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   24-JAN-2024, entry version 118.
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.Q9LDX1; -.
DR   iPTMnet; Q9LDX1; -.
DR   PaxDb; 3702-AT5G23570-1; -.
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; AT5G23570; SGS3.
DR   eggNOG; ENOG502QPU5; Eukaryota.
DR   HOGENOM; CLU_020338_1_0_1; -.
DR   InParanoid; Q9LDX1; -.
DR   OMA; RSYHEMV; -.
DR   OrthoDB; 1222097at2759; -.
DR   PhylomeDB; Q9LDX1; -.
DR   PRO; PR:Q9LDX1; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LDX1; baseline and differential.
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 processing; 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; XS domain; 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; PROTEIN SUPPRESSOR OF GENE SILENCING 3; 1.
DR   PANTHER; PTHR46602:SF1; PROTEIN SUPPRESSOR OF GENE SILENCING 3; 1.
DR   Pfam; PF03468; XS; 1.
DR   Pfam; PF03470; zf-XS; 1.
DR   Genevisible; Q9LDX1; AT.
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
FT                   post-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
//