SGS3_ARATH
ID SGS3_ARATH Reviewed; 625 AA.
AC Q9LDX1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Protein SUPPRESSOR OF GENE SILENCING 3 {ECO:0000303|PubMed:10850495};
DE Short=AtSGS3 {ECO:0000303|PubMed:10850495};
GN Name=SGS3 {ECO:0000303|PubMed:10850495};
GN OrderedLocusNames=At5g23570 {ECO:0000312|Araport:AT5G23570};
GN ORFNames=MQM1.17 {ECO:0000312|EMBL:BAA97244.1};
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 [GENOMIC DNA], AND MUTAGENESIS OF GLU-500.
RX PubMed=10850495; DOI=10.1016/s0092-8674(00)80863-6;
RA Mourrain P., Beclin C., Elmayan T., Feuerbach F., Godon C., Morel J.-B.,
RA Jouette D., Lacombe A.-M., Nikic S., Picault N., Remoue K., Sanial M.,
RA Vo T.-A., Vaucheret H.;
RT "Arabidopsis SGS2 and SGS3 genes are required for posttranscriptional gene
RT silencing and natural virus resistance.";
RL Cell 101:533-542(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 GENE FAMILY.
RX PubMed=12162795; DOI=10.1186/1471-2105-3-21;
RA Bateman A.;
RT "The SGS3 protein involved in PTGS finds a family.";
RL BMC Bioinformatics 3:21-21(2002).
RN [6]
RP FUNCTION.
RX PubMed=15466488; DOI=10.1101/gad.1231804;
RA Peragine A., Yoshikawa M., Wu G., Albrecht H.L., Poethig R.S.;
RT "SGS3 and SGS2/SDE1/RDR6 are required for juvenile development and the
RT production of trans-acting siRNAs in Arabidopsis.";
RL Genes Dev. 18:2368-2379(2004).
RN [7]
RP FUNCTION.
RX PubMed=15165191; DOI=10.1111/j.1365-313x.2004.02103.x;
RA Muangsan N., Beclin C., Vaucheret H., Robertson D.;
RT "Geminivirus VIGS of endogenous genes requires SGS2/SDE1 and SGS3 and
RT defines a new branch in the genetic pathway for silencing in plants.";
RL Plant J. 38:1004-1014(2004).
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TOMATO YELLOW LEAF CURL VIRUS
RP PROTEIN V2.
RX PubMed=18165314; DOI=10.1073/pnas.0709036105;
RA Glick E., Zrachya A., Levy Y., Mett A., Gidoni D., Belausov E.,
RA Citovsky V., Gafni Y.;
RT "Interaction with host SGS3 is required for suppression of RNA silencing by
RT tomato yellow leaf curl virus V2 protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:157-161(2008).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, REPRESSION BY HEAT, SUBCELLULAR LOCATION,
RP AND INTERACTION WITH SGIP1.
RC STRAIN=cv. Columbia;
RX PubMed=30778176; DOI=10.1038/s41422-019-0145-8;
RA Liu J., Feng L., Gu X., Deng X., Qiu Q., Li Q., Zhang Y., Wang M., Deng Y.,
RA Wang E., He Y., Baeurle I., Li J., Cao X., He Z.;
RT "An H3K27me3 demethylase-HSFA2 regulatory loop orchestrates
RT transgenerational thermomemory in Arabidopsis.";
RL Cell Res. 29:379-390(2019).
CC -!- FUNCTION: Required for post-transcriptional gene silencing and natural
CC virus resistance. May bind nucleic acids and is essential for the
CC biogenesis of trans-acting siRNAs but is not required for silencing
CC induced by IR-PTGS. Involved in the juvenile-to-adult transition
CC regulation. In case of begomoviruses infection, it is targeted by the
CC viral protein V2 leading to suppression of post-transcriptional gene
CC silencing. Involved in the mechanisms necessary for quick response to
CC heat and subsequent heritable transgenerational memory of heat
CC acclimation (global warming) such as early flowering and attenuated
CC immunity; this process includes epigenetic regulation as well as post-
CC transcriptional gene silencing (PTGS) (PubMed:30778176). In response to
CC heat, HSFA2 is activated and promotes the expression of REF6 which in
CC turn derepresses HSFA2, thus establishing an heritable feedback loop
CC able to trigger SGIP1 and subsequent SGIP1-mediated SGS3 degradation;
CC this prevents the biosynthesis of trans-acting siRNA (tasiRNA) and
CC leads to the release of HTT5, which drives early flowering but
CC attenuates immunity (PubMed:30778176). {ECO:0000269|PubMed:15165191,
CC ECO:0000269|PubMed:15466488, ECO:0000269|PubMed:30778176}.
CC -!- SUBUNIT: Interacts with begomoviruses protein V2 (PubMed:18165314).
CC Interacts with SGIP1 in cytoplasmic granules (PubMed:30778176).
CC {ECO:0000269|PubMed:18165314, ECO:0000269|PubMed:30778176}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:18165314}. Cytoplasmic granule
CC {ECO:0000269|PubMed:30778176}. Note=Accumulates in inclusion bodies in
CC the cell periphery (PubMed:18165314). May interact with the ER network
CC from the perinuclear region out to the cell periphery (By similarity).
CC Co-localizes with SGIP1 in cytoplasmic granules (PubMed:30778176).
CC {ECO:0000250, ECO:0000269|PubMed:18165314,
CC ECO:0000269|PubMed:30778176}.
CC -!- INDUCTION: Fades out in response to heat through an enhanced protein
CC degradation (at protein level) triggered by the E3 ligase SGIP1-
CC mediated ubiquitination. {ECO:0000269|PubMed:30778176}.
CC -!- DISRUPTION PHENOTYPE: Early flowering and bolting at room temperature
CC (22 degrees Celsius), lost sensitivity to heat and accumulation of FT,
CC associated with reduced levels of TAS1-siRNAs (PubMed:30778176).
CC Attenuated immunity leading to an increased susceptibility to the
CC pathogenic bacteria Pst DC3000 (avrRpt2), with slightly reduced
CC induction of ICS1 and salicylic acid (SA) levels upon pathogen
CC infection (PubMed:30778176). {ECO:0000269|PubMed:30778176}.
CC -!- SIMILARITY: Belongs to the SGS3 family. {ECO:0000305}.
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DR EMBL; AF239719; AAF73960.1; -; Genomic_DNA.
DR EMBL; AB025633; BAA97244.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93184.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69842.1; -; Genomic_DNA.
DR EMBL; BT002944; AAO22757.1; -; mRNA.
DR EMBL; BT004380; AAO42374.1; -; mRNA.
DR RefSeq; NP_001331491.1; NM_001343817.1.
DR RefSeq; NP_197747.1; NM_122263.3.
DR AlphaFoldDB; Q9LDX1; -.
DR SMR; Q9LDX1; -.
DR BioGRID; 17697; 1.
DR DIP; DIP-29658N; -.
DR IntAct; Q9LDX1; 2.
DR MINT; Q9LDX1; -.
DR STRING; 3702.AT5G23570.1; -.
DR PaxDb; Q9LDX1; -.
DR PRIDE; Q9LDX1; -.
DR ProteomicsDB; 232652; -.
DR EnsemblPlants; AT5G23570.1; AT5G23570.1; AT5G23570.
DR EnsemblPlants; AT5G23570.3; AT5G23570.3; AT5G23570.
DR GeneID; 832422; -.
DR Gramene; AT5G23570.1; AT5G23570.1; AT5G23570.
DR Gramene; AT5G23570.3; AT5G23570.3; AT5G23570.
DR KEGG; ath:AT5G23570; -.
DR Araport; AT5G23570; -.
DR TAIR; locus:2171716; AT5G23570.
DR eggNOG; ENOG502QPU5; Eukaryota.
DR HOGENOM; CLU_020338_1_0_1; -.
DR InParanoid; Q9LDX1; -.
DR OMA; DFERMQQ; -.
DR OrthoDB; 370807at2759; -.
DR PhylomeDB; Q9LDX1; -.
DR PRO; PR:Q9LDX1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LDX1; baseline and differential.
DR Genevisible; Q9LDX1; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IMP:TAIR.
DR GO; GO:0010286; P:heat acclimation; IMP:UniProtKB.
DR GO; GO:0050688; P:regulation of defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:2000028; P:regulation of photoperiodism, flowering; IMP:UniProtKB.
DR GO; GO:0070921; P:regulation of siRNA production; IMP:UniProtKB.
DR GO; GO:0009408; P:response to heat; IMP:UniProtKB.
DR GO; GO:0009616; P:RNAi-mediated antiviral immune response; IMP:TAIR.
DR GO; GO:0030422; P:siRNA processing; IEP:TAIR.
DR GO; GO:0010267; P:ta-siRNA processing; IMP:TAIR.
DR GO; GO:0010050; P:vegetative phase change; IMP:TAIR.
DR GO; GO:0010025; P:wax biosynthetic process; IGI:TAIR.
DR CDD; cd12266; RRM_like_XS; 1.
DR Gene3D; 3.30.70.2890; -; 1.
DR InterPro; IPR044287; SGS3.
DR InterPro; IPR005380; XS_domain.
DR InterPro; IPR038588; XS_domain_sf.
DR InterPro; IPR005381; Znf-XS_domain.
DR PANTHER; PTHR46602; PTHR46602; 1.
DR Pfam; PF03468; XS; 1.
DR Pfam; PF03470; zf-XS; 1.
PE 1: Evidence at protein level;
KW Antiviral protein; Coiled coil; Cytoplasm; Host-virus interaction;
KW Plant defense; Reference proteome; RNA-mediated gene silencing;
KW Stress response.
FT CHAIN 1..625
FT /note="Protein SUPPRESSOR OF GENE SILENCING 3"
FT /id="PRO_0000333289"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 30..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 452..533
FT /evidence="ECO:0000255"
FT COILED 564..615
FT /evidence="ECO:0000255"
FT COMPBIAS 51..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..185
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 500
FT /note="E->K: In sgs3-3; complete suppression of post-
FT transcriptional gene silencing."
FT /evidence="ECO:0000269|PubMed:10850495"
SQ SEQUENCE 625 AA; 71972 MW; 456E2A1396706A96 CRC64;
MSSRAGPMSK EKNVQGGYRP EVEQLVQGLA GTRLASSQDD GGEWEVISKK NKNKPGNTSG
KTWVSQNSNP PRAWGGQQQG RGSNVSGRGN NVSGRGNGNG RGIQANISGR GRALSRKYDN
NFVAPPPVSR PPLEGGWNWQ ARGGSAQHTA VQEFPDVEDD VDNASEEEND SDALDDSDDD
LASDDYDSDV SQKSHGSRKQ NKWFKKFFGS LDSLSIEQIN EPQRQWHCPA CQNGPGAIDW
YNLHPLLAHA RTKGARRVKL HRELAEVLEK DLQMRGASVI PCGEIYGQWK GLGEDEKDYE
IVWPPMVIIM NTRLDKDDND KWLGMGNQEL LEYFDKYEAL RARHSYGPQG HRGMSVLMFE
SSATGYLEAE RLHRELAEMG LDRIAWGQKR SMFSGGVRQL YGFLATKQDL DIFNQHSQGK
TRLKFELKSY QEMVVKELRQ ISEDNQQLNY FKNKLSKQNK HAKVLEESLE IMSEKLRRTA
EDNRIVRQRT KMQHEQNREE MDAHDRFFMD SIKQIHERRD AKEENFEMLQ QQERAKVVGQ
QQQNINPSSN DDCRKRAEEV SSFIEFQEKE MEEFVEEREM LIKDQEKKME DMKKRHHEEI
FDLEKEFDEA LEQLMYKHGL HNEDD
