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E3 ubiquitin-protein ligase EL5 (EC 2.3.2.27) (Protein ELICITOR 5) (RING-type E3 ubiquitin transferase EL5)

 EL5_ORYSJ               Reviewed;         325 AA.
Q9LRB7; Q0E0C5;
01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-APR-2018, entry version 107.
RecName: Full=E3 ubiquitin-protein ligase EL5;
EC=2.3.2.27 {ECO:0000269|PubMed:12028574, ECO:0000269|PubMed:16186120};
AltName: Full=Protein ELICITOR 5;
AltName: Full=RING-type E3 ubiquitin transferase EL5 {ECO:0000305};
Name=EL5.1; Synonyms=EL5;
OrderedLocusNames=Os02g0559800, LOC_Os02g35329; ORFNames=P0435E12.16;
and
Name=EL5.2; Synonyms=EL5;
OrderedLocusNames=Os02g0560200, LOC_Os02g35347; ORFNames=P0435E12.20;
and
Name=EL5.3; Synonyms=EL5;
OrderedLocusNames=Os02g0560600, LOC_Os02g35365; ORFNames=P0435E12.24;
and
Name=EL5.4; Synonyms=EL5;
OrderedLocusNames=Os02g0561000, LOC_Os02g35383; ORFNames=P0435E12.28;
and
Name=EL5.5; Synonyms=EL5;
OrderedLocusNames=Os02g0561400, LOC_Os02g35401; ORFNames=P0435E12.32;
and
Name=EL5.6; Synonyms=EL5;
OrderedLocusNames=Os02g0561800, LOC_Os02g35429; ORFNames=P0435E12.37;
Oryza sativa subsp. japonica (Rice).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade;
Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
NCBI_TaxID=39947;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
STRAIN=cv. Nipponbare;
PubMed=11448732; DOI=10.1016/S0168-9452(00)00390-3;
Takai R., Hasegawa K., Kaku H., Shibuya N., Minami E.;
"Isolation and analysis of expression mechanisms of a rice gene, EL5,
which shows structural similarity to ATL family from Arabidopsis, in
response to N-acetylchitooligosaccharide elicitor.";
Plant Sci. 160:577-583(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Nipponbare;
PubMed=16100779; DOI=10.1038/nature03895;
International rice genome sequencing project (IRGSP);
"The map-based sequence of the rice genome.";
Nature 436:793-800(2005).
[3]
GENOME REANNOTATION.
STRAIN=cv. Nipponbare;
PubMed=18089549; DOI=10.1093/nar/gkm978;
The rice annotation project (RAP);
"The rice annotation project database (RAP-DB): 2008 update.";
Nucleic Acids Res. 36:D1028-D1033(2008).
[4]
GENOME REANNOTATION.
STRAIN=cv. Nipponbare;
PubMed=24280374; DOI=10.1186/1939-8433-6-4;
Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H.,
McCombie W.R., Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S.,
Childs K.L., Davidson R.M., Lin H., Quesada-Ocampo L.,
Vaillancourt B., Sakai H., Lee S.S., Kim J., Numa H., Itoh T.,
Buell C.R., Matsumoto T.;
"Improvement of the Oryza sativa Nipponbare reference genome using
next generation sequence and optical map data.";
Rice 6:4-4(2013).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Nipponbare;
The rice full-length cDNA consortium;
"Oryza sativa full length cDNA.";
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
[6]
FUNCTION, CATALYTIC ACTIVITY, DOMAIN, AND MUTAGENESIS OF CYS-153.
PubMed=12028574; DOI=10.1046/j.1365-313X.2002.01299.x;
Takai R., Matsuda N., Nakano A., Hasegawa K., Akimoto C., Shibuya N.,
Minami E.;
"EL5, a rice N-acetylchitooligosaccharide elicitor-responsive RING-H2
finger protein, is a ubiquitin ligase which functions in vitro in co-
operation with an elicitor-responsive ubiquitin-conjugating enzyme,
OsUBC5b.";
Plant J. 30:447-455(2002).
[7]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF VAL-136; LEU-138;
ARG-148; CYS-153; GLU-160; VAL-162; ASP-163; MET-164; TRP-165;
LEU-166; THR-171; LEU-174 AND ARG-176.
PubMed=16186120; DOI=10.1074/jbc.M411127200;
Katoh S., Tsunoda Y., Murata K., Minami E., Katoh E.;
"Active site residues and amino acid specificity of the ubiquitin
carrier protein-binding RING-H2 finger domain.";
J. Biol. Chem. 280:41015-41024(2005).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-138; CYS-153;
VAL-162 AND TRP-165.
PubMed=17559513; DOI=10.1111/j.1365-313X.2007.03120.x;
Koiwai H., Tagiri A., Katoh S., Katoh E., Ichikawa H., Minami E.,
Nishizawa Y.;
"RT RING-H2 type ubiquitin ligase EL5 is involved in root development
through the maintenance of cell viability in rice.";
Plant J. 51:92-104(2007).
[9]
FUNCTION.
PubMed=19704739; DOI=10.4161/psb.3.2.5081;
Nishizawa Y., Katoh S., Koiwai H., Katoh E.;
"EL5 is involved in root development as an anti-cell death ubiquitin
ligase.";
Plant Signal. Behav. 3:148-150(2008).
[10]
STRUCTURE BY NMR OF 129-181 IN COMPLEX WITH ZINC.
PubMed=12588869; DOI=10.1074/jbc.M210531200;
Katoh S., Hong C., Tsunoda Y., Murata K., Takai R., Minami E.,
Yamazaki T., Katoh E.;
"High precision NMR structure and function of the RING-H2 finger
domain of EL5, a rice protein whose expression is increased upon
exposure to pathogen-derived oligosaccharides.";
J. Biol. Chem. 278:15341-15348(2003).
-!- FUNCTION: Functions as a E3 ubiquitin-protein ligase in
cooperation with the E2 ubiquitin conjugating enzymes UBC5A and
UBC5B. Involved in root development. Required for the maintenance
of cell viability after the initiation of root primordial
formation. May mediate the degradation of cytotoxic proteins
produced in root cells after the actions of auxin, cytokinin and
jasmonic acid. Mediates 'Lys-48'-linked polyubiquitination of MBP
in vitro. {ECO:0000269|PubMed:12028574,
ECO:0000269|PubMed:16186120, ECO:0000269|PubMed:17559513,
ECO:0000269|PubMed:19704739}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000269|PubMed:12028574,
ECO:0000269|PubMed:16186120}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17559513};
Single-pass membrane protein {ECO:0000269|PubMed:17559513}.
-!- INDUCTION: By N-acetylchitooligosaccharide elicitor and by protein
phosphatase inhibitor calyculin A. Induction by N-
acetylchitooligosaccharide elicitor is inhibited by the protein
kinase inhibitor K-252a. {ECO:0000269|PubMed:11448732}.
-!- DOMAIN: The RING-type zinc-finger domain is required for E3
ubiquitin ligase activity. {ECO:0000269|PubMed:12028574}.
-----------------------------------------------------------------------
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EMBL; AB045120; BAA96874.1; -; mRNA.
EMBL; AP005883; BAD16530.1; -; Genomic_DNA.
EMBL; AP005883; BAD16534.1; -; Genomic_DNA.
EMBL; AP005883; BAD16538.1; -; Genomic_DNA.
EMBL; AP005883; BAD16542.1; -; Genomic_DNA.
EMBL; AP005883; BAD16545.1; -; Genomic_DNA.
EMBL; AP005883; BAD16550.1; -; Genomic_DNA.
EMBL; AP008208; BAF09063.1; -; Genomic_DNA.
EMBL; AP014958; BAS79271.1; -; Genomic_DNA.
EMBL; AP014958; BAS79266.1; -; Genomic_DNA.
EMBL; AP014958; BAS79262.1; -; Genomic_DNA.
EMBL; AP014958; BAS79258.1; -; Genomic_DNA.
EMBL; AP014958; BAS79254.1; -; Genomic_DNA.
EMBL; AP014958; BAS79250.1; -; Genomic_DNA.
EMBL; AK243670; -; NOT_ANNOTATED_CDS; mRNA.
RefSeq; XP_015623318.1; XM_015767832.1.
RefSeq; XP_015623949.1; XM_015768463.1.
RefSeq; XP_015623951.1; XM_015768465.1.
RefSeq; XP_015623952.1; XM_015768466.1.
RefSeq; XP_015623959.1; XM_015768473.1.
RefSeq; XP_015623960.1; XM_015768474.1.
PDB; 1IYM; NMR; -; A=129-181.
PDBsum; 1IYM; -.
ProteinModelPortal; Q9LRB7; -.
SMR; Q9LRB7; -.
STRING; 39947.LOC_Os02g35329.1; -.
PaxDb; Q9LRB7; -.
EnsemblPlants; Os02t0559800-01; Os02t0559800-01; Os02g0559800.
EnsemblPlants; Os02t0560200-01; Os02t0560200-01; Os02g0560200.
EnsemblPlants; Os02t0560600-01; Os02t0560600-01; Os02g0560600.
EnsemblPlants; Os02t0561000-01; Os02t0561000-01; Os02g0561000.
EnsemblPlants; Os02t0561400-01; Os02t0561400-01; Os02g0561400.
EnsemblPlants; Os02t0561800-01; Os02t0561800-01; Os02g0561800.
GeneID; 107276747; -.
GeneID; 107276748; -.
GeneID; 107276749; -.
GeneID; 107276750; -.
GeneID; 107276751; -.
GeneID; 4329685; -.
Gramene; Os02t0559800-01; Os02t0559800-01; Os02g0559800.
Gramene; Os02t0560200-01; Os02t0560200-01; Os02g0560200.
Gramene; Os02t0560600-01; Os02t0560600-01; Os02g0560600.
Gramene; Os02t0561000-01; Os02t0561000-01; Os02g0561000.
Gramene; Os02t0561400-01; Os02t0561400-01; Os02g0561400.
Gramene; Os02t0561800-01; Os02t0561800-01; Os02g0561800.
KEGG; osa:107276747; -.
KEGG; osa:107276748; -.
KEGG; osa:107276749; -.
KEGG; osa:107276750; -.
KEGG; osa:107276751; -.
KEGG; osa:4329685; -.
eggNOG; KOG0800; Eukaryota.
eggNOG; ENOG41121N2; LUCA.
HOGENOM; HOG000243710; -.
InParanoid; Q9LRB7; -.
KO; K16286; -.
OMA; ERVTICV; -.
OrthoDB; EOG09360R75; -.
UniPathway; UPA00143; -.
EvolutionaryTrace; Q9LRB7; -.
Proteomes; UP000059680; Chromosome 2.
Genevisible; Q9LRB7; OS.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0051301; P:cell division; IMP:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:0048364; P:root development; IMP:UniProtKB.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF13639; zf-RING_2; 1.
SMART; SM00184; RING; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Membrane;
Metal-binding; Reference proteome; Transferase; Transmembrane;
Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 325 E3 ubiquitin-protein ligase EL5.
/FTId=PRO_0000055900.
TRANSMEM 38 58 Helical. {ECO:0000255}.
ZN_FING 134 176 RING-type; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00175}.
COMPBIAS 182 194 Pro-rich.
MUTAGEN 136 136 V->A: Loss of E3 ubiquitin ligase
activity. {ECO:0000269|PubMed:16186120}.
MUTAGEN 138 138 L->A: Reduces E3 ubiquitin ligase
activity. {ECO:0000269|PubMed:16186120,
ECO:0000269|PubMed:17559513}.
MUTAGEN 148 148 R->A: Reduces E3 ubiquitin ligase
activity. {ECO:0000269|PubMed:16186120}.
MUTAGEN 153 153 C->A: Loss of E3 ubiquitin ligase
activity. Rootless phenotype.
{ECO:0000269|PubMed:12028574,
ECO:0000269|PubMed:16186120,
ECO:0000269|PubMed:17559513}.
MUTAGEN 153 153 C->K: Loss of E3 ubiquitin ligase
activity. {ECO:0000269|PubMed:12028574,
ECO:0000269|PubMed:16186120,
ECO:0000269|PubMed:17559513}.
MUTAGEN 160 160 E->A: No effect on E3 ubiquitin ligase
activity. {ECO:0000269|PubMed:16186120}.
MUTAGEN 162 162 V->A: Reduces E3 ubiquitin ligase
activity. Short crown roots with necrotic
lateral roots.
{ECO:0000269|PubMed:16186120,
ECO:0000269|PubMed:17559513}.
MUTAGEN 163 163 D->A: Reduces E3 ubiquitin ligase
activity. {ECO:0000269|PubMed:16186120}.
MUTAGEN 164 164 M->A: No effect on E3 ubiquitin ligase
activity. {ECO:0000269|PubMed:16186120}.
MUTAGEN 165 165 W->A: Loss of E3 ubiquitin ligase
activity. Rootless phenotype.
{ECO:0000269|PubMed:16186120,
ECO:0000269|PubMed:17559513}.
MUTAGEN 166 166 L->A: Loss of E3 ubiquitin ligase
activity. {ECO:0000269|PubMed:16186120}.
MUTAGEN 171 171 T->A: No effect on E3 ubiquitin ligase
activity. {ECO:0000269|PubMed:16186120}.
MUTAGEN 174 174 L->A: Reduces E3 ubiquitin ligase
activity. {ECO:0000269|PubMed:16186120}.
MUTAGEN 176 176 R->A,D: Loss of E3 ubiquitin ligase
activity. {ECO:0000269|PubMed:16186120}.
TURN 135 137 {ECO:0000244|PDB:1IYM}.
STRAND 151 153 {ECO:0000244|PDB:1IYM}.
HELIX 161 164 {ECO:0000244|PDB:1IYM}.
TURN 165 168 {ECO:0000244|PDB:1IYM}.
STRAND 173 175 {ECO:0000244|PDB:1IYM}.
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


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