33 in the nucleus
CC (PubMed:21990940). {ECO:0000269|PubMed:11943170,
CC ECO:0000269|PubMed:21990940}.
CC -!- INTERACTION:
CC Q9LDH1; O24629: SIGA; NbExp=3; IntAct=EBI-2118209, EBI-2118157;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:11943170}. Nucleus {ECO:0000269|PubMed:21990940}.
CC Note=Can localize to both chloroplast and nucleus. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves and roots, but not in flowers.
CC {ECO:0000269|PubMed:11943170}.
CC -!- INDUCTION: By light (PubMed:11943170). Accumulates in response to
CC infection with the bacterial pathogen Pseudomonas syringae
CC (PubMed:20040062). Induced by infection with the necrotrophic fungal
CC pathogen B.cinerea (PubMed:21990940). {ECO:0000269|PubMed:11943170,
CC ECO:0000269|PubMed:20040062, ECO:0000269|PubMed:21990940}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants show impaired induction of some defense-
CC related genes triggered by pathogen infection and treatments with
CC salicylic acid (SA) and jasmonic acid (JA) (PubMed:20040062). Increased
CC susceptibility to the necrotrophic fungal pathogen B.cinerea
CC (PubMed:21990940). {ECO:0000269|PubMed:20040062,
CC ECO:0000269|PubMed:21990940}.
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DR EMBL; AF224762; AAF34713.1; -; mRNA.
DR EMBL; AL390921; CAC00734.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79554.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63329.1; -; Genomic_DNA.
DR EMBL; AY042831; AAK68771.1; -; mRNA.
DR EMBL; BT002607; AAO00967.1; -; mRNA.
DR PIR; T51259; T51259.
DR RefSeq; NP_001325423.1; NM_001339806.1.
DR RefSeq; NP_191230.1; NM_115530.2.
DR AlphaFoldDB; Q9LDH1; -.
DR BioGRID; 10154; 2.
DR IntAct; Q9LDH1; 2.
DR STRING; 3702.AT3G56710.1; -.
DR PaxDb; Q9LDH1; -.
DR PRIDE; Q9LDH1; -.
DR ProteomicsDB; 234521; -.
DR EnsemblPlants; AT3G56710.1; AT3G56710.1; AT3G56710.
DR EnsemblPlants; AT3G56710.2; AT3G56710.2; AT3G56710.
DR GeneID; 824838; -.
DR Gramene; AT3G56710.1; AT3G56710.1; AT3G56710.
DR Gramene; AT3G56710.2; AT3G56710.2; AT3G56710.
DR KEGG; ath:AT3G56710; -.
DR Araport; AT3G56710; -.
DR TAIR; locus:2103580; AT3G56710.
DR eggNOG; ENOG502S9W6; Eukaryota.
DR HOGENOM; CLU_1733985_0_0_1; -.
DR InParanoid; Q9LDH1; -.
DR OMA; CEYFEPL; -.
DR OrthoDB; 1463611at2759; -.
DR PhylomeDB; Q9LDH1; -.
DR PRO; PR:Q9LDH1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LDH1; baseline and differential.
DR Genevisible; Q9LDH1; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0071482; P:cellular response to light stimulus; IEP:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR InterPro; IPR039335; SIB1/2.
DR InterPro; IPR008889; VQ.
DR PANTHER; PTHR33624; PTHR33624; 1.
DR Pfam; PF05678; VQ; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Nucleus; Plant defense; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..54
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 55..151
FT /note="Sigma factor binding protein 1, chloroplastic"
FT /id="PRO_0000418098"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 16..32
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000305|PubMed:21990940"
FT MOTIF 58..67
FT /note="VQ"
FT /evidence="ECO:0000305"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..37
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 62..63
FT /note="VQ->AA: Loss of interaction with WRKY33 protein."
FT /evidence="ECO:0000269|PubMed:21990940"
SQ SEQUENCE 151 AA; 16862 MW; A7217DEA0D94E02E CRC64;
MESSSSTFLT TTSLDKKKPS PVSRKSPKQK KKTTSTNKPI KVRYISNPMR VQTCASKFRE
LVQELTGQDA VDLQPEPIYS PSSDDHNLSP PAENLAPRVL HQEPFGERDS DCYEPLNAED
MFLPDQMSAG FSGFFSNGFY NVNDFGSIDS M
