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SL11_ORYSI
ID   SL11_ORYSI              Reviewed;         694 AA.
AC   A2ZLU6; Q64HA9;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Protein spotted leaf 11;
DE            EC=2.3.2.27;
DE   AltName: Full=Cell death-related protein SPL11;
DE   AltName: Full=RING-type E3 ubiquitin transferase SPL11 {ECO:0000305};
GN   Name=SPL11; ORFNames=OsI_037539;
OS   Oryza sativa subsp. indica (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=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
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   [2]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=cv. IR68;
RX   PubMed=10939258; DOI=10.1094/mpmi.2000.13.8.869;
RA   Yin Z., Chen J., Zeng L., Goh M., Leung H., Khush G.S., Wang G.-L.;
RT   "Characterizing rice lesion mimic mutants and identifying a mutant with
RT   broad-spectrum resistance to rice blast and bacterial blight.";
RL   Mol. Plant Microbe Interact. 13:869-876(2000).
RN   [3]
RP   FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF VAL-290.
RC   STRAIN=cv. IR64, and cv. IR68;
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).
CC   -!- FUNCTION: Defense related protein that negatively regulates programmed
CC       cell death. In vitro, possesses E3 ubiquitin ligase activity.
CC       {ECO:0000269|PubMed:15377756}.
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   -!- 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: Plants exhibit non-race-specific resistance to
CC       rice blast fungus (M.grisea) and to bacterial blight (X.oryzae pv
CC       oryzae). Lesion mimic mutant spl11 is expressing defense-related genes
CC       in fully expanded leaf. {ECO:0000269|PubMed:10939258}.
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DR   EMBL; CM000137; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A2ZLU6; -.
DR   SMR; A2ZLU6; -.
DR   STRING; 39946.A2ZLU6; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000007015; Chromosome 12.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
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   Reference proteome; Repeat; Transferase; Ubl conjugation pathway.
FT   CHAIN           1..694
FT                   /note="Protein spotted leaf 11"
FT                   /id="PRO_0000300254"
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
 
 
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