P12319 (FCERA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
High affinity immunoglobulin epsilon receptor subunit alpha

Alternative name(s):
Fc-epsilon RI-alpha
Short name=FcERI
IgE Fc receptor subunit alpha

Gene names

Name:	FCER1A
Synonyms:	FCE1A

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	257 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	Binds to the Fc region of immunoglobulins epsilon. High affinity receptor. Responsible for initiating the allergic response. Binding of allergen to receptor-bound IgE leads to cell activation and the release of mediators (such as histamine) responsible for the manifestations of allergy. The same receptor also induces the secretion of important lymphokines.
Subunit structure	Tetramer of an alpha chain, a beta chain, and two disulfide linked gamma chains.
Subcellular location	Cell membrane; Single-pass type I membrane protein.
Sequence similarities	Contains 2 Ig-like (immunoglobulin-like) domains.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
Ligand	IgE-binding protein
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	activation of JUN kinase activity Inferred from electronic annotation. Source: Compara leukotriene biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of calcium-mediated signaling Inferred from electronic annotation. Source: Compara positive regulation of granulocyte macrophage colony-stimulating factor biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of interleukin-3 biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of mast cell degranulation Inferred from electronic annotation. Source: Compara positive regulation of peptidyl-tyrosine phosphorylation Inferred from electronic annotation. Source: Compara positive regulation of type I hypersensitivity Inferred from electronic annotation. Source: Compara serotonin secretion Inferred from electronic annotation. Source: Compara
Cellular_component	external side of plasma membrane Inferred from electronic annotation. Source: Compara integral to plasma membrane Traceable author statement Ref.2. Source: ProtInc
Molecular_function	IgE receptor activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Ref.4

Chain

26 – 257

232

High affinity immunoglobulin epsilon receptor subunit alpha

PRO_0000015161

Regions

Topological domain

26 – 205

180

Extracellular Potential

Transmembrane

206 – 224

19

Helical; Potential

Topological domain

225 – 257

33

Cytoplasmic Potential

Domain

30 – 110

81

Ig-like 1

Domain

111 – 193

83

Ig-like 2

Amino acid modifications

Glycosylation

46

1

N-linked (GlcNAc...) Ref.6 Ref.7

Glycosylation

67

1

N-linked (GlcNAc...) Ref.6 Ref.7

Glycosylation

75

1

N-linked (GlcNAc...) Potential

Glycosylation

99

1

N-linked (GlcNAc...) Ref.7

Glycosylation

160

1

N-linked (GlcNAc...) Potential

Glycosylation

165

1

N-linked (GlcNAc...) Ref.7

Glycosylation

191

1

N-linked (GlcNAc...) Ref.6 Ref.7

Disulfide bond

51 ↔ 93

Ref.6 Ref.7

Disulfide bond

132 ↔ 176

Ref.6 Ref.7

Natural variations

Natural variant

84

1

K → R.
Corresponds to variant rs2298804 [ dbSNP | Ensembl ].

VAR_020091

Natural variant

101

1

S → N.
Corresponds to variant rs2298805 [ dbSNP | Ensembl ].

VAR_020092

Secondary structure

1

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257

Helix Strand Turn

Details...

Beta strand

33 – 37

5

Beta strand

39 – 42

4

Beta strand

47 – 50

4

Beta strand

53 – 55

3

Beta strand

63 – 66

4

Beta strand

69 – 72

4

Beta strand

75 – 80

6

Helix

85 – 87

3

Beta strand

89 – 94

6

Beta strand

96 – 99

4

Beta strand

104 – 109

6

Beta strand

111 – 118

8

Beta strand

120 – 123

4

Beta strand

128 – 134

7

Helix

135 – 137

3

Beta strand

140 – 147

8

Beta strand

150 – 157

8

Beta strand

158 – 165

8

Helix

168 – 170

3

Beta strand

172 – 180

9

Beta strand

183 – 186

4

Beta strand

190 – 195

6

Sequences

	Sequence		Length	Mass (Da)
	P12319 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: F183BB2357DDAD58	FASTA	257	29,596
	10 20 30 40 50 60 MAPAMESPTL LCVALLFFAP DGVLAVPQKP KVSLNPPWNR IFKGENVTLT CNGNNFFEVS 70 80 90 100 110 120 STKWFHNGSL SEETNSSLNI VNAKFEDSGE YKCQHQQVNE SEPVYLEVFS DWLLLQASAE 130 140 150 160 170 180 VVMEGQPLFL RCHGWRNWDV YKVIYYKDGE ALKYWYENHN ISITNATVED SGTYYCTGKV 190 200 210 220 230 240 WQLDYESEPL NITVIKAPRE KYWLQFFIPL LVVILFAVDT GLFISTQQQV TFLLKIKRTR 250 KGFRLLNPHP KPNPKNN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of the gene coding for the alpha subunit of the human high affinity IgE receptor." Kochan J., Pettine L.F., Hakimi J., Kishi K., Kinet J.-P. Nucleic Acids Res. 16:3584-3584(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Human and rat mast cell high-affinity immunoglobulin E receptors: characterization of putative alpha-chain gene products." Shimizu A., Tepler I., Benfey P.N., Berenstein E.H., Siraganian R.P., Leder P. Proc. Natl. Acad. Sci. U.S.A. 85:1907-1911(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Mast cell.
[3]	"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: Prostate.
[4]	"High-level expression of the truncated alpha chain of human high-affinity receptor for IgE as a soluble form by baculovirus-infected insect cells. Biochemical characterization of the recombinant product." Yagi S., Yanagida M., Tanida I., Hasegawa A., Okumura K., Ra C. Eur. J. Biochem. 220:593-598(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 26-197.
[5]	"A modeling study of the alpha-subunit of human high-affinity receptor for immunoglobulin-E." Padlan E.A., Helm B.A. Receptor 2:129-144(1992) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING OF 26-197.
[6]	"Crystal structure of the human high-affinity IgE receptor." Garman S.C., Kinet J.P., Jardetzky T.S. Cell 95:951-961(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 26-201, GLYCOSYLATION AT ASN-46; ASN-67 AND ASN-191, DISULFIDE BONDS.
[7]	"The analysis of the human high affinity IgE receptor Fc epsilon Ri alpha from multiple crystal forms." Garman S.C., Sechi S., Kinet J.P., Jardetzky T.S. J. Mol. Biol. 311:1049-1062(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 26-201, GLYCOSYLATION AT ASN-46; ASN-67; ASN-99; ASN-165 AND ASN-191, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X06948 mRNA. Translation: CAA30025.1.
J03605 mRNA. Translation: AAA36204.1.
BC005912 mRNA. Translation: AAH05912.1.

IPI

IPI00549768.

PIR

S00682.

RefSeq

NP_001992.1. NM_002001.3.

UniGene

Hs.897.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ALS	model	-	A	26-197	[»]
1ALT	model	-	A	26-197	[»]
1F2Q	X-ray	2.40	A	26-201	[»]
1F6A	X-ray	3.50	A	26-201	[»]
1J86	X-ray	3.20	A/B	26-201	[»]
1J87	X-ray	3.20	A	26-197	[»]
1J88	X-ray	3.20	A/B/C/D/E	26-197	[»]
1J89	X-ray	4.10	A/B/C/D/E	26-197	[»]
1RPQ	X-ray	3.00	A/B/C/D	26-201	[»]
2Y7Q	X-ray	3.40	A	26-201	[»]

ProteinModelPortal

P12319.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6166N.

IntAct

P12319. 1 interaction.

STRING

9606.ENSP00000315719.

PTM databases

PhosphoSite

P12319.

Polymorphism databases

DMDM

119865.

Proteomic databases

PaxDb

P12319.

PRIDE

P12319.

Protocols and materials databases

DNASU

2205.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000368115; ENSP00000357097; ENSG00000179639.

GeneID

2205.

KEGG

hsa:2205.

UCSC

uc001ftq.3. human.

Organism-specific databases

CTD

2205.

GeneCards

GC01P159259.

HGNC

HGNC:3609. FCER1A.

HPA

CAB022102.

MIM

147140. gene.

neXtProt

NX_P12319.

PharmGKB

PA28056.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG27903.

HOGENOM

HOG000251632.

HOVERGEN

HBG051602.

InParanoid

P12319.

KO

K08089.

OMA

IKRTRKG.

OrthoDB

EOG4DBTFQ.

Enzyme and pathway databases

Pathway_Interaction_DB

fcer1pathway. Fc-epsilon receptor I signaling in mast cells.

Gene expression databases

ArrayExpress

P12319.

Bgee

P12319.

CleanEx

HS_FCER1A.

Genevestigator

P12319.

GermOnline

ENSG00000179639. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 2 hits.

InterPro

IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]

SMART

SM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P12319.

ChEMBL

CHEMBL2248.

DrugBank

DB00895. Benzylpenicilloyl Polylysine.
DB00043. Omalizumab.

EvolutionaryTrace

P12319.

GenomeRNAi

2205.

NextBio

8931.

SOURCE

Search...

Entry information

Entry name

FCERA_HUMAN

Accession

Primary (citable) accession number: P12319

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	May 1, 2013
This is version 137 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.