P06734 · FCER2_HUMAN
- ProteinLow affinity immunoglobulin epsilon Fc receptor
- GeneFCER2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids321 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Low-affinity receptor for immunoglobulin E (IgE) and CR2/CD21. Has essential roles in the regulation of IgE production and in the differentiation of B cells. On B cells, initiates IgE-dependent antigen uptake and presentation to T cells (PubMed:2167225).
On macrophages, upon IgE binding and antigen cross-linking induces intracellular killing of parasites through activation of L-Arginine-nitric oxide pathway (PubMed:7544003).
On macrophages, upon IgE binding and antigen cross-linking induces intracellular killing of parasites through activation of L-Arginine-nitric oxide pathway (PubMed:7544003).
Miscellaneous
There are two kinds of Fc receptors for IgE, which differ in both structure and function: high affinity receptors on basophils and mast cells and low affinity receptors on lymphocytes and monocytes.
Features
Showing features for site, binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | external side of plasma membrane | |
Cellular Component | extracellular exosome | |
Cellular Component | plasma membrane | |
Molecular Function | carbohydrate binding | |
Molecular Function | IgE binding | |
Molecular Function | integrin binding | |
Molecular Function | low-affinity IgE receptor activity | |
Molecular Function | metal ion binding | |
Molecular Function | protease binding | |
Biological Process | B cell antigen processing and presentation | |
Biological Process | Fc receptor-mediated immune complex endocytosis | |
Biological Process | immune response | |
Biological Process | macrophage activation | |
Biological Process | positive regulation of humoral immune response mediated by circulating immunoglobulin | |
Biological Process | positive regulation of killing of cells of another organism | |
Biological Process | positive regulation of nitric-oxide synthase activity | |
Biological Process | positive regulation of nitric-oxide synthase biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameLow affinity immunoglobulin epsilon Fc receptor
- Alternative names
- Cleaved into 2 chains
- CD Antigen Name
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP06734
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type II membrane protein
Cell membrane ; Lipid-anchor
Note: Also exists as a soluble excreted form, sCD23.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-21 | Cytoplasmic | ||||
Sequence: MEEGQYSEIEELPRRRCCRRG | ||||||
Transmembrane | 22-47 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: TQIVLLGLVTAALWAGLLTLLLLWHW | ||||||
Topological domain | 48-321 | Extracellular | ||||
Sequence: DTTQSLKQLEERAARNVSQVSKNLESHHGDQMAQKSQSTQISQELEELRAEQQRLKSQDLELSWNLNGLQADLSSFKSQELNERNEASDLLERLREEVTKLRMELQVSSGFVCNTCPEKWINFQRKCYYFGKGTKQWVHARYACDDMEGQLVSIHSPEEQDFLTKHASHTGSWIGLRNLDLKGEFIWVDGSHVDYSNWAPGEPTSRSQGEDCVMMRGSGRWNDAFCDRKLGAWVCDRLATCTPPASEGSAESMGPDSRPDPDGRLPTPSAPLHS |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_035387 | 62 | in dbSNP:rs2228137 | |||
Sequence: R → W | ||||||
Natural variant | VAR_035388 | 284 | in dbSNP:rs8102872 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_069800 | 316 | ||||
Sequence: S → F |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 492 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, lipidation, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000017391 | 1-321 | Low affinity immunoglobulin epsilon Fc receptor membrane-bound form | |||
Sequence: MEEGQYSEIEELPRRRCCRRGTQIVLLGLVTAALWAGLLTLLLLWHWDTTQSLKQLEERAARNVSQVSKNLESHHGDQMAQKSQSTQISQELEELRAEQQRLKSQDLELSWNLNGLQADLSSFKSQELNERNEASDLLERLREEVTKLRMELQVSSGFVCNTCPEKWINFQRKCYYFGKGTKQWVHARYACDDMEGQLVSIHSPEEQDFLTKHASHTGSWIGLRNLDLKGEFIWVDGSHVDYSNWAPGEPTSRSQGEDCVMMRGSGRWNDAFCDRKLGAWVCDRLATCTPPASEGSAESMGPDSRPDPDGRLPTPSAPLHS | ||||||
Lipidation | 17 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Lipidation | 18 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Glycosylation | 63 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Chain | PRO_0000017392 | 150-321 | Low affinity immunoglobulin epsilon Fc receptor soluble form | |||
Sequence: MELQVSSGFVCNTCPEKWINFQRKCYYFGKGTKQWVHARYACDDMEGQLVSIHSPEEQDFLTKHASHTGSWIGLRNLDLKGEFIWVDGSHVDYSNWAPGEPTSRSQGEDCVMMRGSGRWNDAFCDRKLGAWVCDRLATCTPPASEGSAESMGPDSRPDPDGRLPTPSAPLHS | ||||||
Disulfide bond | 160↔288 | |||||
Sequence: CNTCPEKWINFQRKCYYFGKGTKQWVHARYACDDMEGQLVSIHSPEEQDFLTKHASHTGSWIGLRNLDLKGEFIWVDGSHVDYSNWAPGEPTSRSQGEDCVMMRGSGRWNDAFCDRKLGAWVCDRLATC | ||||||
Disulfide bond | 163↔174 | |||||
Sequence: CPEKWINFQRKC | ||||||
Disulfide bond | 191↔282 | |||||
Sequence: CDDMEGQLVSIHSPEEQDFLTKHASHTGSWIGLRNLDLKGEFIWVDGSHVDYSNWAPGEPTSRSQGEDCVMMRGSGRWNDAFCDRKLGAWVC | ||||||
Disulfide bond | 259↔273 | |||||
Sequence: CVMMRGSGRWNDAFC | ||||||
Glycosylation | 296 | O-linked (Xyl...) (chondroitin sulfate) serine | ||||
Sequence: S |
Post-translational modification
N- and O-glycosylated.
The secreted form sCD23 is produced by ADAM10-mediated ectodomain shedding.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Detected in urine (at protein level).
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homotrimer. Interacts (via C-type lectin domain) with IGHE (via CH3 region); this interaction regulates IgE homeostasis. Interacts (via the C-terminus) with CR2/CD21 (via Sushi domain 1 and 2) (PubMed:1386409, PubMed:16172256).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P06734 | ATF7 P17544 | 3 | EBI-10199985, EBI-765623 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, repeat, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 66-85 | Disordered | ||||
Sequence: QVSKNLESHHGDQMAQKSQS | ||||||
Repeat | 69-89 | |||||
Sequence: KNLESHHGDQMAQKSQSTQIS | ||||||
Repeat | 90-110 | |||||
Sequence: QELEELRAEQQRLKSQDLELS | ||||||
Repeat | 111-131 | |||||
Sequence: WNLNGLQADLSSFKSQELNER | ||||||
Domain | 162-284 | C-type lectin | ||||
Sequence: TCPEKWINFQRKCYYFGKGTKQWVHARYACDDMEGQLVSIHSPEEQDFLTKHASHTGSWIGLRNLDLKGEFIWVDGSHVDYSNWAPGEPTSRSQGEDCVMMRGSGRWNDAFCDRKLGAWVCDR | ||||||
Region | 290-321 | Disordered | ||||
Sequence: PPASEGSAESMGPDSRPDPDGRLPTPSAPLHS |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length321
- Mass (Da)36,469
- Last updated1988-01-01 v1
- ChecksumF86708C0E6515B87
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 269 | in Ref. 3; CAA28465 | ||||
Sequence: N → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M15059 EMBL· GenBank· DDBJ | AAA52434.1 EMBL· GenBank· DDBJ | mRNA | ||
M14766 EMBL· GenBank· DDBJ | AAA52435.1 EMBL· GenBank· DDBJ | mRNA | ||
X04772 EMBL· GenBank· DDBJ | CAA28465.1 EMBL· GenBank· DDBJ | mRNA | ||
AC008763 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC014108 EMBL· GenBank· DDBJ | AAH14108.1 EMBL· GenBank· DDBJ | mRNA | ||
BC062591 EMBL· GenBank· DDBJ | AAH62591.1 EMBL· GenBank· DDBJ | mRNA | ||
M23562 EMBL· GenBank· DDBJ | AAA52433.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. |