ARI15_ARATH
ID ARI15_ARATH Reviewed; 452 AA.
AC Q84RQ8; Q9FFN8;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Probable E3 ubiquitin-protein ligase ARI15;
DE EC=2.3.2.31 {ECO:0000250|UniProtKB:Q9Y4X5};
DE AltName: Full=ARIADNE-like protein ARI15;
DE AltName: Full=Protein ariadne homolog 15;
DE AltName: Full=RING-type E3 ubiquitin transferase ARI15 {ECO:0000305};
GN Name=ARI15; OrderedLocusNames=At5g63760; ORFNames=MBK5.24;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, NOMENCLATURE, AND
RP GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=12529512; DOI=10.1104/pp.012781;
RA Mladek C., Guger K., Hauser M.-T.;
RT "Identification and characterization of the ARIADNE gene family in
RT Arabidopsis. A group of putative E3 ligases.";
RL Plant Physiol. 131:27-40(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=12446796; DOI=10.1093/oxfordjournals.molbev.a004029;
RA Marin I., Ferrus A.;
RT "Comparative genomics of the RBR family, including the Parkinson's disease-
RT related gene parkin and the genes of the ariadne subfamily.";
RL Mol. Biol. Evol. 19:2039-2050(2002).
CC -!- FUNCTION: Might act as an E3 ubiquitin-protein ligase, or as part of E3
CC complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating
CC enzymes and then transfers it to substrates. {ECO:0000250,
CC ECO:0000269|PubMed:12446796}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000250|UniProtKB:Q9Y4X5};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 4 Zn(2+) ions per subunit. {ECO:0000305};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12529512}.
CC -!- DOMAIN: Members of the RBR family are atypical E3 ligases. They
CC interact with the E2 conjugating enzyme UBE2L3 and function like HECT-
CC type E3 enzymes: they bind E2s via the first RING-type zinc finger, but
CC require an obligate trans-thiolation step during the ubiquitin
CC transfer, requiring a conserved active site Cys residue in the second
CC RING-type zinc finger. The active site probably forms a thioester
CC intermediate with ubiquitin taken from the active-site cysteine of the
CC E2 before ultimately transferring it to a Lys residue on the substrate.
CC {ECO:0000250|UniProtKB:Q9Y4X5}.
CC -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Lacks two Cys residues in the RING-type zinc finger domain 2
CC that are conserved features of the family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10469.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ510218; CAD52897.1; -; Genomic_DNA.
DR EMBL; AB005234; BAB10469.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97793.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97794.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70851.1; -; Genomic_DNA.
DR EMBL; BT022004; AAY25416.1; -; mRNA.
DR EMBL; BT029215; ABJ17150.1; -; mRNA.
DR RefSeq; NP_001332429.1; NM_001345608.1.
DR RefSeq; NP_201181.2; NM_125771.3.
DR RefSeq; NP_974987.1; NM_203258.2.
DR AlphaFoldDB; Q84RQ8; -.
DR SMR; Q84RQ8; -.
DR STRING; 3702.AT5G63760.2; -.
DR PaxDb; Q84RQ8; -.
DR PRIDE; Q84RQ8; -.
DR ProteomicsDB; 245189; -.
DR EnsemblPlants; AT5G63760.1; AT5G63760.1; AT5G63760.
DR EnsemblPlants; AT5G63760.2; AT5G63760.2; AT5G63760.
DR EnsemblPlants; AT5G63760.3; AT5G63760.3; AT5G63760.
DR GeneID; 836496; -.
DR Gramene; AT5G63760.1; AT5G63760.1; AT5G63760.
DR Gramene; AT5G63760.2; AT5G63760.2; AT5G63760.
DR Gramene; AT5G63760.3; AT5G63760.3; AT5G63760.
DR KEGG; ath:AT5G63760; -.
DR Araport; AT5G63760; -.
DR TAIR; locus:2160584; AT5G63760.
DR eggNOG; KOG1815; Eukaryota.
DR HOGENOM; CLU_009823_3_2_1; -.
DR InParanoid; Q84RQ8; -.
DR OMA; QTVESHN; -.
DR OrthoDB; 469819at2759; -.
DR PhylomeDB; Q84RQ8; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q84RQ8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q84RQ8; baseline and differential.
DR Genevisible; Q84RQ8; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; PTHR11685; 1.
DR Pfam; PF01485; IBR; 1.
DR SMART; SM00647; IBR; 2.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Metal-binding; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..452
FT /note="Probable E3 ubiquitin-protein ligase ARI15"
FT /id="PRO_0000356208"
FT ZN_FING 26..88
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 106..174
FT /note="IBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 208..239
FT /note="RING-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 414..445
FT /note="RanBP2-type"
FT REGION 22..256
FT /note="TRIAD supradomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
SQ SEQUENCE 452 AA; 51767 MW; D2F3A23CC5DDEA20 CRC64;
MEKLMTESGL KPVVIDSNQD LSRVYCGICS NIGDDDYDGD AVVVDGDLIS TPFCSHKFCK
ACWSKYLKKN FFSVEKNHTA ISCPDRDCRA AVGPETVEKL TVRDQAMYEL YILKSYREKY
LGWKLKLCPA RGCNYVIEFH LASEDEEHSL NIVCLCGHIF CWRCMLESHR PVTCNNASDW
LSRDLEKLIE EVDKPSTVSW IDANTKPCPH CFIPVEIDGE RPWAQFLTCV CSGRFCWKCF
RSPETHGTSG SCLAPARSSN VGFNHWNRAK PGISCLDLWN ASQVNLVNAK YELEAFEESI
IKKPSDLKEQ DVKVLREGLM LIVQCRQFLK WSCAYDYIHT EYDMAKREYL RFLQQNASGI
VHSFSQSIKE ETEAKELTCG KLLSETTNIG NFFYHFIKTL REGLPEVQAE SYDNYGGPYW
LCDRCTYGNS WFQRACKMCC DPTASKMDEL SD
