SIB2_ARATH
ID SIB2_ARATH Reviewed; 141 AA.
AC O80669;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Sigma factor binding protein 2, chloroplastic;
DE Short=Sigma factor binding protein II;
DE AltName: Full=VQ motif-containing protein 16 {ECO:0000303|PubMed:22535423};
DE Short=AtVQ16 {ECO:0000303|PubMed:22535423};
DE Flags: Precursor;
GN Name=SIB2; Synonyms=VQ16 {ECO:0000303|PubMed:22535423};
GN OrderedLocusNames=At2g41180; ORFNames=T3K9.5;
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].
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 FUNCTION, INTERACTION WITH WRKY33, SUBCELLULAR LOCATION, INDUCTION, AND
RP 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 [5]
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: Functions as activator of WRKY33 in plant defense against
CC necrotrophic pathogens by stimulating the DNA-binding activity of
CC WRKY33. {ECO:0000269|PubMed:21990940}.
CC -!- SUBUNIT: Interacts with sigma factors in chloroplast (By similarity).
CC Interacts with WRKY33 in the nucleus (PubMed:21990940).
CC {ECO:0000250|UniProtKB:Q9LDH1, ECO:0000269|PubMed:21990940}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000250|UniProtKB:Q9LDH1}. Nucleus {ECO:0000269|PubMed:21990940}.
CC Note=Can localize to both chloroplast and nucleus. {ECO:0000305}.
CC -!- INDUCTION: By infection with the necrotrophic fungal pathogen
CC B.cinerea. {ECO:0000269|PubMed:21990940}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants have increased susceptibility to the
CC necrotrophic fungal pathogen B.cinerea. {ECO:0000269|PubMed:21990940}.
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DR EMBL; AC004261; AAD11994.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09941.1; -; Genomic_DNA.
DR EMBL; AY057686; AAL15317.1; -; mRNA.
DR EMBL; AY099785; AAM20636.1; -; mRNA.
DR EMBL; BT000291; AAN15610.1; -; mRNA.
DR PIR; T02101; T02101.
DR RefSeq; NP_030663.1; NM_129683.2.
DR AlphaFoldDB; O80669; -.
DR BioGRID; 4054; 1.
DR STRING; 3702.AT2G41180.1; -.
DR PaxDb; O80669; -.
DR PRIDE; O80669; -.
DR EnsemblPlants; AT2G41180.1; AT2G41180.1; AT2G41180.
DR GeneID; 818717; -.
DR Gramene; AT2G41180.1; AT2G41180.1; AT2G41180.
DR KEGG; ath:AT2G41180; -.
DR Araport; AT2G41180; -.
DR TAIR; locus:2063270; AT2G41180.
DR eggNOG; ENOG502SFCE; Eukaryota.
DR HOGENOM; CLU_1733985_0_0_1; -.
DR InParanoid; O80669; -.
DR OMA; RPCESEM; -.
DR OrthoDB; 1463611at2759; -.
DR PhylomeDB; O80669; -.
DR PRO; PR:O80669; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80669; differential.
DR Genevisible; O80669; AT.
DR GO; GO:0009507; C:chloroplast; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
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; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..38
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 39..141
FT /note="Sigma factor binding protein 2, chloroplastic"
FT /id="PRO_0000418099"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 13..29
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000305|PubMed:21990940"
FT MOTIF 55..64
FT /note="VQ"
FT /evidence="ECO:0000305"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 141 AA; 15570 MW; ABD7A3AD2C8FFE31 CRC64;
MDQSSSTLLI NQRKSSSSPT RIPPKQKRKS TTTHKPIKVR YISNPMRVET CPSKFRELVQ
ELTGQDAADL PPSPTTFTAV DLHRPCESEM NLEPLDGEVR GEYYSPLDEE VFNAPQMSAG
LSGFFSSGFY NVNALGSIGS L
