FCERA_RAT
ID FCERA_RAT Reviewed; 245 AA.
AC P12371; P12840;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 150.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2959318; DOI=10.1021/bi00389a002;
RA Kinet J.-P., Metzger H., Hakimi J., Kochan J.;
RT "A cDNA presumptively coding for the alpha subunit of the receptor with
RT high affinity for immunoglobulin E.";
RL Biochemistry 26:4605-4610(1987).
RN [2]
RP SEQUENCE REVISION.
RA Kochan J.;
RL Submitted (MAR-1988) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=2969594; DOI=10.1073/pnas.85.15.5639;
RA Liu F.-T., Albrandt K., Robertson M.W.;
RT "cDNA heterogeneity suggests structural variants related to the high-
RT affinity IgE receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:5639-5643(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-16, AND ALTERNATIVE SPLICING.
RX PubMed=2522441; DOI=10.1016/s0021-9258(18)83636-5;
RA Tepler I., Shimizu A., Leder P.;
RT "The gene for the rat mast cell high affinity IgE receptor alpha chain.
RT Structure and alternative mRNA splicing patterns.";
RL J. Biol. Chem. 264:5912-5915(1989).
RN [6]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=17728245; DOI=10.1074/jbc.m705950200;
RA Ganguly S., Grodzki C., Sugden D., Moller M., Odom S., Gaildrat P.,
RA Gery I., Siraganian R.P., Rivera J., Klein D.C.;
RT "Neural adrenergic/cyclic AMP regulation of the immunoglobulin E receptor
RT alpha-subunit expression in the mammalian pinealocyte: a
RT neuroendocrine/immune response link?";
RL J. Biol. Chem. 282:32758-32764(2007).
RN [7]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=19103603; DOI=10.1074/jbc.m808394200;
RA Bailey M.J., Coon S.L., Carter D.A., Humphries A., Kim J.S., Shi Q.,
RA Gaildrat P., Morin F., Ganguly S., Hogenesch J.B., Weller J.L., Rath M.F.,
RA Moller M., Baler R., Sugden D., Rangel Z.G., Munson P.J., Klein D.C.;
RT "Night/day changes in pineal expression of >600 genes: central role of
RT adrenergic/cAMP signaling.";
RL J. Biol. Chem. 284:7606-7622(2009).
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 -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P12371-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P12371-2; Sequence=VSP_012760, VSP_012761;
CC -!- TISSUE SPECIFICITY: Expressed in leukocytes and pinealocytes at night
CC (at protein level). {ECO:0000269|PubMed:17728245,
CC ECO:0000269|PubMed:19103603}.
CC -!- INDUCTION: Exhibits night/day variations with a 15-fold increased
CC expression at night in the pineal gland. Up-regulation is due to a
CC large degree to the release of norepinephrine from nerve terminals in
CC the pineal gland and cAMP signaling pathway (at protein level).
CC {ECO:0000269|PubMed:17728245, ECO:0000269|PubMed:19103603}.
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DR EMBL; M17153; AAA42045.1; -; mRNA.
DR EMBL; J03606; AAA41582.1; -; mRNA.
DR EMBL; M21622; AAA41146.1; -; mRNA.
DR EMBL; M21623; AAA41147.1; -; mRNA.
DR PIR; C31327; A30154.
DR PIR; D31327; D31327.
DR RefSeq; NP_036856.1; NM_012724.4. [P12371-1]
DR AlphaFoldDB; P12371; -.
DR SMR; P12371; -.
DR STRING; 10116.ENSRNOP00000054898; -.
DR GlyGen; P12371; 7 sites.
DR PaxDb; P12371; -.
DR PRIDE; P12371; -.
DR Ensembl; ENSRNOT00000104245; ENSRNOP00000092868; ENSRNOG00000009177. [P12371-1]
DR GeneID; 25047; -.
DR KEGG; rno:25047; -.
DR CTD; 2205; -.
DR RGD; 2597; Fcer1a.
DR eggNOG; ENOG502RTXR; Eukaryota.
DR GeneTree; ENSGT01050000244808; -.
DR InParanoid; P12371; -.
DR OrthoDB; 866496at2759; -.
DR PhylomeDB; P12371; -.
DR Reactome; R-RNO-2454202; Fc epsilon receptor (FCERI) signaling.
DR Reactome; R-RNO-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
DR Reactome; R-RNO-2871796; FCERI mediated MAPK activation.
DR Reactome; R-RNO-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-RNO-2871837; FCERI mediated NF-kB activation.
DR PRO; PR:P12371; -.
DR Proteomes; UP000002494; Chromosome 13.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0019768; F:high-affinity IgE receptor activity; TAS:RGD.
DR GO; GO:0019863; F:IgE binding; ISO:RGD.
DR GO; GO:0019767; F:IgE receptor activity; ISO:RGD.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:RGD.
DR GO; GO:0006955; P:immune response; TAS:RGD.
DR GO; GO:0019370; P:leukotriene biosynthetic process; ISO:RGD.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; ISO:RGD.
DR GO; GO:0032725; P:positive regulation of granulocyte macrophage colony-stimulating factor production; ISO:RGD.
DR GO; GO:0032752; P:positive regulation of interleukin-3 production; ISO:RGD.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; ISO:RGD.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:RGD.
DR GO; GO:0043306; P:positive regulation of mast cell degranulation; ISO:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:0001812; P:positive regulation of type I hypersensitivity; ISO:RGD.
DR GO; GO:0050776; P:regulation of immune response; IBA:GO_Central.
DR GO; GO:0001820; P:serotonin secretion; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; ISO:RGD.
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 Pfam; PF13895; Ig_2; 1.
DR SMART; SM00409; IG; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW IgE-binding protein; Immunoglobulin domain; Membrane; Receptor;
KW Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT CHAIN 24..245
FT /note="High affinity immunoglobulin epsilon receptor
FT subunit alpha"
FT /id="PRO_0000015163"
FT TOPO_DOM 24..204
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..245
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..103
FT /note="Ig-like 1"
FT DOMAIN 113..181
FT /note="Ig-like 2"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 130..174
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 141..157
FT /note="VIYYKDDIAFKYSYDSN -> ITQLSIVGYNSFSHHWR (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:2969594"
FT /id="VSP_012760"
FT VAR_SEQ 158..245
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2969594"
FT /id="VSP_012761"
SQ SEQUENCE 245 AA; 27793 MW; A0E67DD363B72197 CRC64;
MDTGGSARLC LALVLISLGV MLTATQKSVV SLDPPWIRIL TGDKVTLICN GNNSSQMNST
KWIHNDSISN VKSSHWVIVS ATIQDSGKYI CQKQGFYKSK PVYLNVMQEW LLLQSSADVV
LDNGSFDIRC RSWKKWKVHK VIYYKDDIAF KYSYDSNNIS IRKATFNDSG SYHCTGYLNK
VECKSDKFSI AVVKDYTIEY RWLQLIFPSL AVILFAVDTG LWFSTHKQFE SILKIQKTGK
GKKKG
