Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00269
Entry Name
UniProt Accession
Theoretical PI
5.38
Molecular Weight
36468.78
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Low affinity immunoglobulin epsilon Fc receptor soluble form
Protein Synonyms/Alias
BLAST-2; C-type lectin domain family 4 member J; Fc-epsilon-RII; Immunoglobulin E-binding factor; Lymphocyte IgE receptor; CD23;
Gene Name
FCER2
Gene Synonyms/Alias
CD23A; CLEC4J; FCE2; IGEBF;
Created Date
01-JAN-1988
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
17
Canonical
EELPRRRCCRRGTQI
[1]
S-Palmitoylation
18
Canonical
ELPRRRCCRRGTQIV
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Ivaldi C, Martin BR, Kieffer-Jaquinod S, Chapel A, Levade T, Garin J, Journet A. Proteomic analysis of S-acylated proteins in human B cells revealspalmitoylation of the immune regulators CD20 and CD23. PLoS One.2012;7(5):e37187. doi: 10.1371/journal.pone.0037187. Epub 2012 May 17. PubMedPMID: 22615937; PubMed Central PMCID: PMC3355122.[PMID:22615937]
Functional Description
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 (it is a B-cell-specific antigen).
Sequence Annotation
Topological domain: 1 21 Cytoplasmic.
Transmembrane: 22 47 Helical; Signal-anchor for type IImembrane protein.
Topological domain: 48 321 Extracellular.
Domain: 162 284 C-type lectin.
Metal binding site: 249 249 Calcium.
Metal binding site: 251 251 Calcium.
Metal binding site: 269 269 Calcium.
Metal binding site: 270 270 Calcium.
Functional site: 149 150 Cleavage.
Protein Length
321 AA.
Protein Sequence
(Canonical)
MEEGQYSEIE ELPRRRCCRR GTQIVLLGLV TAALWAGLLT LLLLWHWDTT QSLKQLEERA  60
ARNVSQVSKN LESHHGDQMA QKSQSTQISQ ELEELRAEQQ RLKSQDLELS WNLNGLQADL  120
SSFKSQELNE RNEASDLLER LREEVTKLRM ELQVSSGFVC NTCPEKWINF QRKCYYFGKG  180
TKQWVHARYA CDDMEGQLVS IHSPEEQDFL TKHASHTGSW IGLRNLDLKG EFIWVDGSHV  240
DYSNWAPGEP TSRSQGEDCV MMRGSGRWND AFCDRKLGAW VCDRLATCTP PASEGSAESM  300
GPDSRPDPDG RLPTPSAPLH S                                            321
FASTA
(Canonical)
>LipidDB-9606-00269|P06734
MEEGQYSEIEELPRRRCCRRGTQIVLLGLVTAALWAGLLTLLLLWHWDTTQSLKQLEERA
ARNVSQVSKNLESHHGDQMAQKSQSTQISQELEELRAEQQRLKSQDLELSWNLNGLQADL
SSFKSQELNERNEASDLLERLREEVTKLRMELQVSSGFVCNTCPEKWINFQRKCYYFGKG
TKQWVHARYACDDMEGQLVSIHSPEEQDFLTKHASHTGSWIGLRNLDLKGEFIWVDGSHV
DYSNWAPGEPTSRSQGEDCVMMRGSGRWNDAFCDRKLGAWVCDRLATCTPPASEGSAESM
GPDSRPDPDGRLPTPSAPLHS
Gene Ontology
GO:0009897; C:external side of plasma membrane; IEA:Ensembl
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0005887; C:integral component of plasma membrane; TAS:ProtInc
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW
GO:0005178; F:integrin binding; TAS:ProtInc
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0007219; P:Notch signaling pathway; TAS:Reactome
GO:0002925; P:positive regulation of humoral immune response mediated by circulating immunoglobulin; IEA:Ensembl
GO:0051712; P:positive regulation of killing of cells of other organism; IDA:BHF-UCL
GO:0051000; P:positive regulation of nitric-oxide synthase activity; IDA:BHF-UCL
GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IDA:BHF-UCL
Interpro
InterPro; IPR001304; C-type_lectin
InterPro; IPR016186; C-type_lectin-like
InterPro; IPR018378; C-type_lectin_CS
InterPro; IPR016187; C-type_lectin_fold
Pfam
Pfam; PF00059; Lectin_C;
SMART
SMART; SM00034; CLECT;
PROSITE
PROSITE; PS00615; C_TYPE_LECTIN_1;
PROSITE; PS50041; C_TYPE_LECTIN_2;
PRINTS