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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
 
 
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