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P06734 (FCER2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 161. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Low affinity immunoglobulin epsilon Fc receptor
Alternative name(s):
BLAST-2
C-type lectin domain family 4 member J
Fc-epsilon-RII
Immunoglobulin E-binding factor
Lymphocyte IgE receptor
CD_antigen=CD23
Gene names
Name:FCER2
Synonyms:CD23A, CLEC4J, FCE2, IGEBF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length321 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 (it is a B-cell-specific antigen).

Subunit structure

Homotrimer. Ref.12

Subcellular location

Cell membrane; Single-pass type II membrane protein. Cell membrane; Lipid-anchor. Secreted. Note: Also exists as a soluble excreted form, sCD23. Ref.8 Ref.9

Post-translational modification

N- and O-glycosylated.

The secreted form sCD23 is produced by ADAM10-mediated ectodomain shedding.

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.

Sequence similarities

Contains 1 C-type lectin domain.

Sequence caution

The sequence AAA52433.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityPolymorphism
   DomainRepeat
Signal-anchor
Transmembrane
Transmembrane helix
   LigandCalcium
IgE-binding protein
Lectin
Metal-binding
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processNotch signaling pathway

Traceable author statement. Source: Reactome

positive regulation of humoral immune response mediated by circulating immunoglobulin

Inferred from electronic annotation. Source: Ensembl

positive regulation of killing of cells of other organism

Inferred from direct assay PubMed 7544003. Source: BHF-UCL

positive regulation of nitric-oxide synthase activity

Inferred from direct assay PubMed 7544003. Source: BHF-UCL

positive regulation of nitric-oxide synthase biosynthetic process

Inferred from direct assay PubMed 7544003. Source: BHF-UCL

   Cellular_componentexternal side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

integral component of plasma membrane

Traceable author statement PubMed 2529542. Source: ProtInc

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

integrin binding

Traceable author statement PubMed 2529542. Source: ProtInc

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 321321Low affinity immunoglobulin epsilon Fc receptor membrane-bound form
PRO_0000017391
Chain150 – 321172Low affinity immunoglobulin epsilon Fc receptor soluble form
PRO_0000017392

Regions

Topological domain1 – 2121Cytoplasmic Potential
Transmembrane22 – 4726Helical; Signal-anchor for type II membrane protein; Potential
Topological domain48 – 321274Extracellular Potential
Repeat69 – 8921
Repeat90 – 11021
Repeat111 – 13121
Domain162 – 284123C-type lectin

Sites

Metal binding2491Calcium
Metal binding2511Calcium
Metal binding2691Calcium
Metal binding2701Calcium
Site149 – 1502Cleavage

Amino acid modifications

Lipidation171S-palmitoyl cysteine Ref.9
Lipidation181S-palmitoyl cysteine Ref.9
Glycosylation631N-linked (GlcNAc...) Potential
Disulfide bond160 ↔ 288 Ref.7 Ref.12 Ref.13
Disulfide bond163 ↔ 174 Ref.7 Ref.12 Ref.13
Disulfide bond191 ↔ 282 Ref.7 Ref.12 Ref.13
Disulfide bond259 ↔ 273 Ref.7 Ref.12 Ref.13

Natural variations

Natural variant621R → W.
Corresponds to variant rs2228137 [ dbSNP | Ensembl ].
VAR_035387
Natural variant2841R → Q.
Corresponds to variant rs8102872 [ dbSNP | Ensembl ].
VAR_035388
Natural variant3161S → F. Ref.14
VAR_069800

Experimental info

Sequence conflict2691N → T in CAA28465. Ref.3

Secondary structure

.................................... 321
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06734 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: F86708C0E6515B87

FASTA32136,469
        10         20         30         40         50         60 
MEEGQYSEIE ELPRRRCCRR GTQIVLLGLV TAALWAGLLT LLLLWHWDTT QSLKQLEERA 

        70         80         90        100        110        120 
ARNVSQVSKN LESHHGDQMA QKSQSTQISQ ELEELRAEQQ RLKSQDLELS WNLNGLQADL 

       130        140        150        160        170        180 
SSFKSQELNE RNEASDLLER LREEVTKLRM ELQVSSGFVC NTCPEKWINF QRKCYYFGKG 

       190        200        210        220        230        240 
TKQWVHARYA CDDMEGQLVS IHSPEEQDFL TKHASHTGSW IGLRNLDLKG EFIWVDGSHV 

       250        260        270        280        290        300 
DYSNWAPGEP TSRSQGEDCV MMRGSGRWND AFCDRKLGAW VCDRLATCTP PASEGSAESM 

       310        320 
GPDSRPDPDG RLPTPSAPLH S 

« Hide

References

« Hide 'large scale' references
[1]"Human lymphocyte Fc receptor for IgE: sequence homology of its cloned cDNA with animal lectins."
Ikuta K., Takami M., Kim C.W., Honjo T., Miyoshi T., Tagaya Y., Kawabe T., Yodoi J.
Proc. Natl. Acad. Sci. U.S.A. 84:819-823(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular structure of human lymphocyte receptor for immunoglobulin E."
Kikutani H., Inui S., Sato R., Barsumian E.L., Owaki H., Yamasaki K., Kaisho T., Uchibayashi N., Hardy R.R., Hirano T., Tsunasawa S., Sakiyama F., Suemura M., Kishimoto T.
Cell 47:657-665(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Cloning and expression of the cDNA coding for a human lymphocyte IgE receptor."
Luedin C., Hofstetter H., Sarfati M., Levy C.A., Suter U., Alaimo D., Kilchherr E., Frost H., Delespesse G.
EMBO J. 6:109-114(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: B-cell and Blood.
[6]"Two species of human Fc epsilon receptor II (Fc epsilon RII/CD23): tissue-specific and IL-4-specific regulation of gene expression."
Yokota A., Kikutani H., Tanaka T., Sato R., Barsumian E.L., Suemura M., Kishimoto T.
Cell 55:611-618(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"Partial characterization of natural and recombinant human soluble CD23."
Rose K., Turcatti G., Graber P., Pochon S., Regamey P.-O., Jansen K.U., Magnenat E., Aubonney N., Bonnefoy J.-Y.
Biochem. J. 286:819-824(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS.
[8]"The low affinity IgE receptor (CD23) is cleaved by the metalloproteinase ADAM10."
Lemieux G.A., Blumenkron F., Yeung N., Zhou P., Williams J., Grammer A.C., Petrovich R., Lipsky P.E., Moss M.L., Werb Z.
J. Biol. Chem. 282:14836-14844(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE BY ADAM10.
[9]"Proteomic analysis of S-acylated proteins in human B cells reveals palmitoylation of the immune regulators CD20 and CD23."
Ivaldi C., Martin B.R., Kieffer-Jaquinod S., Chapel A., Levade T., Garin J., Journet A.
PLoS ONE 7:E37187-E37187(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-17 AND CYS-18, SUBCELLULAR LOCATION.
Tissue: B-cell.
[10]"Modeling of the lectin-homology domains of the human and murine low-affinity Fc epsilon receptor (Fc epsilon RII/CD23)."
Padlan E.A., Helm B.A.
Receptor 3:325-341(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF LECTIN DOMAIN.
[11]"Structure-based modeling of the ligand binding domain of the human cell surface receptor CD23 and comparison of two independently derived molecular models."
Bajorath J., Aruffo A.
Protein Sci. 5:240-247(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF 173-285.
[12]"The structure of human CD23 and its interactions with IgE and CD21."
Hibbert R.G., Teriete P., Grundy G.J., Beavil R.L., Reljic R., Holers V.M., Hannan J.P., Sutton B.J., Gould H.J., McDonnell J.M.
J. Exp. Med. 202:751-760(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 156-298, DISULFIDE BONDS, SUBUNIT.
[13]"Structural changes in the lectin domain of CD23, the low-affinity IgE receptor, upon calcium binding."
Wurzburg B.A., Tarchevskaya S.S., Jardetzky T.S.
Structure 14:1049-1058(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 150-321 ALONE AND IN COMPLEX WITH CALCIUM, DISULFIDE BONDS.
[14]"Mutations in the autoregulatory domain of beta-tubulin 4a cause hereditary dystonia."
Hersheson J., Mencacci N.E., Davis M., Macdonald N., Trabzuni D., Ryten M., Pittman A., Paudel R., Kara E., Fawcett K., Plagnol V., Bhatia K.P., Medlar A.J., Stanescu H.C., Hardy J., Kleta R., Wood N.W., Houlden H.
Ann. Neurol. 73:546-553(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PHE-316.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M15059 mRNA. Translation: AAA52434.1.
M14766 mRNA. Translation: AAA52435.1.
X04772 mRNA. Translation: CAA28465.1.
AC008763 Genomic DNA. No translation available.
BC014108 mRNA. Translation: AAH14108.1.
BC062591 mRNA. Translation: AAH62591.1.
M23562 Genomic DNA. Translation: AAA52433.1. Sequence problems.
CCDSCCDS12184.1.
PIRLNHUER. A26067.
RefSeqNP_001193948.2. NM_001207019.2.
NP_001207429.1. NM_001220500.1.
NP_001993.2. NM_002002.4.
XP_005272519.1. XM_005272462.2.
XP_006722750.1. XM_006722687.1.
UniGeneHs.465778.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HLImodel-A173-285[»]
1KJEmodel-A173-285[»]
1T8CNMR-A156-298[»]
1T8DNMR-A156-298[»]
2H2RX-ray1.50A/B150-321[»]
2H2TX-ray1.30B150-321[»]
4EZMX-ray3.10G/H/I/J/K/L156-298[»]
4G96X-ray2.25A/B/C/D156-298[»]
4G9AX-ray2.00A/B/C/D156-298[»]
4GI0X-ray2.27A/B/C156-298[»]
4GJ0X-ray1.95A/B/C/D156-298[»]
4GJXX-ray2.80A/B/C/D/E/F/G/H156-298[»]
4GK1X-ray2.24A/B/C/D/E/F/G156-298[»]
4GKOX-ray3.30G/H/I/J/K/L156-298[»]
4J6JX-ray1.90A/B/C/D156-298[»]
4J6KX-ray2.30A/B/C/D/E/F/G/H156-298[»]
4J6LX-ray3.15A/B/C/D/E/F/G/H156-298[»]
4J6MX-ray2.48A/B/C/D/E/F/G/H156-298[»]
4J6NX-ray2.85A/B156-298[»]
4J6PX-ray1.90A/B/C/D156-298[»]
4J6QX-ray2.54A156-298[»]
4KI1X-ray3.20E/F/G/H156-298[»]
ProteinModelPortalP06734.
SMRP06734. Positions 134-291.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108502. 3 interactions.
STRING9606.ENSP00000264072.

Chemistry

BindingDBP06734.
ChEMBLCHEMBL2940.

PTM databases

PhosphoSiteP06734.

Polymorphism databases

DMDM119862.

Proteomic databases

MaxQBP06734.
PaxDbP06734.
PRIDEP06734.

Protocols and materials databases

DNASU2208.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000346664; ENSP00000264072; ENSG00000104921.
ENST00000597921; ENSP00000471974; ENSG00000104921.
GeneID2208.
KEGGhsa:2208.
UCSCuc002mhm.2. human.

Organism-specific databases

CTD2208.
GeneCardsGC19M007754.
HGNCHGNC:3612. FCER2.
HPACAB002624.
HPA008928.
MIM151445. gene.
neXtProtNX_P06734.
PharmGKBPA28058.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG235454.
HOGENOMHOG000089951.
HOVERGENHBG051599.
InParanoidP06734.
KOK06468.
OMAKCYYFGE.
OrthoDBEOG7FV3QQ.
PhylomeDBP06734.
TreeFamTF333341.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressP06734.
BgeeP06734.
CleanExHS_FCER2.
GenevestigatorP06734.

Family and domain databases

Gene3D3.10.100.10. 1 hit.
InterProIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMSSF56436. SSF56436. 1 hit.
PROSITEPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP06734.
GeneWikiCD23.
GenomeRNAi2208.
NextBio8943.
PMAP-CutDBP06734.
PROP06734.
SOURCESearch...

Entry information

Entry nameFCER2_HUMAN
AccessionPrimary (citable) accession number: P06734
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: July 9, 2014
This is version 161 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries