SGT1A_ARATH
ID SGT1A_ARATH Reviewed; 350 AA.
AC Q9SUR9; Q84LL4; Q8W515;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 159.
DE RecName: Full=Protein SGT1 homolog A {ECO:0000250|UniProtKB:Q08446};
DE Short=AtSGT1a;
DE AltName: Full=Suppressor of G2 allele of SKP1 homolog A {ECO:0000250|UniProtKB:Q08446};
GN Name=SGT1A; OrderedLocusNames=At4g23570; ORFNames=F9D16.40;
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] (ISOFORM 1), 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 [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 [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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [MRNA] OF 77-350.
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 [6]
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 [7]
RP INDUCTION BY HEAT SHOCK.
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 [8]
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 151-240 IN COMPLEX WITH BARLEY
RP HSP90, AND MUTAGENESIS OF TYR-157; PHE-168; TYR-199; THR-220; LYS-221 AND
RP GLU-223.
RX PubMed=18818696; DOI=10.1038/emboj.2008.190;
RA Zhang M., Boter M., Li K., Kadota Y., Panaretou B., Prodromou C.,
RA Shirasu K., Pearl L.H.;
RT "Structural and functional coupling of Hsp90- and Sgt1-centred multi-
RT protein complexes.";
RL EMBO J. 27:2789-2798(2008).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 150-241 IN COMPLEX WITH RAR1 AND
RP BARLEY HSP90, AND SUBUNIT.
RX PubMed=20670895; DOI=10.1016/j.molcel.2010.05.010;
RA Zhang M., Kadota Y., Prodromou C., Shirasu K., Pearl L.H.;
RT "Structural basis for assembly of Hsp90-Sgt1-CHORD protein complexes:
RT implications for chaperoning of NLR innate immunity receptors.";
RL Mol. Cell 39:269-281(2010).
CC -!- FUNCTION: Functions in R gene-mediated resistance, but participates in
CC a lower extent than SGT1B to RPP5-mediated resistance. Not required for
CC RPM1, RPS2, RPS4 and RPS5-mediated resistance. Probably required for
CC SCF-mediated ubiquitination, by coupling HSP90 to SCF complex for
CC ubiquitination of HSP90 client proteins. {ECO:0000269|PubMed:16619029}.
CC -!- SUBUNIT: Interacts with RAR1. Forms a ternary complex with RAR1 and
CC barley HSP90. {ECO:0000269|PubMed:11847307,
CC ECO:0000269|PubMed:18818696, ECO:0000269|PubMed:20670895}.
CC -!- INTERACTION:
CC Q9SUR9; Q7XJ80: HSP90; Xeno; NbExp=8; IntAct=EBI-1778186, EBI-8080730;
CC Q9SUR9; Q0Q0I7: HSP90-2; Xeno; NbExp=2; IntAct=EBI-1778186, EBI-8081141;
CC Q9SUR9; A0A0H3NF38: sspH2; Xeno; NbExp=2; IntAct=EBI-1778186, EBI-10689860;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SUR9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SUR9-2; Sequence=VSP_040398;
CC -!- INDUCTION: By infection with the oomycete H.parasitica (downy mildew)
CC and heat shock. {ECO:0000269|PubMed:16619029,
CC ECO:0000269|PubMed:18065690}.
CC -!- SIMILARITY: Belongs to the SGT1 family. {ECO:0000305}.
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DR EMBL; AF439975; AAL33611.1; -; mRNA.
DR EMBL; AL035394; CAA23023.1; -; Genomic_DNA.
DR EMBL; AL161559; CAB79312.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84776.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84777.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84778.1; -; Genomic_DNA.
DR EMBL; AY063978; AAL36334.1; -; mRNA.
DR EMBL; AY096395; AAM20035.1; -; mRNA.
DR EMBL; AJ318020; CAC85267.1; -; mRNA.
DR PIR; T05589; T05589.
DR RefSeq; NP_001031704.1; NM_001036627.2. [Q9SUR9-2]
DR RefSeq; NP_194088.1; NM_118488.6. [Q9SUR9-1]
DR RefSeq; NP_849429.1; NM_179098.3. [Q9SUR9-1]
DR PDB; 2JKI; X-ray; 3.30 A; S/T/U=151-240.
DR PDB; 2XCM; X-ray; 2.20 A; C/D=150-241.
DR PDBsum; 2JKI; -.
DR PDBsum; 2XCM; -.
DR AlphaFoldDB; Q9SUR9; -.
DR SMR; Q9SUR9; -.
DR BioGRID; 13746; 12.
DR IntAct; Q9SUR9; 7.
DR MINT; Q9SUR9; -.
DR PaxDb; Q9SUR9; -.
DR PRIDE; Q9SUR9; -.
DR ProteomicsDB; 232585; -. [Q9SUR9-1]
DR EnsemblPlants; AT4G23570.1; AT4G23570.1; AT4G23570. [Q9SUR9-1]
DR EnsemblPlants; AT4G23570.2; AT4G23570.2; AT4G23570. [Q9SUR9-1]
DR EnsemblPlants; AT4G23570.3; AT4G23570.3; AT4G23570. [Q9SUR9-2]
DR GeneID; 828457; -.
DR Gramene; AT4G23570.1; AT4G23570.1; AT4G23570. [Q9SUR9-1]
DR Gramene; AT4G23570.2; AT4G23570.2; AT4G23570. [Q9SUR9-1]
DR Gramene; AT4G23570.3; AT4G23570.3; AT4G23570. [Q9SUR9-2]
DR KEGG; ath:AT4G23570; -.
DR Araport; AT4G23570; -.
DR TAIR; locus:2128404; AT4G23570.
DR eggNOG; KOG0376; Eukaryota.
DR eggNOG; KOG1309; Eukaryota.
DR InParanoid; Q9SUR9; -.
DR OMA; WYQSHDS; -.
DR OrthoDB; 1426397at2759; -.
DR PhylomeDB; Q9SUR9; -.
DR EvolutionaryTrace; Q9SUR9; -.
DR PRO; PR:Q9SUR9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SUR9; baseline and differential.
DR Genevisible; Q9SUR9; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:TAIR.
DR GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR GO; GO:0071365; P:cellular response to auxin stimulus; IMP:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0006952; P:defense response; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IBA:GO_Central.
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:0050821; P:protein stabilization; IBA:GO_Central.
DR GO; GO:1900150; P:regulation of defense response to fungus; IMP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS: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; 2.
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 3D-structure; Alternative splicing; Immunity; Innate immunity;
KW Plant defense; Reference proteome; Repeat; TPR repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..350
FT /note="Protein SGT1 homolog A"
FT /id="PRO_0000403647"
FT REPEAT 2..35
FT /note="TPR 1"
FT REPEAT 37..69
FT /note="TPR 2"
FT REPEAT 71..103
FT /note="TPR 3"
FT DOMAIN 149..238
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT DOMAIN 260..350
FT /note="SGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00386"
FT VAR_SEQ 53
FT /note="T -> TA (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_040398"
FT MUTAGEN 157
FT /note="Y->A,R: Diminishes the interaction with barley
FT HSP90."
FT /evidence="ECO:0000269|PubMed:18818696"
FT MUTAGEN 168
FT /note="F->S,R: Diminishes the interaction with barley
FT HSP90."
FT /evidence="ECO:0000269|PubMed:18818696"
FT MUTAGEN 199
FT /note="Y->A,R: No effect on the interaction with barley
FT HSP90."
FT /evidence="ECO:0000269|PubMed:18818696"
FT MUTAGEN 220
FT /note="T->A,R: No effect on the interaction with barley
FT HSP90."
FT /evidence="ECO:0000269|PubMed:18818696"
FT MUTAGEN 221
FT /note="K->E: Diminishes the interaction with barley HSP90."
FT /evidence="ECO:0000269|PubMed:18818696"
FT MUTAGEN 223
FT /note="E->A,R: Diminishes the interaction with barley
FT HSP90."
FT /evidence="ECO:0000269|PubMed:18818696"
FT CONFLICT 225
FT /note="C -> R (in Ref. 1; AAL33611)"
FT /evidence="ECO:0000305"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:2XCM"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:2XCM"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:2XCM"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:2XCM"
FT STRAND 183..190
FT /evidence="ECO:0007829|PDB:2XCM"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:2JKI"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:2XCM"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:2XCM"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:2XCM"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:2XCM"
FT STRAND 222..231
FT /evidence="ECO:0007829|PDB:2XCM"
SQ SEQUENCE 350 AA; 39225 MW; D23DBE83BC8ACFA5 CRC64;
MAKELADKAK EAFVDDDFDV AVDLYSKAID LDPNCAEFFA DRAQAYIKLE SFTEAVADAN
KAIELDPSLT KAYLRKGTAC MKLEEYRTAK TALEKGASIT PSESKFKKLI DECNFLITEE
EKDLVQPVPS TLPSSVTAPP VSELDVTPTA KYRHEYYQKP EEVVVTVFAK GIPKQNVNID
FGEQILSVVI EVPGEDAYYL QPRLFGKIIP DKCKYEVLST KIEICLAKAD IITWASLEHG
KGPAVLPKPN VSSEVSQRPA YPSSKKVKDW DKLEAEVKKQ EKDEKLEGDA ALNKFFREIY
QNADEDMRRA MSKSFVESNG TVLSTNWQEV GTKTIESTPP DGMELKKWEI
