P15133 · E3RDA_ADE02
- ProteinPre-early 3 receptor internalization and degradation alpha protein
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Prevents infected cell apoptosis induced by the host immune system. Acts by down-regulating a number of cell surface receptors in the tumor necrosis factor (TNF) receptor superfamily, namely FAS, TNFRSF10A/TRAIL receptor 1, and TNFRSF10B/TRAIL receptor 2. Down-regulation of these death receptors protects adenovirus-infected cells from apoptosis induced by the death receptor ligands Fas ligand and TRAIL. RID complex also down-regulates certain tyrosine kinase cell surface receptors, especially the epidermal growth factor receptor (EGFR). RID-mediated Fas and EGFR down-regulation occurs via endocytosis of the receptors into endosomes followed by transport to and degradation within lysosomes.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 22-23 | Cleavage; by host signal peptidase | ||||
Sequence: AA |
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 | host cell endoplasmic reticulum | |
Cellular Component | host cell membrane | |
Cellular Component | membrane |
Names & Taxonomy
Protein names
- Recommended namePre-early 3 receptor internalization and degradation alpha protein
- Short namesPre-E3-RID-alpha protein
- Cleaved into 1 chains
Organism names
- Taxonomic lineageViruses > Varidnaviria > Bamfordvirae > Preplasmiviricota > Tectiliviricetes > Rowavirales > Adenoviridae > Mastadenovirus > Human mastadenovirus C
- Virus hosts
Accessions
- Primary accessionP15133
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Pre-early 3 receptor internalization and degradation alpha protein
Host membrane ; Multi-pass membrane protein
Early 3 receptor internalization and degradation alpha protein
Host membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-4 | Cytoplasmic | ||||
Sequence: MIPR | ||||||
Transmembrane | 5-25 | Helical; Name=TM1 | ||||
Sequence: VLILLTLVALFCACSTLAAVA | ||||||
Topological domain | 26-34 | Lumenal | ||||
Sequence: HIEVDCIPP | ||||||
Transmembrane | 35-60 | Helical | ||||
Sequence: FTVYLLYGFVTLILICSLVTVVIAFI | ||||||
Topological domain | 61-91 | Cytoplasmic | ||||
Sequence: QFIDWVCVRIAYLRHHPQYRDRTIADLLRIL |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 31 | Complete loss of disulfide bonding. | ||||
Sequence: C → S |
PTM/Processing
Features
Showing features for propeptide, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Propeptide | PRO_0000421690 | 1-22 | Signal peptide | |||
Sequence: MIPRVLILLTLVALFCACSTLA | ||||||
Chain | PRO_0000421689 | 1-91 | Pre-early 3 receptor internalization and degradation alpha protein | |||
Sequence: MIPRVLILLTLVALFCACSTLAAVAHIEVDCIPPFTVYLLYGFVTLILICSLVTVVIAFIQFIDWVCVRIAYLRHHPQYRDRTIADLLRIL | ||||||
Chain | PRO_0000036470 | 23-91 | Early 3 receptor internalization and degradation alpha protein | |||
Sequence: AVAHIEVDCIPPFTVYLLYGFVTLILICSLVTVVIAFIQFIDWVCVRIAYLRHHPQYRDRTIADLLRIL | ||||||
Disulfide bond | 31 | Interchain (with C-31 in Early 3 receptor internalization and degradation alpha protein) | ||||
Sequence: C |
Post-translational modification
The signal peptide is only cleaved partially by host signal peptidase. This results in two forms of the protein, one uncleaved with two transmembrane regions, and one cleaved with one transmembrane region (PubMed:1531278).
Keywords
- PTM
Expression
Keywords
- Developmental stage
Interaction
Subunit
Homodimer with only one chain cleaved by signal peptidase. Interacts with E3 RID-beta and E3 CR1-alpha.
Family & Domains
Sequence similarities
Belongs to the adenoviridae E3-RID-alpha family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length91
- Mass (Da)10,375
- Last updated1990-04-01 v1
- Checksum9328F70C6BBCE9EE
Keywords
- Technical term