O01965 · ARI11_CAEEL
- ProteinE3 ubiquitin-protein ligase ari-1.1
- Geneari-1.1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids494 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
E3 ubiquitin-protein transferase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 ubc-18 (By similarity).
Acts with ubc-18 to regulate pharyngeal development (PubMed:16457801, PubMed:19521497).
Acts with ubc-18 to regulate pharyngeal development (PubMed:16457801, PubMed:19521497).
Catalytic activity
Activity regulation
Autoinhibited by the ariadne domain, which masks the second RING-type zinc finger that contains the active site and inhibits the E3 activity.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 128 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 131 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 142 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 144 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 147 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 150 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 169 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 174 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 214 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 219 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 235 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 237 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 242 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 245 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 250 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 255 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 282 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 285 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Active site | 295 | |||||
Sequence: C | ||||||
Binding site | 300 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 305 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 310 | Zn2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 313 | Zn2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 320 | Zn2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 327 | Zn2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Cellular Component | ubiquitin ligase complex | |
Molecular Function | ubiquitin conjugating enzyme binding | |
Molecular Function | ubiquitin protein ligase activity | |
Molecular Function | zinc ion binding | |
Biological Process | protein polyubiquitination | |
Biological Process | ubiquitin-dependent protein catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase ari-1.1
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis
Accessions
- Primary accessionO01965
Proteomes
Organism-specific databases
Phenotypes & Variants
Disruption phenotype
RNAi-mediated knockdown on a pha-1 or on a lin-35;ubc-18 mutant background produces a high percentage of animals with the Pun (pharyngeal unattached) phenotype, whereby the pharynx fails to elongate and form an attachment to the anterior alimentary opening or buccal cavity.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000452644 | 1-494 | E3 ubiquitin-protein ligase ari-1.1 | |||
Sequence: MSSDDEINMDDSDSSQGEIDDGCMSDDDGIVLESREQNSSDYKDNGEPDNEVLNHDSLEAEMKKTITDVQAVLQVKTGVCRILLHKYKWNKESLLERFYEHPDTTTFLIDAHVIPRRQERLPAGDAECDICCSLGELSGLSCNHRACTQCWKAYLTNKIANNAQSEIECMAPNCKLLIEDEKVMFYITDPTVIATYRKLIVASYVETNRLLKWCPGIDCGKAVRVSHWEPRLVVCSCGSRFCFSCGHDWHEPVNCRLLKLWLKKCNDDSETSNWINANTKECPKCMITIEKDGGCNHMTCKNTACRFEFCWMCLGPWEPHGSSWYSCNRFDDSAAKNARDAQEVSRANLQRYLFYYNRYMGHQQSLRLEGKLYATVKSKMEQMQTLSMSWIEVQFLRKAVDVLSECRRTLMFTYAFAFYLKRDNNAIIFESNQKDLEMETEQLSGFLERDLDNENLVTLKQKVQDKYRYVEHRRKVLLDHCSEGADQELWVFNE |
Proteomic databases
Expression
Developmental stage
Expression is dynamic during early embryonic development, with ubiquitous somatic expression occurring between the 50- and 200-cell stage (PubMed:16457801).
By the late proliferative phase of embryogenesis, expression is reduced, but maintained at high levels in muscle precursors (PubMed:16457801).
Later in embryogenesis, moderate expression occurs in the lateral ectoderm (PubMed:16457801).
Pharyngeal expression is very low at both the comma and 1.5-fold embryonic stages (PubMed:16457801).
Expression is highest in muscle and neuronal cells in larvae and adults, including many of the amphid neurons that are proximal to the posterior bulb of the pharynx (PubMed:16457801).
Consistent expression in cells of the somatic gonad including distal tip, sheath, and spermathecal cells, as well as in vulval cells undergoing morphogenesis (PubMed:16457801).
Neuronal expression in the midbody includes the CAN, HSN, and ALM cells; neurons of the ventral and dorsal cords; and a number of posterior deirid neurons (PubMed:16457801).
Expressed in all pairs of coelomocytes (PubMed:16457801).
By the late proliferative phase of embryogenesis, expression is reduced, but maintained at high levels in muscle precursors (PubMed:16457801).
Later in embryogenesis, moderate expression occurs in the lateral ectoderm (PubMed:16457801).
Pharyngeal expression is very low at both the comma and 1.5-fold embryonic stages (PubMed:16457801).
Expression is highest in muscle and neuronal cells in larvae and adults, including many of the amphid neurons that are proximal to the posterior bulb of the pharynx (PubMed:16457801).
Consistent expression in cells of the somatic gonad including distal tip, sheath, and spermathecal cells, as well as in vulval cells undergoing morphogenesis (PubMed:16457801).
Neuronal expression in the midbody includes the CAN, HSN, and ALM cells; neurons of the ventral and dorsal cords; and a number of posterior deirid neurons (PubMed:16457801).
Expressed in all pairs of coelomocytes (PubMed:16457801).
Gene expression databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-27 | Acidic residues | ||||
Sequence: MSSDDEINMDDSDSSQGEIDDGCMSDD | ||||||
Region | 1-52 | Disordered | ||||
Sequence: MSSDDEINMDDSDSSQGEIDDGCMSDDDGIVLESREQNSSDYKDNGEPDNEV | ||||||
Compositional bias | 28-52 | Basic and acidic residues | ||||
Sequence: DGIVLESREQNSSDYKDNGEPDNEV | ||||||
Region | 124-331 | TRIAD supradomain | ||||
Sequence: GDAECDICCSLGELSGLSCNHRACTQCWKAYLTNKIANNAQSEIECMAPNCKLLIEDEKVMFYITDPTVIATYRKLIVASYVETNRLLKWCPGIDCGKAVRVSHWEPRLVVCSCGSRFCFSCGHDWHEPVNCRLLKLWLKKCNDDSETSNWINANTKECPKCMITIEKDGGCNHMTCKNTACRFEFCWMCLGPWEPHGSSWYSCNRFD | ||||||
Zinc finger | 128-174 | RING-type 1 | ||||
Sequence: CDICCSLGELSGLSCNHRACTQCWKAYLTNKIANNAQSEIECMAPNC | ||||||
Zinc finger | 194-255 | IBR-type | ||||
Sequence: ATYRKLIVASYVETNRLLKWCPGIDCGKAVRVSHWEPRLVVCSCGSRFCFSCGHDWHEPVNC | ||||||
Zinc finger | 282-313 | RING-type 2; atypical | ||||
Sequence: CPKCMITIEKDGGCNHMTCKNTACRFEFCWMC | ||||||
Region | 346-494 | Ariadne domain | ||||
Sequence: RANLQRYLFYYNRYMGHQQSLRLEGKLYATVKSKMEQMQTLSMSWIEVQFLRKAVDVLSECRRTLMFTYAFAFYLKRDNNAIIFESNQKDLEMETEQLSGFLERDLDNENLVTLKQKVQDKYRYVEHRRKVLLDHCSEGADQELWVFNE |
Domain
Members of the RBR family are atypical E3 ligases. They interact with an E2 conjugating enzyme and function like HECT-type E3 enzymes: they bind E2s via the first RING-type zinc finger, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved active site Cys residue in the second RING-type zinc finger. The active site probably forms a thioester intermediate with ubiquitin taken from the active-site cysteine of the E2 before ultimately transferring it to a Lys residue on the substrate.
Sequence similarities
Belongs to the RBR family. Ariadne subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length494
- Mass (Da)57,251
- Last updated2001-12-01 v3
- Checksum25BF128B84F805E3
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-27 | Acidic residues | ||||
Sequence: MSSDDEINMDDSDSSQGEIDDGCMSDD | ||||||
Compositional bias | 28-52 | Basic and acidic residues | ||||
Sequence: DGIVLESREQNSSDYKDNGEPDNEV |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BX284601 EMBL· GenBank· DDBJ | CCD61206.1 EMBL· GenBank· DDBJ | Genomic DNA |