SL11_ORYSJ
ID SL11_ORYSJ Reviewed; 694 AA.
AC Q0IMG9; Q2QND2; Q64HA9;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=E3 ubiquitin-protein ligase SPL11;
DE EC=2.3.2.27;
DE AltName: Full=Cell death-related protein SPL11;
DE AltName: Full=Protein spotted leaf 11;
DE AltName: Full=RING-type E3 ubiquitin transferase SPL11 {ECO:0000305};
GN Name=SPL11; OrderedLocusNames=Os12g0570000, LOC_Os12g38210;
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 [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF VAL-290.
RC STRAIN=cv. Nipponbare;
RX PubMed=15377756; DOI=10.1105/tpc.104.025171;
RA Zeng L.-R., Qu S., Bordeos A., Yang C., Baraoidan M., Yan H., Xie Q.,
RA Nahm B.H., Leung H., Wang G.-L.;
RT "Spotted leaf11, a negative regulator of plant cell death and defense,
RT encodes a U-Box/Armadillo repeat protein endowed with E3 Ubiquitin ligase
RT activity.";
RL Plant Cell 16:2795-2808(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 178-694.
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP FUNCTION, INTERACTION WITH SPIN1, AND SUBCELLULAR LOCATION.
RX PubMed=18586868; DOI=10.1105/tpc.108.058610;
RA Vega-Sanchez M.E., Zeng L., Chen S., Leung H., Wang G.L.;
RT "SPIN1, a K homology domain protein negatively regulated and ubiquitinated
RT by the E3 ubiquitin ligase SPL11, is involved in flowering time control in
RT rice.";
RL Plant Cell 20:1456-1469(2008).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that negatively regulates
CC programmed cell death and disease resistance. Participates in flowering
CC time control by mediating ubiquitination and subsequent proteasomal
CC degradation of SPIN1. {ECO:0000269|PubMed:15377756,
CC ECO:0000269|PubMed:18586868}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with SPIN1 (via N-terminus).
CC {ECO:0000269|PubMed:18586868}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18586868}. Cytoplasm
CC {ECO:0000269|PubMed:18586868}.
CC -!- TISSUE SPECIFICITY: Highly expressed in leaf, at intermediate levels in
CC shoot and weakly in root. {ECO:0000269|PubMed:15377756}.
CC -!- INDUCTION: In both incompatible and compatible interactions with rice
CC blast fungus (M.grisea).
CC -!- DISRUPTION PHENOTYPE: Lesion mimic (spontaneous cell death) phenotype.
CC Expression of defense-related genes and enhanced non-race-specific
CC resistance to rice blast fungus (M.oryzea) and to bacterial blight
CC (X.oryzae pv oryzae). Delay in flowering time under long day (LD)
CC conditions. {ECO:0000269|PubMed:15377756}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABA99652.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF30096.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY652589; AAT94160.1; -; mRNA.
DR EMBL; AY652590; AAT94161.1; -; Genomic_DNA.
DR EMBL; DP000011; ABA99652.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008218; BAF30096.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK105835; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; Q0IMG9; -.
DR SMR; Q0IMG9; -.
DR STRING; 4530.OS12T0570000-01; -.
DR PaxDb; Q0IMG9; -.
DR PRIDE; Q0IMG9; -.
DR eggNOG; KOG0167; Eukaryota.
DR HOGENOM; CLU_006348_0_0_1; -.
DR InParanoid; Q0IMG9; -.
DR PlantReactome; R-OSA-9611432; Recognition of fungal and bacterial pathogens and immunity response.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000763; Chromosome 12.
DR Proteomes; UP000059680; Chromosome 12.
DR Genevisible; Q0IMG9; OS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0031348; P:negative regulation of defense response; IMP:UniProtKB.
DR GO; GO:0043069; P:negative regulation of programmed cell death; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0048586; P:regulation of long-day photoperiodism, flowering; IMP:UniProtKB.
DR CDD; cd16664; RING-Ubox_PUB; 1.
DR Gene3D; 1.20.930.20; -; 1.
DR Gene3D; 1.25.10.10; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR036537; Adaptor_Cbl_N_dom_sf.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR045210; RING-Ubox_PUB.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00514; Arm; 3.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00185; ARM; 5.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Flowering; Nucleus; Plant defense; Reference proteome; Repeat;
KW Transferase; Ubl conjugation pathway.
FT CHAIN 1..694
FT /note="E3 ubiquitin-protein ligase SPL11"
FT /id="PRO_0000072127"
FT DOMAIN 272..346
FT /note="U-box"
FT REPEAT 398..438
FT /note="ARM 1"
FT REPEAT 439..479
FT /note="ARM 2"
FT REPEAT 480..520
FT /note="ARM 3"
FT REPEAT 521..561
FT /note="ARM 4"
FT REPEAT 562..602
FT /note="ARM 5"
FT REPEAT 603..650
FT /note="ARM 6"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 290
FT /note="V->R: Loss of E3 ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:15377756"
SQ SEQUENCE 694 AA; 75300 MW; 3FEDB892C7289E05 CRC64;
MAGDRAEEEE GEAPPPEARA AAAVERVAAA VEAVAAGAGA GAGEYRNAYR RQLLALSRRI
RLLGPFVEEL RERRRGEGEG EEEERALAPL ADALEAALAL LRLGREGSRI SLVLERDSVM
KKFQGVILQL EQALCDIPYN ELDISDEVRE QVELVHAQLK RAKERIDMPD DEFYNDLLSV
YDKNYDPSAE LAILGRLSEK LHLMTITDLT QESLALHEMV ASGGGQDPGE HIERMSMLLK
KIKDFVQTQN PDMGPPMASR VLDSNGDSRP ITIPDEFRCP ISLELMKDPV IVSTGQTYER
ACIEKWIASG HHTCPTTQQK MSTSALTPNY VLRSLISQWC ETNGMEPPKR STQPNKPTPA
CSSSERANID ALLSKLCSPD TEEQRSAAAE LRLLAKRNAN NRICIAEAGA IPLLLSLLSS
SDLRTQEHAV TALLNLSIHE DNKASIISSG AVPSIVHVLK NGSMEARENA AATLFSLSVI
DEYKVTIGGM GAIPALVVLL GEGSQRGKKD AAAALFNLCI YQGNKGRAIR AGLVPLIMGL
VTNPTGALMD EAMAILSILS SHPEGKAAIG AAEPVPVLVE MIGSGTPRNR ENAAAVMLHL
CSGEHHLVHL ARAQECGIMV PLRELALNGT DRGKRKAVQL LERMSRFLVQ QQEEQESQSQ
ASAQVPPQAT PEQVPENDIP EQLDSPASQY PMVV
