FCERA_HUMAN
ID FCERA_HUMAN Reviewed; 257 AA.
AC P12319;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=High affinity immunoglobulin epsilon receptor subunit alpha;
DE AltName: Full=Fc-epsilon RI-alpha;
DE Short=FcERI;
DE AltName: Full=IgE Fc receptor subunit alpha;
DE Flags: Precursor;
GN Name=FCER1A; Synonyms=FCE1A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2967464; DOI=10.1093/nar/16.8.3584;
RA Kochan J., Pettine L.F., Hakimi J., Kishi K., Kinet J.-P.;
RT "Isolation of the gene coding for the alpha subunit of the human high
RT affinity IgE receptor.";
RL Nucleic Acids Res. 16:3584-3584(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Mast cell;
RX PubMed=2964640; DOI=10.1073/pnas.85.6.1907;
RA Shimizu A., Tepler I., Benfey P.N., Berenstein E.H., Siraganian R.P.,
RA Leder P.;
RT "Human and rat mast cell high-affinity immunoglobulin E receptors:
RT characterization of putative alpha-chain gene products.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:1907-1911(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 26-197.
RX PubMed=8125119; DOI=10.1111/j.1432-1033.1994.tb18660.x;
RA Yagi S., Yanagida M., Tanida I., Hasegawa A., Okumura K., Ra C.;
RT "High-level expression of the truncated alpha chain of human high-affinity
RT receptor for IgE as a soluble form by baculovirus-infected insect cells.
RT Biochemical characterization of the recombinant product.";
RL Eur. J. Biochem. 220:593-598(1994).
RN [5]
RP 3D-STRUCTURE MODELING OF 26-197.
RX PubMed=1472946;
RA Padlan E.A., Helm B.A.;
RT "A modeling study of the alpha-subunit of human high-affinity receptor for
RT immunoglobulin-E.";
RL Receptor 2:129-144(1992).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 26-201, GLYCOSYLATION AT ASN-46;
RP ASN-67 AND ASN-191, AND DISULFIDE BONDS.
RX PubMed=9875849; DOI=10.1016/s0092-8674(00)81719-5;
RA Garman S.C., Kinet J.P., Jardetzky T.S.;
RT "Crystal structure of the human high-affinity IgE receptor.";
RL Cell 95:951-961(1998).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 26-201, GLYCOSYLATION AT ASN-46;
RP ASN-67; ASN-99; ASN-165 AND ASN-191, AND DISULFIDE BONDS.
RX PubMed=11531339; DOI=10.1006/jmbi.2001.4929;
RA Garman S.C., Sechi S., Kinet J.P., Jardetzky T.S.;
RT "The analysis of the human high affinity IgE receptor Fc epsilon Ri alpha
RT from multiple crystal forms.";
RL J. Mol. Biol. 311:1049-1062(2001).
CC -!- FUNCTION: Binds to the Fc region of immunoglobulins epsilon. High
CC affinity receptor. Responsible for initiating the allergic response.
CC Binding of allergen to receptor-bound IgE leads to cell activation and
CC the release of mediators (such as histamine) responsible for the
CC manifestations of allergy. The same receptor also induces the secretion
CC of important lymphokines.
CC -!- SUBUNIT: Tetramer of an alpha chain, a beta chain, and two disulfide
CC linked gamma chains.
CC -!- INTERACTION:
CC P12319; Q14696: MESD; NbExp=3; IntAct=EBI-3908910, EBI-6165891;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
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DR EMBL; X06948; CAA30025.1; -; mRNA.
DR EMBL; J03605; AAA36204.1; -; mRNA.
DR EMBL; BC005912; AAH05912.1; -; mRNA.
DR CCDS; CCDS1184.1; -.
DR PIR; S00682; S00682.
DR RefSeq; NP_001992.1; NM_002001.3.
DR PDB; 1F2Q; X-ray; 2.40 A; A=26-201.
DR PDB; 1F6A; X-ray; 3.50 A; A=26-201.
DR PDB; 1J86; X-ray; 3.20 A; A/B=26-201.
DR PDB; 1J87; X-ray; 3.20 A; A=26-197.
DR PDB; 1J88; X-ray; 3.20 A; A/B/C/D/E=26-197.
DR PDB; 1J89; X-ray; 4.10 A; A/B/C/D/E=26-197.
DR PDB; 1RPQ; X-ray; 3.00 A; A/B/C/D=26-201.
DR PDB; 2Y7Q; X-ray; 3.40 A; A=26-201.
DR PDB; 7SHT; EM; 7.29 A; A=30-197.
DR PDBsum; 1F2Q; -.
DR PDBsum; 1F6A; -.
DR PDBsum; 1J86; -.
DR PDBsum; 1J87; -.
DR PDBsum; 1J88; -.
DR PDBsum; 1J89; -.
DR PDBsum; 1RPQ; -.
DR PDBsum; 2Y7Q; -.
DR PDBsum; 7SHT; -.
DR AlphaFoldDB; P12319; -.
DR SMR; P12319; -.
DR BioGRID; 108499; 41.
DR DIP; DIP-6166N; -.
DR IntAct; P12319; 2.
DR STRING; 9606.ENSP00000357097; -.
DR BindingDB; P12319; -.
DR ChEMBL; CHEMBL2248; -.
DR DrugBank; DB00895; Benzylpenicilloyl polylysine.
DR DrugBank; DB00043; Omalizumab.
DR DrugBank; DB05797; TNX-901.
DR GuidetoPHARMACOLOGY; 2933; -.
DR GlyGen; P12319; 7 sites.
DR iPTMnet; P12319; -.
DR PhosphoSitePlus; P12319; -.
DR BioMuta; FCER1A; -.
DR DMDM; 119865; -.
DR PaxDb; P12319; -.
DR PeptideAtlas; P12319; -.
DR PRIDE; P12319; -.
DR ProteomicsDB; 52851; -.
DR ABCD; P12319; 4 sequenced antibodies.
DR Antibodypedia; 20472; 692 antibodies from 38 providers.
DR DNASU; 2205; -.
DR Ensembl; ENST00000368115.5; ENSP00000357097.1; ENSG00000179639.11.
DR Ensembl; ENST00000693622.1; ENSP00000509626.1; ENSG00000179639.11.
DR GeneID; 2205; -.
DR KEGG; hsa:2205; -.
DR MANE-Select; ENST00000693622.1; ENSP00000509626.1; NM_001387280.1; NP_001374209.1.
DR UCSC; uc001ftq.4; human.
DR CTD; 2205; -.
DR DisGeNET; 2205; -.
DR GeneCards; FCER1A; -.
DR HGNC; HGNC:3609; FCER1A.
DR HPA; ENSG00000179639; Tissue enhanced (skin).
DR MIM; 147140; gene.
DR neXtProt; NX_P12319; -.
DR OpenTargets; ENSG00000179639; -.
DR PharmGKB; PA28056; -.
DR VEuPathDB; HostDB:ENSG00000179639; -.
DR eggNOG; ENOG502RTXR; Eukaryota.
DR GeneTree; ENSGT01050000244808; -.
DR HOGENOM; CLU_023383_1_0_1; -.
DR InParanoid; P12319; -.
DR OMA; IRCHSWK; -.
DR OrthoDB; 866496at2759; -.
DR PhylomeDB; P12319; -.
DR TreeFam; TF335097; -.
DR PathwayCommons; P12319; -.
DR Reactome; R-HSA-2454202; Fc epsilon receptor (FCERI) signaling.
DR Reactome; R-HSA-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
DR Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
DR Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR SignaLink; P12319; -.
DR SIGNOR; P12319; -.
DR BioGRID-ORCS; 2205; 44 hits in 1062 CRISPR screens.
DR ChiTaRS; FCER1A; human.
DR EvolutionaryTrace; P12319; -.
DR GeneWiki; FCER1A; -.
DR GenomeRNAi; 2205; -.
DR Pharos; P12319; Tbio.
DR PRO; PR:P12319; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P12319; protein.
DR Bgee; ENSG00000179639; Expressed in upper leg skin and 152 other tissues.
DR ExpressionAtlas; P12319; baseline and differential.
DR Genevisible; P12319; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0019863; F:IgE binding; IEA:UniProtKB-KW.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0050776; P:regulation of immune response; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF13895; Ig_2; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; IgE-binding protein; Immunoglobulin domain; Membrane;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:8125119"
FT CHAIN 26..257
FT /note="High affinity immunoglobulin epsilon receptor
FT subunit alpha"
FT /id="PRO_0000015161"
FT TOPO_DOM 26..205
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..110
FT /note="Ig-like 1"
FT DOMAIN 111..193
FT /note="Ig-like 2"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11531339,
FT ECO:0000269|PubMed:9875849"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11531339,
FT ECO:0000269|PubMed:9875849"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11531339"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11531339"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11531339,
FT ECO:0000269|PubMed:9875849"
FT DISULFID 51..93
FT /evidence="ECO:0000269|PubMed:11531339,
FT ECO:0000269|PubMed:9875849, ECO:0007744|PDB:1F2Q"
FT DISULFID 132..176
FT /evidence="ECO:0000269|PubMed:11531339,
FT ECO:0000269|PubMed:9875849, ECO:0007744|PDB:1F2Q"
FT VARIANT 84
FT /note="K -> R (in dbSNP:rs2298804)"
FT /id="VAR_020091"
FT VARIANT 101
FT /note="S -> N (in dbSNP:rs2298805)"
FT /id="VAR_020092"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:1F2Q"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:1F2Q"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:1F2Q"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1F6A"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:1F2Q"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:2Y7Q"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:1F2Q"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:1F2Q"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:1F2Q"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:1RPQ"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:1F2Q"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:1F2Q"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:1F2Q"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:1F2Q"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:1F2Q"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:1F2Q"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:1RPQ"
FT STRAND 158..165
FT /evidence="ECO:0007829|PDB:1F2Q"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:1F2Q"
FT STRAND 172..180
FT /evidence="ECO:0007829|PDB:1F2Q"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:1F2Q"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:1F2Q"
SQ SEQUENCE 257 AA; 29596 MW; F183BB2357DDAD58 CRC64;
MAPAMESPTL LCVALLFFAP DGVLAVPQKP KVSLNPPWNR IFKGENVTLT CNGNNFFEVS
STKWFHNGSL SEETNSSLNI VNAKFEDSGE YKCQHQQVNE SEPVYLEVFS DWLLLQASAE
VVMEGQPLFL RCHGWRNWDV YKVIYYKDGE ALKYWYENHN ISITNATVED SGTYYCTGKV
WQLDYESEPL NITVIKAPRE KYWLQFFIPL LVVILFAVDT GLFISTQQQV TFLLKIKRTR
KGFRLLNPHP KPNPKNN
