ID ARI11_CAEEL Reviewed; 494 AA. AC O01965; DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 3. DT 22-FEB-2023, entry version 149. DE RecName: Full=E3 ubiquitin-protein ligase ari-1.1 {ECO:0000305}; DE EC=2.3.2.31 {ECO:0000250|UniProtKB:Q9Y4X5}; GN Name=ari-1.1 {ECO:0000312|WormBase:C27A12.8}; GN ORFNames=C27A12.8 {ECO:0000312|WormBase:C27A12.8}; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940}; RN [1] {ECO:0000312|Proteomes:UP000001940} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940}; 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). RN [2] {ECO:0000305} RP FUNCTION, INTERACTION WITH UBC-18, SUBCELLULAR LOCATION, DEVELOPMENTAL RP STAGE, AND DISRUPTION PHENOTYPE. RX PubMed=16457801; DOI=10.1016/j.ydbio.2005.11.045; RA Qiu X., Fay D.S.; RT "ARI-1, an RBR family ubiquitin-ligase, functions with UBC-18 to regulate RT pharyngeal development in C. elegans."; RL Dev. Biol. 291:239-252(2006). RN [3] RP FUNCTION. RX PubMed=19521497; DOI=10.1371/journal.pgen.1000510; RA Mani K., Fay D.S.; RT "A mechanistic basis for the coordinated regulation of pharyngeal RT morphogenesis in Caenorhabditis elegans by LIN-35/Rb and UBC-18-ARI-1."; RL PLoS Genet. 5:E1000510-E1000510(2009). CC -!- FUNCTION: E3 ubiquitin-protein transferase, which catalyzes CC ubiquitination of target proteins together with ubiquitin-conjugating CC enzyme E2 ubc-18 (By similarity). Acts with ubc-18 to regulate CC pharyngeal development (PubMed:16457801, PubMed:19521497). CC {ECO:0000250|UniProtKB:Q9Y4X5, ECO:0000269|PubMed:16457801, CC ECO:0000269|PubMed:19521497}. 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 -!- ACTIVITY REGULATION: Autoinhibited by the ariadne domain, which masks CC the second RING-type zinc finger that contains the active site and CC inhibits the E3 activity. {ECO:0000250|UniProtKB:Q9Y4X5}. CC -!- SUBUNIT: Interacts with ubiquitin-conjugating enzyme E2 ubc-18. CC {ECO:0000269|PubMed:16457801}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16457801}. Cytoplasm CC {ECO:0000269|PubMed:16457801}. CC -!- DEVELOPMENTAL STAGE: Expression is dynamic during early embryonic CC development, with ubiquitous somatic expression occurring between the CC 50- and 200-cell stage (PubMed:16457801). By the late proliferative CC phase of embryogenesis, expression is reduced, but maintained at high CC levels in muscle precursors (PubMed:16457801). Later in embryogenesis, CC moderate expression occurs in the lateral ectoderm (PubMed:16457801). CC Pharyngeal expression is very low at both the comma and 1.5-fold CC embryonic stages (PubMed:16457801). Expression is highest in muscle and CC neuronal cells in larvae and adults, including many of the amphid CC neurons that are proximal to the posterior bulb of the pharynx CC (PubMed:16457801). Consistent expression in cells of the somatic gonad CC including distal tip, sheath, and spermathecal cells, as well as in CC vulval cells undergoing morphogenesis (PubMed:16457801). Neuronal CC expression in the midbody includes the CAN, HSN, and ALM cells; neurons CC of the ventral and dorsal cords; and a number of posterior deirid CC neurons (PubMed:16457801). Expressed in all pairs of coelomocytes CC (PubMed:16457801). {ECO:0000269|PubMed:16457801}. CC -!- DOMAIN: Members of the RBR family are atypical E3 ligases. They CC interact with an E2 conjugating enzyme and function like HECT-type E3 CC enzymes: they bind E2s via the first RING-type zinc finger, but require CC an obligate trans-thiolation step during the ubiquitin transfer, CC requiring a conserved active site Cys residue in the second RING-type CC zinc finger. The active site probably forms a thioester intermediate CC with ubiquitin taken from the active-site cysteine of the E2 before CC ultimately transferring it to a Lys residue on the substrate. CC {ECO:0000250|UniProtKB:Q9Y4X5}. CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown on a pha-1 or on a lin- CC 35;ubc-18 mutant background produces a high percentage of animals with CC the Pun (pharyngeal unattached) phenotype, whereby the pharynx fails to CC elongate and form an attachment to the anterior alimentary opening or CC buccal cavity. {ECO:0000269|PubMed:16457801}. CC -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX284601; CCD61206.1; -; Genomic_DNA. DR PIR; H87793; H87793. DR RefSeq; NP_491749.2; NM_059348.5. DR AlphaFoldDB; O01965; -. DR SMR; O01965; -. DR IntAct; O01965; 1. DR STRING; 6239.C27A12.8.1; -. DR EPD; O01965; -. DR PaxDb; O01965; -. DR PeptideAtlas; O01965; -. DR EnsemblMetazoa; C27A12.8.1; C27A12.8.1; WBGene00016158. DR GeneID; 172284; -. DR KEGG; cel:CELE_C27A12.8; -. DR UCSC; C27A12.8.1; c. elegans. DR AGR; WB:WBGene00016158; -. DR CTD; 172284; -. DR WormBase; C27A12.8; CE29680; WBGene00016158; ari-1.1. DR eggNOG; KOG1815; Eukaryota. DR GeneTree; ENSGT00940000155744; -. DR HOGENOM; CLU_009823_4_2_1; -. DR InParanoid; O01965; -. DR OMA; CAAHACD; -. DR OrthoDB; 3084186at2759; -. DR PhylomeDB; O01965; -. DR Reactome; R-CEL-1169408; ISG15 antiviral mechanism. DR PRO; PR:O01965; -. DR Proteomes; UP000001940; Chromosome I. DR Bgee; WBGene00016158; Expressed in adult organism and 4 other tissues. DR GO; GO:0005737; C:cytoplasm; IDA:WormBase. DR GO; GO:0005634; C:nucleus; IDA:WormBase. 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; 1.20.120.1750; -; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR045840; Ariadne. 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:SF212; E3 UBIQUITIN-PROTEIN LIGASE ARIH1; 1. DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1. DR Pfam; PF19422; Ariadne; 1. DR Pfam; PF01485; IBR; 2. DR SMART; SM00647; IBR; 2. DR SUPFAM; SSF57850; RING/U-box; 3. DR PROSITE; PS51873; TRIAD; 1. PE 1: Evidence at protein level; KW Cytoplasm; Metal-binding; Nucleus; Reference proteome; Repeat; Transferase; KW Ubl conjugation pathway; Zinc; Zinc-finger. FT CHAIN 1..494 FT /note="E3 ubiquitin-protein ligase ari-1.1" FT /id="PRO_0000452644" FT ZN_FING 128..174 FT /note="RING-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT ZN_FING 194..255 FT /note="IBR-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT ZN_FING 282..313 FT /note="RING-type 2; atypical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT REGION 1..52 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 124..331 FT /note="TRIAD supradomain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT REGION 346..494 FT /note="Ariadne domain" FT /evidence="ECO:0000250|UniProtKB:Q9Y4X5" FT COMPBIAS 1..27 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 28..52 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 295 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 128 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 131 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 142 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 144 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="1" 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 169 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 174 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 214 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 219 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 235 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 237 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="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 245 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 282 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 285 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 300 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 310 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="6" 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 320 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 327 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" SQ SEQUENCE 494 AA; 57251 MW; 25BF128B84F805E3 CRC64; MSSDDEINMD DSDSSQGEID DGCMSDDDGI VLESREQNSS DYKDNGEPDN EVLNHDSLEA EMKKTITDVQ AVLQVKTGVC RILLHKYKWN KESLLERFYE HPDTTTFLID AHVIPRRQER LPAGDAECDI CCSLGELSGL SCNHRACTQC WKAYLTNKIA NNAQSEIECM APNCKLLIED EKVMFYITDP TVIATYRKLI VASYVETNRL LKWCPGIDCG KAVRVSHWEP RLVVCSCGSR FCFSCGHDWH EPVNCRLLKL WLKKCNDDSE TSNWINANTK ECPKCMITIE KDGGCNHMTC KNTACRFEFC WMCLGPWEPH GSSWYSCNRF DDSAAKNARD AQEVSRANLQ RYLFYYNRYM GHQQSLRLEG KLYATVKSKM EQMQTLSMSW IEVQFLRKAV DVLSECRRTL MFTYAFAFYL KRDNNAIIFE SNQKDLEMET EQLSGFLERD LDNENLVTLK QKVQDKYRYV EHRRKVLLDH CSEGADQELW VFNE //