SGT1_ORYSJ
ID SGT1_ORYSJ Reviewed; 367 AA.
AC Q0JL44; Q9SE32;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Protein SGT1 homolog {ECO:0000250|UniProtKB:Q08446};
DE Short=OsSGT1 {ECO:0000303|PubMed:18257679};
DE AltName: Full=Suppressor of G2 allele of SKP1 homolog {ECO:0000250|UniProtKB:Q08446};
GN Name=SGT1 {ECO:0000303|PubMed:14733924};
GN OrderedLocusNames=Os01g0624500, LOC_Os01g43540; ORFNames=OsJ_02663;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10571178; DOI=10.1016/s0092-8674(00)81522-6;
RA Shirasu K., Lahaye T., Tan M.-W., Zhou F., Azevedo C., Schulze-Lefert P.;
RT "A novel class of eukaryotic zinc-binding proteins is required for disease
RT resistance signaling in barley and development in C. elegans.";
RL Cell 99:355-366(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP FUNCTION, INTERACTION WITH RAR1, AND SUBCELLULAR LOCATION.
RX PubMed=18257679; DOI=10.1094/mpmi-21-3-0294;
RA Wang Y., Gao M., Li Q., Wang L., Wang J., Jeon J.S., Qu N., Zhang Y.,
RA He Z.;
RT "OsRAR1 and OsSGT1 physically interact and function in rice basal disease
RT resistance.";
RL Mol. Plant Microbe Interact. 21:294-303(2008).
RN [7]
RP INTERACTION WITH RAD6, TISSUE SPECIFICITY, AND INDUCTION BY HYDROGEN
RP PEROXIDE.
RX PubMed=14733924; DOI=10.1016/j.bbrc.2003.12.144;
RA Yamamoto T., Mori Y., Ishibashi T., Uchiyama Y., Sakaguchi N., Furukawa T.,
RA Hashimoto J., Kimura S., Sakaguchi K.;
RT "Characterization of Rad6 from a higher plant, rice (Oryza sativa L.) and
RT its interaction with Sgt1, a subunit of the SCF ubiquitin ligase complex.";
RL Biochem. Biophys. Res. Commun. 314:434-439(2004).
CC -!- FUNCTION: Involved in basal disease resistance to bacterial blight
CC (X.oryzae). May act as positive regulator of basal defense. Probably
CC required for SCF-mediated ubiquitination, by coupling HSP90 to SCF
CC complex for ubiquitination of HSP90 client proteins.
CC {ECO:0000269|PubMed:18257679}.
CC -!- SUBUNIT: Interacts (via CS domain) with RAR1 (via CHORD 2 domain).
CC Interacts with RAD6. {ECO:0000269|PubMed:14733924,
CC ECO:0000269|PubMed:18257679}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18257679}. Nucleus
CC {ECO:0000269|PubMed:18257679}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, root tips, shoot apical
CC meristem (SAM), young leaves, flag leaves and ears.
CC {ECO:0000269|PubMed:14733924}.
CC -!- INDUCTION: By hydrogen peroxide. {ECO:0000269|PubMed:14733924}.
CC -!- SIMILARITY: Belongs to the SGT1 family. {ECO:0000305}.
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DR EMBL; AF192467; AAF18438.1; -; mRNA.
DR EMBL; AP008207; BAF05534.1; -; Genomic_DNA.
DR EMBL; AP014957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM000138; EEE55012.1; -; Genomic_DNA.
DR RefSeq; XP_015621707.1; XM_015766221.1.
DR AlphaFoldDB; Q0JL44; -.
DR SMR; Q0JL44; -.
DR IntAct; Q0JL44; 9.
DR STRING; 4530.OS01T0624500-01; -.
DR PaxDb; Q0JL44; -.
DR PRIDE; Q0JL44; -.
DR GeneID; 4326682; -.
DR KEGG; osa:4326682; -.
DR eggNOG; KOG1309; Eukaryota.
DR HOGENOM; CLU_039532_2_1_1; -.
DR InParanoid; Q0JL44; -.
DR OrthoDB; 1426397at2759; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000007752; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
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 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; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Plant defense; Reference proteome; Repeat; TPR repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..367
FT /note="Protein SGT1 homolog"
FT /id="PRO_0000403650"
FT REPEAT 6..39
FT /note="TPR 1"
FT REPEAT 40..73
FT /note="TPR 2"
FT REPEAT 75..107
FT /note="TPR 3"
FT DOMAIN 165..254
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT DOMAIN 277..367
FT /note="SGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00386"
FT REGION 261..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 126
FT /note="S -> T (in Ref. 1; AAF18438)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 367 AA; 40938 MW; 885E7758A754FED1 CRC64;
MATAAASDLE SKAKAAFVDD DFELAAELYT QAIEASPATA ELYADRAQAH IKLGNYTEAV
ADANKAIELD PSMHKAYLRK GAACIRLEEY QTAKAALELG YSFASGDSRF TRLMKECDER
IAEELSEVPV KKAEDGAAAP SVASFVEEKD DAANMDNTPP MVEVKPKYRH DFYNSATEVV
LTIFAKGVPA ENVVVDFGEQ MLSVSIEVPG EEPYHFQPRL FSKIIPEKSR YQVLSTKVEI
RLAKAEQITW TSLDYDKKPK AVPQKIIPPA ESAQRPSYPS SKSKKDWDKL EAEVKKEEKE
EKLEGDAALN KFFRDIYSDA DEDMRRAMMK SFVESNGTVL STNWKDVGSK KVEGSPPDGM
ELKKWEY
