ARI2_CAEEL
ID ARI2_CAEEL Reviewed; 482 AA.
AC Q22431;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Potential E3 ubiquitin-protein ligase ariadne-2;
DE EC=2.3.2.31 {ECO:0000250|UniProtKB:Q9Y4X5};
DE AltName: Full=Protein ariadne-2;
DE Short=Ari-2;
DE AltName: Full=RING-type E3 ubiquitin transferase ariadne-2 {ECO:0000305};
GN Name=ari-2 {ECO:0000312|WormBase:T12E12.1};
GN ORFNames=T12E12.1 {ECO:0000312|WormBase:T12E12.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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, such as UBC-2/UBE2L3, and then transfers it to substrates.
CC {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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}.
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DR EMBL; BX284604; CCD70522.1; -; Genomic_DNA.
DR PIR; T29562; T29562.
DR RefSeq; NP_500829.2; NM_068428.5.
DR AlphaFoldDB; Q22431; -.
DR SMR; Q22431; -.
DR BioGRID; 42461; 1.
DR STRING; 6239.T12E12.1; -.
DR iPTMnet; Q22431; -.
DR EPD; Q22431; -.
DR PaxDb; Q22431; -.
DR PeptideAtlas; Q22431; -.
DR EnsemblMetazoa; T12E12.1.1; T12E12.1.1; WBGene00020462.
DR GeneID; 177339; -.
DR KEGG; cel:CELE_T12E12.1; -.
DR UCSC; T12E12.1; c. elegans.
DR CTD; 37542; -.
DR WormBase; T12E12.1; CE31725; WBGene00020462; ari-2.
DR eggNOG; KOG1812; Eukaryota.
DR GeneTree; ENSGT00940000154875; -.
DR HOGENOM; CLU_009823_0_1_1; -.
DR InParanoid; Q22431; -.
DR OMA; ICKVCHT; -.
DR OrthoDB; 469819at2759; -.
DR PhylomeDB; Q22431; -.
DR Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:Q22431; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00020462; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IPR045840; Ariadne.
DR InterPro; IPR031126; Ariadne-2.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; PTHR11685; 1.
DR PANTHER; PTHR11685:SF210; PTHR11685:SF210; 1.
DR Pfam; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 1.
DR SMART; SM00647; IBR; 2.
DR PROSITE; PS51873; TRIAD; 1.
PE 3: Inferred from homology;
KW Coiled coil; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..482
FT /note="Potential E3 ubiquitin-protein ligase ariadne-2"
FT /id="PRO_0000055758"
FT ZN_FING 129..177
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 198..260
FT /note="IBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 287..316
FT /note="RING-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 125..334
FT /note="TRIAD supradomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT COILED 433..459
FT /evidence="ECO:0000255"
FT ACT_SITE 300
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 313
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
SQ SEQUENCE 482 AA; 55808 MW; DFD258B9111E0F6F CRC64;
MDDEDMSCTS GDDYAGYGDE DYYNEADVDA ADDVAVTPTH SEEADYECLS VNQVERVFID
GVNSLVSRIS INEKFARILL QANHWDVDKI ARLVRNDRND FLRKCHIDAK PEPKRKLSST
QSVLAKGYCS VCAMDGYTEL PHLTCGHCFC EHCWKSHVES RLSEGVASRI ECMESECEVY
APSEFVLSII KNSPVIKLKY ERFLLRDMVN SHPHLKFCVG NECPVIIRST EVKPKRVTCM
QCHTSFCVKC GADYHAPTSC ETIKQWMTKC ADDSETANYI SAHTKDCPQC HSCIEKAGGC
NHIQCTRCRH HFCWMCFGDW KSHGSEYYEC SRYKENPSVA AEANHVKARR ALEKYLHYFE
RFENHSKSLK MEEELRDKIR KKIDDKVNEH NGTWIDWQYL HKSVSLLTKC RYTLQYTYPF
AYFLSATPRK NLFEYQQAQL EKEVEELAWA VERADGTARG ALEAHMHRAE HKRQTLLHDF
FF
