P06734 (FCER2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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:

1. Low affinity immunoglobulin epsilon Fc receptor membrane-bound form
2. Low affinity immunoglobulin epsilon Fc receptor soluble form

Gene names

Name:	FCER2
Synonyms:	CD23A, CLEC4J, FCE2, IGEBF

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	321 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Cell membrane Membrane Secreted
Coding sequence diversity	Polymorphism
Domain	Repeat Signal-anchor Transmembrane Transmembrane helix
Ligand	Calcium IgE-binding protein Lectin Metal-binding
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of humoral immune response mediated by circulating immunoglobulin Inferred from electronic annotation. Source: Compara 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_component	external side of plasma membrane Inferred from electronic annotation. Source: Compara extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Traceable author statement PubMed 2529542. Source: ProtInc
Molecular_function	carbohydrate 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 321

321

Low affinity immunoglobulin epsilon Fc receptor membrane-bound form

PRO_0000017391

Chain

150 – 321

172

Low affinity immunoglobulin epsilon Fc receptor soluble form

PRO_0000017392

Regions

Topological domain

1 – 21

21

Cytoplasmic Potential

Transmembrane

22 – 47

26

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

48 – 321

274

Extracellular Potential

Repeat

69 – 89

21

Repeat

90 – 110

21

Repeat

111 – 131

21

Domain

162 – 284

123

C-type lectin

Sites

Metal binding

249

1

Calcium

Metal binding

251

1

Calcium

Metal binding

269

1

Calcium

Metal binding

270

1

Calcium

Site

149 – 150

2

Cleavage

Amino acid modifications

Lipidation

17

1

S-palmitoyl cysteine Ref.9

Lipidation

18

1

S-palmitoyl cysteine Ref.9

Glycosylation

63

1

N-linked (GlcNAc...) Potential

Disulfide bond

160 ↔ 288

Ref.7 Ref.12 Ref.13

Disulfide bond

163 ↔ 174

Ref.7 Ref.12 Ref.13

Disulfide bond

191 ↔ 282

Ref.7 Ref.12 Ref.13

Disulfide bond

259 ↔ 273

Ref.7 Ref.12 Ref.13

Natural variations

Natural variant

62

1

R → W.
Corresponds to variant rs2228137 [ dbSNP | Ensembl ].

VAR_035387

Natural variant

284

1

R → Q.
Corresponds to variant rs8102872 [ dbSNP | Ensembl ].

VAR_035388

Experimental info

Sequence conflict

269

1

N → T in CAA28465. Ref.3

Secondary structure

1

.

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321

Helix Strand Turn

Details...

Beta strand

159 – 162

4

Beta strand

164 – 166

3

Beta strand

168 – 170

3

Beta strand

173 – 182

10

Helix

184 – 193

10

Helix

204 – 211

8

Beta strand

215 – 217

3

Beta strand

219 – 226

8

Turn

227 – 230

4

Beta strand

231 – 234

4

Beta strand

245 – 248

4

Beta strand

252 – 255

4

Beta strand

259 – 262

4

Turn

264 – 266

3

Beta strand

268 – 271

4

Beta strand

277 – 285

9

Beta strand

287 – 289

3

Beta strand

291 – 294

4

Sequences

	Sequence		Length	Mass (Da)
	P06734 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: F86708C0E6515B87	FASTA	321	36,469
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
+	Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - Glycan Binding

CD23

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.

IPI

IPI00027491.
IPI00217263.

PIR

LNHUER. A26067.

RefSeq

NP_001193948.2. NM_001207019.2.
NP_001207429.1. NM_001220500.1.
NP_001993.2. NM_002002.4.

UniGene

Hs.465778.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HLI	model	-	A	173-285	[»]
1KJE	model	-	A	173-285	[»]
1T8C	NMR	-	A	156-298	[»]
1T8D	NMR	-	A	156-298	[»]
2H2R	X-ray	1.50	A/B	150-321	[»]
2H2T	X-ray	1.30	B	150-321	[»]
4EZM	X-ray	3.10	G/H/I/J/K/L	156-298	[»]

ProteinModelPortal

P06734.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000264072.

PTM databases

PhosphoSite

P06734.

Polymorphism databases

DMDM

119862.

Proteomic databases

PaxDb

P06734.

PRIDE

P06734.

Protocols and materials databases

DNASU

2208.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000346664; ENSP00000264072; ENSG00000104921.
ENST00000597921; ENSP00000471974; ENSG00000104921.

GeneID

2208.

KEGG

hsa:2208.

UCSC

uc002mhm.2. human.
uc021unx.1. human.

Organism-specific databases

CTD

2208.

GeneCards

GC19M007754.

HGNC

HGNC:3612. FCER2.

HPA

CAB002624.
HPA008928.

MIM

151445. gene.

neXtProt

NX_P06734.

PharmGKB

PA28058.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG235454.

HOGENOM

HOG000089951.

HOVERGEN

HBG051599.

InParanoid

P06734.

KO

K06468.

OMA

KCYYFGE.

OrthoDB

EOG4KKZ3Q.

PhylomeDB

P06734.

Enzyme and pathway databases

Pathway_Interaction_DB

il4_2pathway. IL4-mediated signaling events.

Gene expression databases

Bgee

P06734.

CleanEx

HS_FCER2.

Genevestigator

P06734.

GermOnline

ENSG00000104921. Homo sapiens.

Family and domain databases

Gene3D

3.10.100.10. 1 hit.

InterPro

IPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
[Graphical view]

Pfam

PF00059. Lectin_C. 1 hit.
[Graphical view]

SMART

SM00034. CLECT. 1 hit.
[Graphical view]

SUPFAM

SSF56436. C-type_lectin_fold. 1 hit.

PROSITE

PS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P06734.

ChEMBL

CHEMBL2940.

EvolutionaryTrace

P06734.

GenomeRNAi

2208.

NextBio

8943.

PMAP-CutDB

P06734.

SOURCE

Search...

Entry information

Entry name

FCER2_HUMAN

Accession

Primary (citable) accession number: P06734

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	May 1, 2013
This is version 149 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.