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P12319 (FCERA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length257 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandIgE-binding protein
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

activation of JUN kinase activity

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

leukotriene biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of calcium-mediated signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of granulocyte macrophage colony-stimulating factor biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-3 biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of mast cell degranulation

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of type I hypersensitivity

Inferred from electronic annotation. Source: Ensembl

serotonin secretion

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell surface

Inferred from direct assay PubMed 1535625. Source: UniProtKB

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Traceable author statement Ref.2. Source: ProtInc

   Molecular_functionIgE receptor activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Ref.4
Chain26 – 257232High affinity immunoglobulin epsilon receptor subunit alpha
PRO_0000015161

Regions

Topological domain26 – 205180Extracellular Potential
Transmembrane206 – 22419Helical; Potential
Topological domain225 – 25733Cytoplasmic Potential
Domain30 – 11081Ig-like 1
Domain111 – 19383Ig-like 2

Amino acid modifications

Glycosylation461N-linked (GlcNAc...) Ref.6 Ref.7
Glycosylation671N-linked (GlcNAc...) Ref.6 Ref.7
Glycosylation751N-linked (GlcNAc...) Potential
Glycosylation991N-linked (GlcNAc...) Ref.7
Glycosylation1601N-linked (GlcNAc...) Potential
Glycosylation1651N-linked (GlcNAc...) Ref.7
Glycosylation1911N-linked (GlcNAc...) Ref.6 Ref.7
Disulfide bond51 ↔ 93 Ref.6 Ref.7
Disulfide bond132 ↔ 176 Ref.6 Ref.7

Natural variations

Natural variant841K → R.
Corresponds to variant rs2298804 [ dbSNP | Ensembl ].
VAR_020091
Natural variant1011S → N.
Corresponds to variant rs2298805 [ dbSNP | Ensembl ].
VAR_020092

Secondary structure

........................................... 257
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12319 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: F183BB2357DDAD58

FASTA25729,596
        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 

« Hide

References

« Hide '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.
PIRS00682.
RefSeqNP_001992.1. NM_002001.3.
UniGeneHs.897.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ALSmodel-A26-197[»]
1ALTmodel-A26-197[»]
1F2QX-ray2.40A26-201[»]
1F6AX-ray3.50A26-201[»]
1J86X-ray3.20A/B26-201[»]
1J87X-ray3.20A26-197[»]
1J88X-ray3.20A/B/C/D/E26-197[»]
1J89X-ray4.10A/B/C/D/E26-197[»]
1RPQX-ray3.00A/B/C/D26-201[»]
2Y7QX-ray3.40A26-201[»]
ProteinModelPortalP12319.
SMRP12319. Positions 26-199.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108499. 3 interactions.
DIPDIP-6166N.
IntActP12319. 1 interaction.
STRING9606.ENSP00000315719.

Chemistry

BindingDBP12319.
ChEMBLCHEMBL2248.
DrugBankDB00895. Benzylpenicilloyl Polylysine.
DB00043. Omalizumab.

PTM databases

PhosphoSiteP12319.

Polymorphism databases

DMDM119865.

Proteomic databases

PaxDbP12319.
PRIDEP12319.

Protocols and materials databases

DNASU2205.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368115; ENSP00000357097; ENSG00000179639.
GeneID2205.
KEGGhsa:2205.
UCSCuc001ftq.3. human.

Organism-specific databases

CTD2205.
GeneCardsGC01P159259.
HGNCHGNC:3609. FCER1A.
HPACAB022102.
MIM147140. gene.
neXtProtNX_P12319.
PharmGKBPA28056.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG27903.
HOGENOMHOG000251632.
HOVERGENHBG051602.
InParanoidP12319.
KOK08089.
OMAYENHNIS.
OrthoDBEOG72NRRC.
TreeFamTF335097.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressP12319.
BgeeP12319.
CleanExHS_FCER1A.
GenevestigatorP12319.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]
SMARTSM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP12319.
GeneWikiFCER1A.
GenomeRNAi2205.
NextBio8931.
PROP12319.
SOURCESearch...

Entry information

Entry nameFCERA_HUMAN
AccessionPrimary (citable) accession number: P12319
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: February 19, 2014
This is version 144 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 1

Human chromosome 1: entries, gene names and cross-references to MIM