ARI11_CAEEL
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 03-AUG-2022, entry version 147.
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}.
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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 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; 469819at2759; -.
DR PhylomeDB; O01965; -.
DR Reactome; R-CEL-1169408; ISG15 antiviral mechanism.
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; 3.30.40.10; -; 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; PTHR11685; 1.
DR Pfam; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 2.
DR SMART; SM00647; IBR; 2.
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
