SGIP1_ARATH
ID SGIP1_ARATH Reviewed; 313 AA.
AC Q9SD71;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=E3 ubiquitin-protein ligase SGIP1 {ECO:0000305|PubMed:11130713};
DE EC=2.3.2.27 {ECO:0000269|PubMed:30778176};
DE AltName: Full=SGS3-INTERACTING PROTEIN 1 {ECO:0000303|PubMed:30778176};
GN Name=SGIP1 {ECO:0000303|PubMed:30778176};
GN OrderedLocusNames=At3g47020 {ECO:0000312|Araport:AT3G47020};
GN ORFNames=F13I12.70 {ECO:0000312|EMBL:CAB61948.1};
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 [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 [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 FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR
RP LOCATION, INTERACTION WITH SGS3, AND INDUCTION BY HEAT.
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: E3 ubiquitin-protein ligase which triggers the ubiquitination
CC and subsequent degradation of SGS3 in response to heat
CC (PubMed:30778176). Involved in the mechanisms necessary for quick
CC response to heat and subsequent heritable transgenerational memory of
CC heat acclimation (global warming) such as early flowering and
CC attenuated immunity; this process includes epigenetic regulation as
CC well as post-transcriptional gene silencing (PTGS) (PubMed:30778176).
CC In response to heat, HSFA2 is activated and promotes the expression of
CC REF6 which in turn derepresses HSFA2, thus establishing an heritable
CC feedback loop able to trigger SGIP1 and subsequent SGIP1-mediated SGS3
CC degradation; this prevents the biosynthesis of trans-acting siRNA
CC (tasiRNA) and leads to the release of HTT5, which drives early
CC flowering but attenuates immunity (PubMed:30778176).
CC {ECO:0000269|PubMed:30778176}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:30778176};
CC -!- PATHWAY: Protein degradation; proteasomal ubiquitin-dependent pathway.
CC {ECO:0000269|PubMed:30778176}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:30778176}.
CC -!- SUBUNIT: Interacts with SGS3 in cytoplasmic granules.
CC {ECO:0000269|PubMed:30778176}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule
CC {ECO:0000269|PubMed:30778176}. Note=Co-localizes with SGS3 in
CC cytoplasmic granules. {ECO:0000269|PubMed:30778176}.
CC -!- INDUCTION: Up-regulated in heat-stressed plants and unstressed progeny
CC in a HSFA2-dependent manner. {ECO:0000269|PubMed:30778176}.
CC -!- DISRUPTION PHENOTYPE: Impaired heat-induced decrease of SGS3 levels and
CC delayed SGS3 degradation associated with abolished heat-dependent early
CC flowering and trans-acting siRNA (tasiRNA siR255 and siR1511)
CC accumulation (PubMed:30778176). Lost heritable transgenerational
CC thermomemory (PubMed:30778176). {ECO:0000269|PubMed:30778176}.
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DR EMBL; AL133292; CAB61948.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78233.1; -; Genomic_DNA.
DR PIR; T45638; T45638.
DR RefSeq; NP_190286.1; NM_114569.1.
DR AlphaFoldDB; Q9SD71; -.
DR PaxDb; Q9SD71; -.
DR PRIDE; Q9SD71; -.
DR ProteomicsDB; 230858; -.
DR EnsemblPlants; AT3G47020.1; AT3G47020.1; AT3G47020.
DR GeneID; 823855; -.
DR Gramene; AT3G47020.1; AT3G47020.1; AT3G47020.
DR KEGG; ath:AT3G47020; -.
DR Araport; AT3G47020; -.
DR TAIR; locus:2075651; AT3G47020.
DR HOGENOM; CLU_027176_8_3_1; -.
DR InParanoid; Q9SD71; -.
DR OMA; RIYTFID; -.
DR OrthoDB; 731539at2759; -.
DR PhylomeDB; Q9SD71; -.
DR UniPathway; UPA00143; -.
DR UniPathway; UPA00144; -.
DR PRO; PR:Q9SD71; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SD71; baseline.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:TAIR.
DR GO; GO:0010286; P:heat acclimation; IMP:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
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 InterPro; IPR013187; F-box-assoc_dom_typ3.
DR InterPro; IPR017451; F-box-assoc_interact_dom.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR Pfam; PF00646; F-box; 1.
DR Pfam; PF08268; FBA_3; 1.
DR SMART; SM00256; FBOX; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR TIGRFAMs; TIGR01640; F_box_assoc_1; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Stress response; Transferase; Ubl conjugation pathway.
FT CHAIN 1..313
FT /note="E3 ubiquitin-protein ligase SGIP1"
FT /id="PRO_0000283464"
FT DOMAIN 16..65
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
SQ SEQUENCE 313 AA; 35859 MW; A088B243FC801183 CRC64;
MEKSQKQVTR PSNSRREYSK EIPIDLLIEI FSRLSTGDIA RCRCVSKIWS SVPRLRDFTE
LFLKISSARP RILFTFLHNG MVPSYDNEIH APVRGFLCSK ASVYNPSTGE CAYPYLELLG
LWDILPVDAE NLAKKVCVPK VLLASEDFAC RVSTLGTEEV CWRMIQCSLP HRPFRDEICI
DGVLYYLANC KGKLGILWPV PSGDQSHEVT RSFVLRILED ANKLIWSRTV YTLSFNWKKL
VNKSLYIVGM TSGGEIVLST RHLNYPFYIV YYNPVNNTAA KNEIQFGNIA NKKAENSRIY
TFIDHVENVE HMD
