SWC6_ARATH
ID SWC6_ARATH Reviewed; 171 AA.
AC Q9FHW2;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=SWR1 complex subunit 6;
DE AltName: Full=Protein SERRATED LEAVES AND EARLY FLOWERING;
GN Name=SWC6; Synonyms=SEF; OrderedLocusNames=At5g37055;
GN ORFNames=MJG14.20, MJG14.4;
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=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, INTERACTION WITH ARP6 AND SWC2, SUBUNIT, DISRUPTION PHENOTYPE,
RP TISSUE SPECIFICITY, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17470967; DOI=10.1242/dev.001891;
RA Choi K., Park C., Lee J., Oh M., Noh B., Lee I.;
RT "Arabidopsis homologs of components of the SWR1 complex regulate flowering
RT and plant development.";
RL Development 134:1931-1941(2007).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INTERACTION WITH
RP ARP6 AND PIE1.
RX PubMed=17142478; DOI=10.1104/pp.106.092270;
RA March-Diaz R., Garcia-Dominguez M., Florencio F.J., Reyes J.C.;
RT "SEF, a new protein required for flowering repression in Arabidopsis,
RT interacts with PIE1 and ARP6.";
RL Plant Physiol. 143:893-901(2007).
RN [7]
RP FUNCTION, AND INTERACTION WITH FLX; SUF4; ASHH2 AND TAF14.
RX PubMed=21282526; DOI=10.1105/tpc.110.075911;
RA Choi K., Kim J., Hwang H.J., Kim S., Park C., Kim S.Y., Lee I.;
RT "The FRIGIDA complex activates transcription of FLC, a strong flowering
RT repressor in Arabidopsis, by recruiting chromatin modification factors.";
RL Plant Cell 23:289-303(2011).
CC -!- FUNCTION: Component of the SWR1 complex which mediates the ATP-
CC dependent exchange of histone H2A for the H2A variant H2A.F/Z leading
CC to transcriptional regulation of selected genes (e.g. FLC) by chromatin
CC remodeling. Coodinates SWR1-C, FRI-C (FLC transcription activator
CC complex), histone methyltransferase and general transcription factors.
CC Represses flowering by positively regulating FLC and MAF4. Binds to the
CC promoter region of FLC chromatin. {ECO:0000269|PubMed:17142478,
CC ECO:0000269|PubMed:17470967, ECO:0000269|PubMed:21282526}.
CC -!- SUBUNIT: Homodimer. Component of the SWR1 chromatin-remodeling complex
CC composed of at least ARP6/ESD1/SUF3, PIE1, SWC6, SWC2 and H2AZs (HTA8,
CC HTA9, HTA11). Interacts directly with ARP6, PIE1 and SWC2. Interacts
CC with FLX and SUF4, two component of the transcription activator complex
CC FRI-C, and with ASHH2 and TAF14. {ECO:0000269|PubMed:17142478,
CC ECO:0000269|PubMed:17470967, ECO:0000269|PubMed:21282526}.
CC -!- INTERACTION:
CC Q9FHW2; Q8LGE3: ARP6; NbExp=6; IntAct=EBI-1537353, EBI-1537316;
CC Q9FHW2; O23160: MYB73; NbExp=3; IntAct=EBI-1537353, EBI-25506855;
CC Q9FHW2; Q7X9V2: PIE1; NbExp=4; IntAct=EBI-1537353, EBI-1537462;
CC Q9FHW2; F4IP06: SWC2; NbExp=3; IntAct=EBI-1537353, EBI-1537394;
CC Q9FHW2; Q9FHW2: SWC6; NbExp=2; IntAct=EBI-1537353, EBI-1537353;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:17470967}.
CC Nucleus {ECO:0000269|PubMed:17470967}. Note=Relocates to the nuclear
CC periphery when interacting with ARP6.
CC -!- TISSUE SPECIFICITY: Expressed in root, lateral root primordia, shoot
CC apex, leaves, stems, inflorescences, flowers, axillary buds, developing
CC siliques and premature seeds. {ECO:0000269|PubMed:17142478,
CC ECO:0000269|PubMed:17470967}.
CC -!- INDUCTION: Not regulated by circadian rhythm, photoperiod or
CC vernalization. {ECO:0000269|PubMed:17470967}.
CC -!- DISRUPTION PHENOTYPE: Early flowering, leaf serration, production of
CC extra petals and weak apical dominance. {ECO:0000269|PubMed:17142478,
CC ECO:0000269|PubMed:17470967}.
CC -!- SIMILARITY: Belongs to the ZNHIT1 family. {ECO:0000305}.
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DR EMBL; AB017068; BAB11357.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94142.1; -; Genomic_DNA.
DR EMBL; AF378857; AAK55660.1; -; mRNA.
DR EMBL; AY050464; AAK91477.1; -; mRNA.
DR EMBL; AK175306; BAD43069.1; -; mRNA.
DR RefSeq; NP_568545.1; NM_123064.3.
DR AlphaFoldDB; Q9FHW2; -.
DR BioGRID; 18927; 8.
DR IntAct; Q9FHW2; 5.
DR STRING; 3702.AT5G37055.1; -.
DR SwissPalm; Q9FHW2; -.
DR PaxDb; Q9FHW2; -.
DR PRIDE; Q9FHW2; -.
DR ProteomicsDB; 226572; -.
DR EnsemblPlants; AT5G37055.1; AT5G37055.1; AT5G37055.
DR GeneID; 833676; -.
DR Gramene; AT5G37055.1; AT5G37055.1; AT5G37055.
DR KEGG; ath:AT5G37055; -.
DR Araport; AT5G37055; -.
DR TAIR; locus:505006661; AT5G37055.
DR eggNOG; KOG3362; Eukaryota.
DR HOGENOM; CLU_106918_0_0_1; -.
DR InParanoid; Q9FHW2; -.
DR OMA; PCGARYC; -.
DR OrthoDB; 1588778at2759; -.
DR PhylomeDB; Q9FHW2; -.
DR PRO; PR:Q9FHW2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FHW2; baseline and differential.
DR Genevisible; Q9FHW2; AT.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0000812; C:Swr1 complex; IDA:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IGI:TAIR.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0043486; P:histone exchange; IBA:GO_Central.
DR GO; GO:0048638; P:regulation of developmental growth; IMP:TAIR.
DR GO; GO:0009909; P:regulation of flower development; IMP:TAIR.
DR InterPro; IPR039723; Vps71/ZNHIT1.
DR InterPro; IPR007529; Znf_HIT.
DR PANTHER; PTHR13093; PTHR13093; 1.
DR Pfam; PF04438; zf-HIT; 1.
DR PROSITE; PS51083; ZF_HIT; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Differentiation; Flowering; Metal-binding; Nucleus;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..171
FT /note="SWR1 complex subunit 6"
FT /id="PRO_0000423728"
FT ZN_FING 134..166
FT /note="HIT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT REGION 63..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
SQ SEQUENCE 171 AA; 19137 MW; 250F42A946949E41 CRC64;
MEEEMSNRRV SNRTRKVATK MAAALTSNDN RTQAAIARLE ALENDNGAIE VIDLNDDEEA
SLDEDDDLGY LQKKQHKGSK RKTRQAKALE ARKAPKSFLE LLQEANLESL PSHVPTYLKA
AVGPPSSSSR RYFCSVCGYI AGYNCCLCGM RFCSIRCQNI HKDTRCQKFV A
