O70352 · CD82_RAT
- ProteinCD82 antigen
- GeneCd82
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids266 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Structural component of specialized membrane microdomains known as tetraspanin-enriched microdomains (TERMs), which act as platforms for receptor clustering and signaling. Participates thereby in diverse biological functions such as cell signal transduction, adhesion, migration and protein trafficking. Acts as a attenuator of EGF signaling, facilitating ligand-induced endocytosis of the receptor and its subsequent desensitization. Mechanistically, modulates ligand-induced ubiquitination and trafficking of EGFR via E3 ligase CBL phosphorylation by PKC. Increases cell-matrix adhesion by regulating the membrane organization of integrin alpha4/ITA4. Modulates adhesion and suppresses cell migration through other integrins such as the alpha6/ITGA6 and beta1/ITGB1. Decreases cell-associated plasminogen activation by interfering with the interaction between urokinase-type plasminogen activator/PLAU and its receptor PLAUR (By similarity).
Associates with CD4 or CD8 and delivers costimulatory signals for the TCR/CD3 pathway. Plays a role in the restrains phagocyte migration but supports macrophage activation (By similarity).
Plays a role in TLR9 trafficking to acidified CpG-containing compartments by controlling interaction between TLR9 and VAMP3 and subsequent myddosome assembly (By similarity).
Inhibits LPS-induced inflammatory response by preventing binding of LPS to TLR4 on the cell surface (By similarity).
Plays a role in the activation of macrophages into anti-inflammatory phenotypes (By similarity).
Independently of Toll-like receptor (TLR) signaling, is recruited to pathogen-containing phagosomes prior to fusion with lysosomes and participates in antigen presentation (By similarity).
Acts also to control angiogenesis and switch angiogenic milieu to quiescent state by binding and sequestering VEGFA and PDGFA to inhibit the signaling they trigger via their respective cell surface receptor (By similarity).
Associates with CD4 or CD8 and delivers costimulatory signals for the TCR/CD3 pathway. Plays a role in the restrains phagocyte migration but supports macrophage activation (By similarity).
Plays a role in TLR9 trafficking to acidified CpG-containing compartments by controlling interaction between TLR9 and VAMP3 and subsequent myddosome assembly (By similarity).
Inhibits LPS-induced inflammatory response by preventing binding of LPS to TLR4 on the cell surface (By similarity).
Plays a role in the activation of macrophages into anti-inflammatory phenotypes (By similarity).
Independently of Toll-like receptor (TLR) signaling, is recruited to pathogen-containing phagosomes prior to fusion with lysosomes and participates in antigen presentation (By similarity).
Acts also to control angiogenesis and switch angiogenic milieu to quiescent state by binding and sequestering VEGFA and PDGFA to inhibit the signaling they trigger via their respective cell surface receptor (By similarity).
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane |
Names & Taxonomy
Protein names
- Recommended nameCD82 antigen
- Alternative names
- CD Antigen Name
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionO70352
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-11 | Cytoplasmic | ||||
Sequence: MGAGCVKVTKY | ||||||
Transmembrane | 12-32 | Helical | ||||
Sequence: FLFLFNLLFFILGAVILGFGV | ||||||
Topological domain | 33-53 | Extracellular | ||||
Sequence: WILADKSSFISVLQTSSSSLQ | ||||||
Transmembrane | 54-72 | Helical | ||||
Sequence: VGAYVFIGVGAITMLMGFL | ||||||
Topological domain | 73-83 | Cytoplasmic | ||||
Sequence: GCIGAVNEVRC | ||||||
Transmembrane | 84-110 | Helical | ||||
Sequence: LLGLYFVFLLLILIAQVTVEVLFYFNA | ||||||
Topological domain | 111-227 | Extracellular | ||||
Sequence: NKLKQEMGNTVMDIIQNYSVNASSSREEAWDYVQAQVKCCGWVSPSNWTRNPVLKNSTKTTYPCSCEKTKEEDNQLIVKKGFCESDNSTASENSPEDWPVHPEGCMEKAQAWLQENF | ||||||
Transmembrane | 228-249 | Helical | ||||
Sequence: GILLGVCAGVAVIELLGLFLSI | ||||||
Topological domain | 250-266 | Cytoplasmic | ||||
Sequence: CLCRYIHSEDYSKVPKY |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, lipidation, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000219228 | 1-266 | CD82 antigen | |||
Sequence: MGAGCVKVTKYFLFLFNLLFFILGAVILGFGVWILADKSSFISVLQTSSSSLQVGAYVFIGVGAITMLMGFLGCIGAVNEVRCLLGLYFVFLLLILIAQVTVEVLFYFNANKLKQEMGNTVMDIIQNYSVNASSSREEAWDYVQAQVKCCGWVSPSNWTRNPVLKNSTKTTYPCSCEKTKEEDNQLIVKKGFCESDNSTASENSPEDWPVHPEGCMEKAQAWLQENFGILLGVCAGVAVIELLGLFLSICLCRYIHSEDYSKVPKY | ||||||
Lipidation | 5 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Lipidation | 74 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Glycosylation | 127 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 131 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 157 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 166 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 197 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Palmitoylated. Palmitoylation contributes to oligomerization and surface expression.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Forms homooligomers. Interacts directly with IGSF8. Interacts with EGFR (By similarity).
Interacts with VEGFA and PDGFA (By similarity).
Interacts with ITGA4. Interacts with ITGA6; this interaction reduces ITGA6 cell surface expression. Interacts with ITGB1. Interacts with TLR4; this interaction inhibits TLR4-mediated signaling pathway (By similarity).
Interacts with TLR9 (By similarity).
Interacts with PLAUR (By similarity).
Interacts with VEGFA and PDGFA (By similarity).
Interacts with ITGA4. Interacts with ITGA6; this interaction reduces ITGA6 cell surface expression. Interacts with ITGB1. Interacts with TLR4; this interaction inhibits TLR4-mediated signaling pathway (By similarity).
Interacts with TLR9 (By similarity).
Interacts with PLAUR (By similarity).
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length266
- Mass (Da)29,487
- Last updated1998-08-01 v1
- ChecksumD6E10AB5AA348474
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6GJM9 | A0A8I6GJM9_RAT | Cd82 | 271 | ||
F7EV99 | F7EV99_RAT | Cd82 | 264 | ||
A6HNI9 | A6HNI9_RAT | Cd82 | 266 | ||
A0A8I5ZP15 | A0A8I5ZP15_RAT | Cd82 | 260 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF049882 EMBL· GenBank· DDBJ | AAC05159.1 EMBL· GenBank· DDBJ | mRNA |