SGT1B_ARATH
ID SGT1B_ARATH Reviewed; 358 AA.
AC Q9SUT5;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 162.
DE RecName: Full=Protein SGT1 homolog B {ECO:0000250|UniProtKB:Q08446};
DE Short=AtSGT1b;
DE AltName: Full=Protein ENHANCED DOWNY MILDEW 1;
DE AltName: Full=Protein ENHANCER OF TIR1-1 AUXIN RESISTANCE 3;
DE AltName: Full=Suppressor of G2 allele of SKP1 homolog B {ECO:0000250|UniProtKB:Q08446};
GN Name=SGT1B; Synonyms=EDM1, ETA3, RPR1; OrderedLocusNames=At4g11260;
GN ORFNames=F8L21.50;
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 [MRNA], AND INTERACTION WITH RAR1.
RX PubMed=11847307; DOI=10.1126/science.1067554;
RA Azevedo C., Sadanandom A., Kitagawa K., Freialdenhoven A., Shirasu K.,
RA Schulze-Lefert P.;
RT "The RAR1 interactor SGT1, an essential component of R gene-triggered
RT disease resistance.";
RL Science 295:2073-2076(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=14504394; DOI=10.1073/pnas.2035132100;
RA Pawlowski J., Holzmann M., Berney C., Fahrni J., Gooday A.J., Cedhagen T.,
RA Habura A., Bowser S.S.;
RT "The evolution of early Foraminifera.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11494-11498(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12034892; DOI=10.1105/tpc.001123;
RA Toer M., Gordon P., Cuzick A., Eulgem T., Sinapidou E., Mert-Tuerk F.,
RA Can C., Dangl J.L., Holub E.B.;
RT "Arabidopsis SGT1b is required for defense signaling conferred by several
RT downy mildew resistance genes.";
RL Plant Cell 14:993-1003(2002).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=11847308; DOI=10.1126/science.1067747;
RA Austin M.J., Muskett P., Kahn K., Feys B.J., Jones J.D., Parker J.E.;
RT "Regulatory role of SGT1 in early R gene-mediated plant defenses.";
RL Science 295:2077-2080(2002).
RN [9]
RP INTERACTION WITH HSP90-2.
RX PubMed=14592967; DOI=10.1093/emboj/cdg547;
RA Hubert D.A., Tornero P., Belkhadir Y., Krishna P., Takahashi A.,
RA Shirasu K., Dangl J.L.;
RT "Cytosolic HSP90 associates with and modulates the Arabidopsis RPM1 disease
RT resistance protein.";
RL EMBO J. 22:5679-5689(2003).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12782725; DOI=10.1105/tpc.010884;
RA Gray W.M., Muskett P.R., Chuang H.W., Parker J.E.;
RT "Arabidopsis SGT1b is required for SCF(TIR1)-mediated auxin response.";
RL Plant Cell 15:1310-1319(2003).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15976272; DOI=10.1126/science.1109977;
RA Holt B.F. III, Belkhadir Y., Dangl J.L.;
RT "Antagonistic control of disease resistance protein stability in the plant
RT immune system.";
RL Science 309:929-932(2005).
RN [12]
RP FUNCTION, AND INDUCTION.
RX PubMed=16619029; DOI=10.1038/sj.emboj.7601084;
RA Azevedo C., Betsuyaku S., Peart J., Takahashi A., Noel L., Sadanandom A.,
RA Casais C., Parker J., Shirasu K.;
RT "Role of SGT1 in resistance protein accumulation in plant immunity.";
RL EMBO J. 25:2007-2016(2006).
RN [13]
RP INTERACTION WITH RAR1.
RX PubMed=17148606; DOI=10.1073/pnas.0607279103;
RA Shang Y., Li X., Cui H., He P., Thilmony R., Chintamanani S.,
RA Zwiesler-Vollick J., Gopalan S., Tang X., Zhou J.M.;
RT "RAR1, a central player in plant immunity, is targeted by Pseudomonas
RT syringae effector AvrB.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:19200-19205(2006).
RN [14]
RP FUNCTION, INTERACTION WITH HSC70-1 AND HSC70-3, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=18065690; DOI=10.1105/tpc.107.051896;
RA Noel L.D., Cagna G., Stuttmann J., Wirthmueller L., Betsuyaku S.,
RA Witte C.P., Bhat R., Pochon N., Colby T., Parker J.E.;
RT "Interaction between SGT1 and cytosolic/nuclear HSC70 chaperones regulates
RT Arabidopsis immune responses.";
RL Plant Cell 19:4061-4076(2007).
RN [15]
RP FUNCTION.
RX PubMed=19304739; DOI=10.1093/pcp/pcp044;
RA Kawamura Y., Takenaka S., Hase S., Kubota M., Ichinose Y., Kanayama Y.,
RA Nakaho K., Klessig D.F., Takahashi H.;
RT "Enhanced defense responses in Arabidopsis induced by the cell wall protein
RT fractions from Pythium oligandrum require SGT1, RAR1, NPR1 and JAR1.";
RL Plant Cell Physiol. 50:924-934(2009).
RN [16]
RP INTERACTION WITH HSP90-2.
RX PubMed=19487680; DOI=10.1073/pnas.0904877106;
RA Hubert D.A., He Y., McNulty B.C., Tornero P., Dangl J.L.;
RT "Specific Arabidopsis HSP90.2 alleles recapitulate RAR1 cochaperone
RT function in plant NB-LRR disease resistance protein regulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:9556-9563(2009).
RN [17]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20854394; DOI=10.1111/j.1469-8137.2010.03470.x;
RA Uppalapati S.R., Ishiga Y., Ryu C.M., Ishiga T., Wang K., Noel L.D.,
RA Parker J.E., Mysore K.S.;
RT "SGT1 contributes to coronatine signaling and Pseudomonas syringae pv.
RT tomato disease symptom development in tomato and Arabidopsis.";
RL New Phytol. 189:83-93(2011).
CC -!- FUNCTION: Involved in plant innate immunity. Is essential for
CC resistance conferred by multiple R genes recognizing different oomycete
CC pathogen isolates like avirulent H.parasitica (downy mildew).
CC Contributes additively with RAR1 to RPP5-dependent resistance. Not
CC required for RPM1, RPS2, RPS4 and RPS5-mediated resistance. Functions
CC as negative regulator of RPS5 accumulation by assisting its
CC degradation. May be involved in heat shock response by associating with
CC HSC70-1 chaperone. Required for the SCF(TIR1)-mediated degradation of
CC Aux/IAA proteins, but maybe not for SCF(TIR1) assembly or binding to
CC its Aux/IAA substrates. Probably required for SCF-mediated
CC ubiquitination, by coupling HSP90 to SCF complex for ubiquitination of
CC HSP90 client proteins. Required for the coronatine/jasmonic acid-
CC mediated signal transduction pathway. {ECO:0000269|PubMed:11847308,
CC ECO:0000269|PubMed:12034892, ECO:0000269|PubMed:12782725,
CC ECO:0000269|PubMed:15976272, ECO:0000269|PubMed:16619029,
CC ECO:0000269|PubMed:18065690, ECO:0000269|PubMed:19304739,
CC ECO:0000269|PubMed:20854394}.
CC -!- SUBUNIT: Interacts with RAR1 and HSP90-2. Interacts (via SGS domain)
CC with HSC70-1 and HSC70-3. {ECO:0000269|PubMed:11847307,
CC ECO:0000269|PubMed:14592967, ECO:0000269|PubMed:17148606,
CC ECO:0000269|PubMed:18065690, ECO:0000269|PubMed:19487680}.
CC -!- INTERACTION:
CC Q9SUT5; P22953: HSP70-1; NbExp=3; IntAct=EBI-1581364, EBI-1238845;
CC Q9SUT5; Q9SE33: RAR1; NbExp=3; IntAct=EBI-1581364, EBI-1781969;
CC Q9SUT5; A0A0H3NF38: sspH2; Xeno; NbExp=2; IntAct=EBI-1581364, EBI-10689860;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18065690}. Nucleus
CC {ECO:0000269|PubMed:18065690}.
CC -!- INDUCTION: By infection with the oomycete H.parasitica (downy mildew).
CC {ECO:0000269|PubMed:16619029}.
CC -!- DISRUPTION PHENOTYPE: Delay in flowering time. Plants loose R gene
CC resistance mediated by RPP2, RPP4, RPP5 and RPP7, and show reduced
CC response to auxin, jasmonate and coronatine, and enhanced tolerance to
CC heat shock. {ECO:0000269|PubMed:11847308, ECO:0000269|PubMed:12034892,
CC ECO:0000269|PubMed:12782725, ECO:0000269|PubMed:15976272,
CC ECO:0000269|PubMed:18065690, ECO:0000269|PubMed:20854394}.
CC -!- SIMILARITY: Belongs to the SGT1 family. {ECO:0000305}.
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DR EMBL; AF439976; AAL33612.1; -; mRNA.
DR EMBL; AJ318019; CAC85266.1; -; mRNA.
DR EMBL; AL096882; CAB51410.1; -; Genomic_DNA.
DR EMBL; AL161531; CAB81227.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82990.1; -; Genomic_DNA.
DR EMBL; AF370229; AAK44044.1; -; mRNA.
DR EMBL; AF428340; AAL16270.1; -; mRNA.
DR EMBL; AY150487; AAN12904.1; -; mRNA.
DR EMBL; AY085464; AAM62690.1; -; mRNA.
DR PIR; T13017; T13017.
DR RefSeq; NP_192865.1; NM_117197.4.
DR AlphaFoldDB; Q9SUT5; -.
DR SMR; Q9SUT5; -.
DR BioGRID; 12027; 11.
DR DIP; DIP-41227N; -.
DR IntAct; Q9SUT5; 10.
DR MINT; Q9SUT5; -.
DR STRING; 3702.AT4G11260.1; -.
DR iPTMnet; Q9SUT5; -.
DR MetOSite; Q9SUT5; -.
DR PaxDb; Q9SUT5; -.
DR PRIDE; Q9SUT5; -.
DR ProteomicsDB; 234576; -.
DR DNASU; 826728; -.
DR EnsemblPlants; AT4G11260.1; AT4G11260.1; AT4G11260.
DR GeneID; 826728; -.
DR Gramene; AT4G11260.1; AT4G11260.1; AT4G11260.
DR KEGG; ath:AT4G11260; -.
DR Araport; AT4G11260; -.
DR TAIR; locus:2128278; AT4G11260.
DR eggNOG; KOG0376; Eukaryota.
DR eggNOG; KOG1309; Eukaryota.
DR HOGENOM; CLU_039532_1_0_1; -.
DR InParanoid; Q9SUT5; -.
DR OMA; WDKLVGD; -.
DR OrthoDB; 1426397at2759; -.
DR PhylomeDB; Q9SUT5; -.
DR PRO; PR:Q9SUT5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SUT5; baseline and differential.
DR Genevisible; Q9SUT5; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; TAS:TAIR.
DR GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IGI:TAIR.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0010187; P:negative regulation of seed germination; IMP:TAIR.
DR GO; GO:0030163; P:protein catabolic process; IMP:TAIR.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR GO; GO:1900150; P:regulation of defense response to fungus; IMP:UniProtKB.
DR GO; GO:0009408; P:response to heat; IMP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:TAIR.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR007699; SGS_dom.
DR InterPro; IPR044563; Sgt1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR45862; PTHR45862; 1.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF05002; SGS; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS51203; CS; 1.
DR PROSITE; PS51048; SGS; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Immunity; Innate immunity; Nucleus; Plant defense;
KW Reference proteome; Repeat; TPR repeat; Ubl conjugation pathway.
FT CHAIN 1..358
FT /note="Protein SGT1 homolog B"
FT /id="PRO_0000403648"
FT REPEAT 2..35
FT /note="TPR 1"
FT REPEAT 37..69
FT /note="TPR 2"
FT REPEAT 70..103
FT /note="TPR 3"
FT DOMAIN 157..246
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT DOMAIN 268..358
FT /note="SGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00386"
FT REGION 255..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 358 AA; 39762 MW; 711172817DD349C3 CRC64;
MAKELAEKAK EAFLDDDFDV AVDLYSKAID LDPNCAAFFA DRAQANIKID NFTEAVVDAN
KAIELEPTLA KAYLRKGTAC MKLEEYSTAK AALEKGASVA PNEPKFKKMI DECDLRIAEE
EKDLVQPMPP SLPSSSTTPL ATEADAPPVP IPAAPAKPMF RHEFYQKPEE AVVTIFAKKV
PKENVTVEFG EQILSVVIDV AGEEAYHLQP RLFGKIIPEK CRFEVLSTKV EIRLAKAEII
TWASLEYGKG QSVLPKPNVS SALSQRPVYP SSKPAKDWDK LEAEVKKQEK DEKLDGDAAM
NKFFSDIYSS ADEDMRRAMN KSFAESNGTV LSTNWKEVGT KKVESTPPDG MELKKWEY
