E3 ubiquitin-protein ligase EL5 - Oryza sativa subsp. japonica (Rice)

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Q9LRB7 (EL5_ORYSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 75. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
E3 ubiquitin-protein ligase EL5
EC=6.3.2.-

Alternative name(s):
Protein ELICITOR 5

Gene names

Name:	EL5.1
Synonyms:	EL5
Ordered Locus Names:	Os02g0559800, LOC_Os02g35329
ORF Names:	P0435E12.16
AND
Name:	EL5.2
Synonyms:	EL5
Ordered Locus Names:	Os02g0560200, LOC_Os02g35347
ORF Names:	P0435E12.20
AND
Name:	EL5.3
Synonyms:	EL5
Ordered Locus Names:	Os02g0560600, LOC_Os02g35365
ORF Names:	P0435E12.24
AND
Name:	EL5.4
Synonyms:	EL5
Ordered Locus Names:	Os02g0556100, LOC_Os02g35383
ORF Names:	P0435E12.28
AND
Name:	EL5.5
Synonyms:	EL5
Ordered Locus Names:	Os02g0561400, LOC_Os02g35401
ORF Names:	P0435E12.32
AND
Name:	EL5.6
Synonyms:	EL5
Ordered Locus Names:	Os02g0561800, LOC_Os02g35429
ORF Names:	P0435E12.37

Organism

Oryza sativa subsp. japonica (Rice) [Reference proteome]

Taxonomic identifier

39947 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza ›

Protein attributes

Sequence length	325 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.4 Ref.5 Ref.6 Ref.7
Pathway	Protein modification; protein ubiquitination.
Subcellular location	Cell membrane; Single-pass membrane protein Ref.6.
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. Ref.1
Domain	The RING-type zinc-finger domain is required for E3 ubiquitin ligase activity. Ref.4
Sequence similarities	Contains 1 RING-type zinc finger.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from mutant phenotype Ref.6. Source: UniProtKB root development Inferred from mutant phenotype Ref.6. Source: UniProtKB
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay Ref.6. Source: UniProtKB
Molecular_function	ubiquitin-protein ligase activity Inferred from direct assay Ref.4. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 325

325

E3 ubiquitin-protein ligase EL5

PRO_0000055900

Regions

Transmembrane

38 – 58

Helical; Potential

Zinc finger

134 – 176

RING-type; atypical

Compositional bias

182 – 194

Pro-rich

Experimental info

Mutagenesis

136

V → A: Loss of E3 ubiquitin ligase activity. Ref.5

Mutagenesis

138

L → A: Reduces E3 ubiquitin ligase activity. Ref.5 Ref.6

Mutagenesis

148

R → A: Reduces E3 ubiquitin ligase activity. Ref.5

Mutagenesis

153

C → A: Loss of E3 ubiquitin ligase activity. Rootless phenotype. Ref.4 Ref.5 Ref.6

Mutagenesis

153

C → K: Loss of E3 ubiquitin ligase activity. Ref.4 Ref.5 Ref.6

Mutagenesis

160

E → A: No effect on E3 ubiquitin ligase activity. Ref.5

Mutagenesis

162

V → A: Reduces E3 ubiquitin ligase activity. Short crown roots with necrotic lateral roots. Ref.5 Ref.6

Mutagenesis

163

D → A: Reduces E3 ubiquitin ligase activity. Ref.5

Mutagenesis

164

M → A: No effect on E3 ubiquitin ligase activity. Ref.5

Mutagenesis

165

W → A: Loss of E3 ubiquitin ligase activity. Rootless phenotype. Ref.5 Ref.6

Mutagenesis

166

L → A: Loss of E3 ubiquitin ligase activity. Ref.5

Mutagenesis

171

T → A: No effect on E3 ubiquitin ligase activity. Ref.5

Mutagenesis

174

L → A: Reduces E3 ubiquitin ligase activity. Ref.5

Mutagenesis

176

R → A or D: Loss of E3 ubiquitin ligase activity. Ref.5

Secondary structure

325

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q9LRB7 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 2CD93BBC85060248
Show »

FASTA

325

33,239

        10         20         30         40         50         60 
MVRGVEQGGP AMDESSSSSS PSPVSAPAGQ AAMTAGGIAT VAAVLIVFAA LTLAFVLLQC 

        70         80         90        100        110        120 
YCDERRRAVT TTSTSGRGRR PRPRRRSGSG GDGGTGGGVD PEVLRSLPVT VYSRSTAAAA 

       130        140        150        160        170        180 
AKEEEEEDDD GVECAVCLAE LEDGEEARFL PRCGHGFHAE CVDMWLGSHS TCPLCRLTVV 

       190        200        210        220        230        240 
VPPPPLPPVP PEPPASYTVS LPASVLLGLS DHGAGAVTMT AEGRSTLVIE IPESAASTTP 

       250        260        270        280        290        300 
RDAAARSSPS LARLRSLRRL WSFGRQGAAG STSSCSCATG GDNDDGDVEH GVSVTVAIRA 

       310        320 
VEAATPARPP EAEAGARTAA AHVRN

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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." Takai R., Hasegawa K., Kaku H., Shibuya N., Minami E. Plant Sci. 160:577-583(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION. Strain: cv. Nipponbare.
[2]	"The map-based sequence of the rice genome." International rice genome sequencing project (IRGSP) Nature 436:793-800(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nipponbare.
[3]	"Collection, mapping, and annotation of over 28,000 cDNA clones from japonica rice." The rice full-length cDNA consortium Science 301:376-379(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Nipponbare.
[4]	"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." Takai R., Matsuda N., Nakano A., Hasegawa K., Akimoto C., Shibuya N., Minami E. Plant J. 30:447-455(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DOMAIN, MUTAGENESIS OF CYS-153.
[5]	"Active site residues and amino acid specificity of the ubiquitin carrier protein-binding RING-H2 finger domain." Katoh S., Tsunoda Y., Murata K., Minami E., Katoh E. J. Biol. Chem. 280:41015-41024(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, 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.
[6]	"RT RING-H2 type ubiquitin ligase EL5 is involved in root development through the maintenance of cell viability in rice." Koiwai H., Tagiri A., Katoh S., Katoh E., Ichikawa H., Minami E., Nishizawa Y. Plant J. 51:92-104(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-138; CYS-153; VAL-162 AND TRP-165.
[7]	"EL5 is involved in root development as an anti-cell death ubiquitin ligase." Nishizawa Y., Katoh S., Koiwai H., Katoh E. Plant Signal. Behav. 3:148-150(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"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." Katoh S., Hong C., Tsunoda Y., Murata K., Takai R., Minami E., Yamazaki T., Katoh E. J. Biol. Chem. 278:15341-15348(2003) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 129-181 IN COMPLEX WITH ZINC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB045120 mRNA. Translation: BAA96874.1.
AP005883 Genomic DNA. Translation: BAD16530.1.
AP005883 Genomic DNA. Translation: BAD16534.1.
AP005883 Genomic DNA. Translation: BAD16538.1.
AP005883 Genomic DNA. Translation: BAD16542.1.
AP005883 Genomic DNA. Translation: BAD16545.1.
AP005883 Genomic DNA. Translation: BAD16550.1.
AK243670 mRNA. No translation available.

RefSeq

NP_001047149.1. NM_001053684.1.

UniGene

Os.3710.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IYM	NMR	-	A	129-181	[»]

ProteinModelPortal

Q9LRB7.

SMR

Q9LRB7. Positions 129-181.

ModBase

Search...

Proteomic databases

PaxDb

Q9LRB7.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

LOC_Os02g35329.1; LOC_Os02g35329.1; LOC_Os02g35329.

GeneID

4329685.

KEGG

dosa:Os02t0559800-01.
dosa:Os02t0560200-01.
dosa:Os02t0560600-01.
dosa:Os02t0561000-01.
dosa:Os02t0561400-01.
dosa:Os02t0561800-01.
dosa:Os02t0561900-00.
dosa:Os11t0649801-00.
osa:4329685.

Organism-specific databases

Gramene

Q9LRB7.

Phylogenomic databases

eggNOG

NOG265447.

HOGENOM

HOG000243710.

K16286.

OMA

LWSFGRQ.

ProtClustDB

CLSN2692836.

Enzyme and pathway databases

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

Q9LRB7.

Family and domain databases

Gene3D

3.30.40.10. 1 hit.

InterPro

IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]

Pfam

PF13639. zf-RING_2. 1 hit.
[Graphical view]

SMART

SM00184. RING. 1 hit.
[Graphical view]

PROSITE

PS00518. ZF_RING_1. False negative.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9LRB7.

Entry information

Entry name

EL5_ORYSJ

Accession

Primary (citable) accession number: Q9LRB7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	October 1, 2000
Last modified:	April 3, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Oryza sativa (rice)

Index of Oryza sativa entries and their corresponding gene designations

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents