EL5_ORYSJ
ID EL5_ORYSJ Reviewed; 325 AA.
AC Q9LRB7; Q0E0C5;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=E3 ubiquitin-protein ligase EL5;
DE EC=2.3.2.27 {ECO:0000269|PubMed:12028574, ECO:0000269|PubMed:16186120};
DE AltName: Full=Protein ELICITOR 5;
DE AltName: Full=RING-type E3 ubiquitin transferase EL5 {ECO:0000305};
GN Name=EL5.1; Synonyms=EL5; OrderedLocusNames=Os02g0559800, LOC_Os02g35329;
GN ORFNames=P0435E12.16;
GN and
GN Name=EL5.2; Synonyms=EL5; OrderedLocusNames=Os02g0560200, LOC_Os02g35347;
GN ORFNames=P0435E12.20;
GN and
GN Name=EL5.3; Synonyms=EL5; OrderedLocusNames=Os02g0560600, LOC_Os02g35365;
GN ORFNames=P0435E12.24;
GN and
GN Name=EL5.4; Synonyms=EL5; OrderedLocusNames=Os02g0561000, LOC_Os02g35383;
GN ORFNames=P0435E12.28;
GN and
GN Name=EL5.5; Synonyms=EL5; OrderedLocusNames=Os02g0561400, LOC_Os02g35401;
GN ORFNames=P0435E12.32;
GN and
GN Name=EL5.6; Synonyms=EL5; OrderedLocusNames=Os02g0561800, LOC_Os02g35429;
GN ORFNames=P0435E12.37;
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], AND INDUCTION.
RC STRAIN=cv. Nipponbare;
RX PubMed=11448732; DOI=10.1016/s0168-9452(00)00390-3;
RA Takai R., Hasegawa K., Kaku H., Shibuya N., Minami E.;
RT "Isolation and analysis of expression mechanisms of a rice gene, EL5, which
RT shows structural similarity to ATL family from Arabidopsis, in response to
RT N-acetylchitooligosaccharide elicitor.";
RL Plant Sci. 160:577-583(2001).
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 MRNA].
RC STRAIN=cv. Nipponbare;
RG The rice full-length cDNA consortium;
RT "Oryza sativa full length cDNA.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, DOMAIN, AND MUTAGENESIS OF CYS-153.
RX PubMed=12028574; DOI=10.1046/j.1365-313x.2002.01299.x;
RA Takai R., Matsuda N., Nakano A., Hasegawa K., Akimoto C., Shibuya N.,
RA Minami E.;
RT "EL5, a rice N-acetylchitooligosaccharide elicitor-responsive RING-H2
RT finger protein, is a ubiquitin ligase which functions in vitro in co-
RT operation with an elicitor-responsive ubiquitin-conjugating enzyme,
RT OsUBC5b.";
RL Plant J. 30:447-455(2002).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF VAL-136; LEU-138; ARG-148;
RP CYS-153; GLU-160; VAL-162; ASP-163; MET-164; TRP-165; LEU-166; THR-171;
RP LEU-174 AND ARG-176.
RX PubMed=16186120; DOI=10.1074/jbc.m411127200;
RA Katoh S., Tsunoda Y., Murata K., Minami E., Katoh E.;
RT "Active site residues and amino acid specificity of the ubiquitin carrier
RT protein-binding RING-H2 finger domain.";
RL J. Biol. Chem. 280:41015-41024(2005).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-138; CYS-153;
RP VAL-162 AND TRP-165.
RX PubMed=17559513; DOI=10.1111/j.1365-313x.2007.03120.x;
RA Koiwai H., Tagiri A., Katoh S., Katoh E., Ichikawa H., Minami E.,
RA Nishizawa Y.;
RT "RT RING-H2 type ubiquitin ligase EL5 is involved in root development
RT through the maintenance of cell viability in rice.";
RL Plant J. 51:92-104(2007).
RN [9]
RP FUNCTION.
RX PubMed=19704739; DOI=10.4161/psb.3.2.5081;
RA Nishizawa Y., Katoh S., Koiwai H., Katoh E.;
RT "EL5 is involved in root development as an anti-cell death ubiquitin
RT ligase.";
RL Plant Signal. Behav. 3:148-150(2008).
RN [10]
RP STRUCTURE BY NMR OF 129-181 IN COMPLEX WITH ZINC.
RX PubMed=12588869; DOI=10.1074/jbc.m210531200;
RA Katoh S., Hong C., Tsunoda Y., Murata K., Takai R., Minami E., Yamazaki T.,
RA Katoh E.;
RT "High precision NMR structure and function of the RING-H2 finger domain of
RT EL5, a rice protein whose expression is increased upon exposure to
RT pathogen-derived oligosaccharides.";
RL J. Biol. Chem. 278:15341-15348(2003).
CC -!- FUNCTION: Functions as a E3 ubiquitin-protein ligase in cooperation
CC with the E2 ubiquitin conjugating enzymes UBC5A and UBC5B. Involved in
CC root development. Required for the maintenance of cell viability after
CC the initiation of root primordial formation. May mediate the
CC degradation of cytotoxic proteins produced in root cells after the
CC actions of auxin, cytokinin and jasmonic acid. Mediates 'Lys-48'-linked
CC polyubiquitination of MBP in vitro. {ECO:0000269|PubMed:12028574,
CC ECO:0000269|PubMed:16186120, ECO:0000269|PubMed:17559513,
CC ECO:0000269|PubMed:19704739}.
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; Evidence={ECO:0000269|PubMed:12028574,
CC ECO:0000269|PubMed:16186120};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17559513};
CC Single-pass membrane protein {ECO:0000269|PubMed:17559513}.
CC -!- INDUCTION: By N-acetylchitooligosaccharide elicitor and by protein
CC phosphatase inhibitor calyculin A. Induction by N-
CC acetylchitooligosaccharide elicitor is inhibited by the protein kinase
CC inhibitor K-252a. {ECO:0000269|PubMed:11448732}.
CC -!- DOMAIN: The RING-type zinc-finger domain is required for E3 ubiquitin
CC ligase activity. {ECO:0000269|PubMed:12028574}.
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DR EMBL; AB045120; BAA96874.1; -; mRNA.
DR EMBL; AP005883; BAD16530.1; -; Genomic_DNA.
DR EMBL; AP005883; BAD16534.1; -; Genomic_DNA.
DR EMBL; AP005883; BAD16538.1; -; Genomic_DNA.
DR EMBL; AP005883; BAD16542.1; -; Genomic_DNA.
DR EMBL; AP005883; BAD16545.1; -; Genomic_DNA.
DR EMBL; AP005883; BAD16550.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF09063.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS79271.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS79266.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS79262.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS79258.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS79254.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS79250.1; -; Genomic_DNA.
DR EMBL; AK243670; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015623318.1; XM_015767832.1.
DR RefSeq; XP_015623949.1; XM_015768463.1.
DR RefSeq; XP_015623951.1; XM_015768465.1.
DR RefSeq; XP_015623952.1; XM_015768466.1.
DR RefSeq; XP_015623959.1; XM_015768473.1.
DR RefSeq; XP_015623960.1; XM_015768474.1.
DR PDB; 1IYM; NMR; -; A=129-181.
DR PDBsum; 1IYM; -.
DR AlphaFoldDB; Q9LRB7; -.
DR BMRB; Q9LRB7; -.
DR SMR; Q9LRB7; -.
DR STRING; 4530.OS02T0559800-01; -.
DR PaxDb; Q9LRB7; -.
DR PRIDE; Q9LRB7; -.
DR EnsemblPlants; Os02t0559800-01; Os02t0559800-01; Os02g0559800.
DR EnsemblPlants; Os02t0560200-01; Os02t0560200-01; Os02g0560200.
DR EnsemblPlants; Os02t0560600-01; Os02t0560600-01; Os02g0560600.
DR EnsemblPlants; Os02t0561000-01; Os02t0561000-01; Os02g0561000.
DR EnsemblPlants; Os02t0561400-01; Os02t0561400-01; Os02g0561400.
DR EnsemblPlants; Os02t0561800-01; Os02t0561800-01; Os02g0561800.
DR GeneID; 107276747; -.
DR GeneID; 107276748; -.
DR GeneID; 107276749; -.
DR GeneID; 107276750; -.
DR GeneID; 107276751; -.
DR GeneID; 4329685; -.
DR Gramene; Os02t0559800-01; Os02t0559800-01; Os02g0559800.
DR Gramene; Os02t0560200-01; Os02t0560200-01; Os02g0560200.
DR Gramene; Os02t0560600-01; Os02t0560600-01; Os02g0560600.
DR Gramene; Os02t0561000-01; Os02t0561000-01; Os02g0561000.
DR Gramene; Os02t0561400-01; Os02t0561400-01; Os02g0561400.
DR Gramene; Os02t0561800-01; Os02t0561800-01; Os02g0561800.
DR KEGG; osa:107276747; -.
DR KEGG; osa:107276748; -.
DR KEGG; osa:107276749; -.
DR KEGG; osa:107276750; -.
DR KEGG; osa:107276751; -.
DR KEGG; osa:4329685; -.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_066543_1_1_1; -.
DR InParanoid; Q9LRB7; -.
DR OMA; PANYYAT; -.
DR OrthoDB; 1487241at2759; -.
DR PlantReactome; R-OSA-9030654; Primary root development.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; Q9LRB7; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; Q9LRB7; OS.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0017119; C:Golgi transport complex; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IMP:UniProtKB.
DR GO; GO:0006896; P:Golgi to vacuole transport; IBA:GO_Central.
DR GO; GO:0006623; P:protein targeting to vacuole; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0048364; P:root development; IMP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Membrane; Metal-binding; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..325
FT /note="E3 ubiquitin-protein ligase EL5"
FT /id="PRO_0000055900"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 134..176
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 136
FT /note="V->A: Loss of E3 ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:16186120"
FT MUTAGEN 138
FT /note="L->A: Reduces E3 ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:16186120,
FT ECO:0000269|PubMed:17559513"
FT MUTAGEN 148
FT /note="R->A: Reduces E3 ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:16186120"
FT MUTAGEN 153
FT /note="C->A: Loss of E3 ubiquitin ligase activity. Rootless
FT phenotype."
FT /evidence="ECO:0000269|PubMed:12028574,
FT ECO:0000269|PubMed:16186120, ECO:0000269|PubMed:17559513"
FT MUTAGEN 153
FT /note="C->K: Loss of E3 ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:12028574,
FT ECO:0000269|PubMed:16186120, ECO:0000269|PubMed:17559513"
FT MUTAGEN 160
FT /note="E->A: No effect on E3 ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:16186120"
FT MUTAGEN 162
FT /note="V->A: Reduces E3 ubiquitin ligase activity. Short
FT crown roots with necrotic lateral roots."
FT /evidence="ECO:0000269|PubMed:16186120,
FT ECO:0000269|PubMed:17559513"
FT MUTAGEN 163
FT /note="D->A: Reduces E3 ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:16186120"
FT MUTAGEN 164
FT /note="M->A: No effect on E3 ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:16186120"
FT MUTAGEN 165
FT /note="W->A: Loss of E3 ubiquitin ligase activity. Rootless
FT phenotype."
FT /evidence="ECO:0000269|PubMed:16186120,
FT ECO:0000269|PubMed:17559513"
FT MUTAGEN 166
FT /note="L->A: Loss of E3 ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:16186120"
FT MUTAGEN 171
FT /note="T->A: No effect on E3 ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:16186120"
FT MUTAGEN 174
FT /note="L->A: Reduces E3 ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:16186120"
FT MUTAGEN 176
FT /note="R->A,D: Loss of E3 ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:16186120"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:1IYM"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:1IYM"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:1IYM"
FT TURN 165..168
FT /evidence="ECO:0007829|PDB:1IYM"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:1IYM"
SQ SEQUENCE 325 AA; 33239 MW; 2CD93BBC85060248 CRC64;
MVRGVEQGGP AMDESSSSSS PSPVSAPAGQ AAMTAGGIAT VAAVLIVFAA LTLAFVLLQC
YCDERRRAVT TTSTSGRGRR PRPRRRSGSG GDGGTGGGVD PEVLRSLPVT VYSRSTAAAA
AKEEEEEDDD GVECAVCLAE LEDGEEARFL PRCGHGFHAE CVDMWLGSHS TCPLCRLTVV
VPPPPLPPVP PEPPASYTVS LPASVLLGLS DHGAGAVTMT AEGRSTLVIE IPESAASTTP
RDAAARSSPS LARLRSLRRL WSFGRQGAAG STSSCSCATG GDNDDGDVEH GVSVTVAIRA
VEAATPARPP EAEAGARTAA AHVRN