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Protein

Low affinity immunoglobulin epsilon Fc receptor

Gene

FCER2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi249Calcium1 Publication1
Metal bindingi251Calcium1 Publication1
Metal bindingi269Calcium1 Publication1
Metal bindingi270Calcium1 Publication1

GO - Molecular functioni

  • carbohydrate binding Source: UniProtKB-KW
  • integrin binding Source: ProtInc
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Ligandi

Calcium, IgE-binding protein, Lectin, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000104921-MONOMER.
ReactomeiR-HSA-2197563. NOTCH2 intracellular domain regulates transcription.

Names & Taxonomyi

Protein namesi
Recommended 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
Cleaved into the following 2 chains:
Gene namesi
Name:FCER2
Synonyms:CD23A, CLEC4J, FCE2, IGEBF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:3612. FCER2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 21CytoplasmicSequence analysisAdd BLAST21
Transmembranei22 – 47Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST26
Topological domaini48 – 321ExtracellularSequence analysisAdd BLAST274

GO - Cellular componenti

  • external side of plasma membrane Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • integral component of plasma membrane Source: ProtInc
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi2208.
OpenTargetsiENSG00000104921.
PharmGKBiPA28058.

Chemistry databases

ChEMBLiCHEMBL2940.

Polymorphism and mutation databases

BioMutaiFCER2.
DMDMi119862.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000173911 – 321Low affinity immunoglobulin epsilon Fc receptor membrane-bound formAdd BLAST321
ChainiPRO_0000017392150 – 321Low affinity immunoglobulin epsilon Fc receptor soluble formAdd BLAST172

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi17S-palmitoyl cysteine1 Publication1
Lipidationi18S-palmitoyl cysteine1 Publication1
Glycosylationi63N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi160 ↔ 288
Disulfide bondi163 ↔ 174
Disulfide bondi191 ↔ 282
Disulfide bondi259 ↔ 273

Post-translational modificationi

N- and O-glycosylated.
The secreted form sCD23 is produced by ADAM10-mediated ectodomain shedding.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei149 – 150Cleavage2

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

MaxQBiP06734.
PaxDbiP06734.
PeptideAtlasiP06734.
PRIDEiP06734.

PTM databases

SwissPalmiP06734.

Miscellaneous databases

PMAP-CutDBP06734.

Expressioni

Gene expression databases

BgeeiENSG00000104921.
CleanExiHS_FCER2.
ExpressionAtlasiP06734. baseline and differential.
GenevisibleiP06734. HS.

Organism-specific databases

HPAiCAB002624.
HPA008928.

Interactioni

Subunit structurei

Homotrimer.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATF7P175443EBI-10199985,EBI-765623

GO - Molecular functioni

  • integrin binding Source: ProtInc

Protein-protein interaction databases

BioGridi108502. 4 interactors.
IntActiP06734. 1 interactor.
STRINGi9606.ENSP00000264072.

Chemistry databases

BindingDBiP06734.

Structurei

Secondary structure

1321
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi159 – 162Combined sources4
Beta strandi164 – 166Combined sources3
Beta strandi168 – 170Combined sources3
Beta strandi173 – 182Combined sources10
Helixi184 – 193Combined sources10
Beta strandi196 – 198Combined sources3
Helixi204 – 211Combined sources8
Beta strandi215 – 217Combined sources3
Beta strandi219 – 226Combined sources8
Turni227 – 230Combined sources4
Beta strandi231 – 234Combined sources4
Turni247 – 252Combined sources6
Beta strandi253 – 256Combined sources4
Beta strandi259 – 262Combined sources4
Turni264 – 266Combined sources3
Beta strandi268 – 271Combined sources4
Beta strandi277 – 285Combined sources9
Beta strandi287 – 289Combined sources3
Beta strandi291 – 294Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP06734.
SMRiP06734.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06734.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati69 – 89Add BLAST21
Repeati90 – 110Add BLAST21
Repeati111 – 131Add BLAST21
Domaini162 – 284C-type lectinPROSITE-ProRule annotationAdd BLAST123

Sequence similaritiesi

Contains 1 C-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4297. Eukaryota.
ENOG410XPJ1. LUCA.
GeneTreeiENSGT00760000118924.
HOGENOMiHOG000089951.
HOVERGENiHBG051599.
InParanoidiP06734.
KOiK06468.
OMAiGQWNDAF.
OrthoDBiEOG091G0KN3.
PhylomeDBiP06734.
TreeFamiTF333341.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin-like.
IPR016186. C-type_lectin-like/link.
IPR018378. C-type_lectin_CS.
IPR016187. CTDL_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P06734-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEGQYSEIE ELPRRRCCRR GTQIVLLGLV TAALWAGLLT LLLLWHWDTT
60 70 80 90 100
QSLKQLEERA ARNVSQVSKN LESHHGDQMA QKSQSTQISQ ELEELRAEQQ
110 120 130 140 150
RLKSQDLELS WNLNGLQADL SSFKSQELNE RNEASDLLER LREEVTKLRM
160 170 180 190 200
ELQVSSGFVC NTCPEKWINF QRKCYYFGKG TKQWVHARYA CDDMEGQLVS
210 220 230 240 250
IHSPEEQDFL TKHASHTGSW IGLRNLDLKG EFIWVDGSHV DYSNWAPGEP
260 270 280 290 300
TSRSQGEDCV MMRGSGRWND AFCDRKLGAW VCDRLATCTP PASEGSAESM
310 320
GPDSRPDPDG RLPTPSAPLH S
Length:321
Mass (Da):36,469
Last modified:January 1, 1988 - v1
Checksum:iF86708C0E6515B87
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti269N → T in CAA28465 (PubMed:3034567).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03538762R → W.Corresponds to variant rs2228137dbSNPEnsembl.1
Natural variantiVAR_035388284R → Q.Corresponds to variant rs8102872dbSNPEnsembl.1
Natural variantiVAR_069800316S → F.1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS12184.1.
PIRiA26067. LNHUER.
RefSeqiNP_001193948.2. NM_001207019.2.
NP_001207429.1. NM_001220500.1.
NP_001993.2. NM_002002.4.
XP_005272519.1. XM_005272462.4.
UniGeneiHs.465778.

Genome annotation databases

EnsembliENST00000346664; ENSP00000264072; ENSG00000104921.
ENST00000597921; ENSP00000471974; ENSG00000104921.
GeneIDi2208.
KEGGihsa:2208.
UCSCiuc002mhm.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

CD23

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS12184.1.
PIRiA26067. LNHUER.
RefSeqiNP_001193948.2. NM_001207019.2.
NP_001207429.1. NM_001220500.1.
NP_001993.2. NM_002002.4.
XP_005272519.1. XM_005272462.4.
UniGeneiHs.465778.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP06734.
SMRiP06734.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108502. 4 interactors.
IntActiP06734. 1 interactor.
STRINGi9606.ENSP00000264072.

Chemistry databases

BindingDBiP06734.
ChEMBLiCHEMBL2940.

PTM databases

SwissPalmiP06734.

Polymorphism and mutation databases

BioMutaiFCER2.
DMDMi119862.

Proteomic databases

MaxQBiP06734.
PaxDbiP06734.
PeptideAtlasiP06734.
PRIDEiP06734.

Protocols and materials databases

DNASUi2208.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000346664; ENSP00000264072; ENSG00000104921.
ENST00000597921; ENSP00000471974; ENSG00000104921.
GeneIDi2208.
KEGGihsa:2208.
UCSCiuc002mhm.3. human.

Organism-specific databases

CTDi2208.
DisGeNETi2208.
GeneCardsiFCER2.
HGNCiHGNC:3612. FCER2.
HPAiCAB002624.
HPA008928.
MIMi151445. gene.
neXtProtiNX_P06734.
OpenTargetsiENSG00000104921.
PharmGKBiPA28058.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4297. Eukaryota.
ENOG410XPJ1. LUCA.
GeneTreeiENSGT00760000118924.
HOGENOMiHOG000089951.
HOVERGENiHBG051599.
InParanoidiP06734.
KOiK06468.
OMAiGQWNDAF.
OrthoDBiEOG091G0KN3.
PhylomeDBiP06734.
TreeFamiTF333341.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000104921-MONOMER.
ReactomeiR-HSA-2197563. NOTCH2 intracellular domain regulates transcription.

Miscellaneous databases

EvolutionaryTraceiP06734.
GeneWikiiCD23.
GenomeRNAii2208.
PMAP-CutDBP06734.
PROiP06734.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000104921.
CleanExiHS_FCER2.
ExpressionAtlasiP06734. baseline and differential.
GenevisibleiP06734. HS.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin-like.
IPR016186. C-type_lectin-like/link.
IPR018378. C-type_lectin_CS.
IPR016187. CTDL_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFCER2_HUMAN
AccessioniPrimary (citable) accession number: P06734
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: November 30, 2016
This is version 182 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.