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High affinity immunoglobulin epsilon receptor subunit alpha (Fc-epsilon RI-alpha) (FcERI) (IgE Fc receptor subunit alpha)

 FCERA_RAT               Reviewed;         245 AA.
P12371; P12840;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
10-MAY-2017, entry version 132.
RecName: Full=High affinity immunoglobulin epsilon receptor subunit alpha;
AltName: Full=Fc-epsilon RI-alpha;
Short=FcERI;
AltName: Full=IgE Fc receptor subunit alpha;
Flags: Precursor;
Name=Fcer1a; Synonyms=Fce1a;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2959318; DOI=10.1021/bi00389a002;
Kinet J.-P., Metzger H., Hakimi J., Kochan J.;
"A cDNA presumptively coding for the alpha subunit of the receptor
with high affinity for immunoglobulin E.";
Biochemistry 26:4605-4610(1987).
[2]
SEQUENCE REVISION.
Kochan J.;
Submitted (MAR-1988) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Mast cell;
PubMed=2964640; DOI=10.1073/pnas.85.6.1907;
Shimizu A., Tepler I., Benfey P.N., Berenstein E.H., Siraganian R.P.,
Leder P.;
"Human and rat mast cell high-affinity immunoglobulin E receptors:
characterization of putative alpha-chain gene products.";
Proc. Natl. Acad. Sci. U.S.A. 85:1907-1911(1988).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
PubMed=2969594; DOI=10.1073/pnas.85.15.5639;
Liu F.-T., Albrandt K., Robertson M.W.;
"cDNA heterogeneity suggests structural variants related to the high-
affinity IgE receptor.";
Proc. Natl. Acad. Sci. U.S.A. 85:5639-5643(1988).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-16, AND ALTERNATIVE SPLICING.
PubMed=2522441;
Tepler I., Shimizu A., Leder P.;
"The gene for the rat mast cell high affinity IgE receptor alpha
chain. Structure and alternative mRNA splicing patterns.";
J. Biol. Chem. 264:5912-5915(1989).
[6]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=17728245; DOI=10.1074/jbc.M705950200;
Ganguly S., Grodzki C., Sugden D., Moller M., Odom S., Gaildrat P.,
Gery I., Siraganian R.P., Rivera J., Klein D.C.;
"Neural adrenergic/cyclic AMP regulation of the immunoglobulin E
receptor alpha-subunit expression in the mammalian pinealocyte: a
neuroendocrine/immune response link?";
J. Biol. Chem. 282:32758-32764(2007).
[7]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=19103603; DOI=10.1074/jbc.M808394200;
Bailey M.J., Coon S.L., Carter D.A., Humphries A., Kim J.S., Shi Q.,
Gaildrat P., Morin F., Ganguly S., Hogenesch J.B., Weller J.L.,
Rath M.F., Moller M., Baler R., Sugden D., Rangel Z.G., Munson P.J.,
Klein D.C.;
"Night/day changes in pineal expression of >600 genes: central role of
adrenergic/cAMP signaling.";
J. Biol. Chem. 284:7606-7622(2009).
-!- 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: Tetramer of an alpha chain, a beta chain, and two
disulfide linked gamma chains.
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
membrane protein.
-!- SUBCELLULAR LOCATION: Isoform 2: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P12371-1; Sequence=Displayed;
Name=2;
IsoId=P12371-2; Sequence=VSP_012760, VSP_012761;
-!- TISSUE SPECIFICITY: Expressed in leukocytes and pinealocytes at
night (at protein level). {ECO:0000269|PubMed:17728245,
ECO:0000269|PubMed:19103603}.
-!- INDUCTION: Exhibits night/day variations with a 15-fold increased
expression at night in the pineal gland. Up-regulation is due to a
large degree to the release of norepinephrine from nerve terminals
in the pineal gland and cAMP signaling pathway (at protein level).
{ECO:0000269|PubMed:17728245, ECO:0000269|PubMed:19103603}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; M17153; AAA42045.1; -; mRNA.
EMBL; J03606; AAA41582.1; -; mRNA.
EMBL; M21622; AAA41146.1; -; mRNA.
EMBL; M21623; AAA41147.1; -; mRNA.
PIR; C31327; A30154.
PIR; D31327; D31327.
RefSeq; NP_036856.1; NM_012724.4. [P12371-1]
UniGene; Rn.9677; -.
ProteinModelPortal; P12371; -.
SMR; P12371; -.
STRING; 10116.ENSRNOP00000054898; -.
PaxDb; P12371; -.
GeneID; 25047; -.
KEGG; rno:25047; -.
CTD; 2205; -.
RGD; 2597; Fcer1a.
eggNOG; ENOG410IJME; Eukaryota.
eggNOG; ENOG410ZPGM; LUCA.
HOGENOM; HOG000251632; -.
HOVERGEN; HBG051602; -.
InParanoid; P12371; -.
KO; K08089; -.
PhylomeDB; P12371; -.
PRO; PR:P12371; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0019768; F:high-affinity IgE receptor activity; TAS:RGD.
GO; GO:0019863; F:IgE binding; TAS:RGD.
GO; GO:0006955; P:immune response; TAS:RGD.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
Pfam; PF13895; Ig_2; 1.
SMART; SM00409; IG; 2.
SUPFAM; SSF48726; SSF48726; 2.
PROSITE; PS50835; IG_LIKE; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; IgE-binding protein;
Immunoglobulin domain; Membrane; Receptor; Reference proteome; Repeat;
Secreted; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 23
CHAIN 24 245 High affinity immunoglobulin epsilon
receptor subunit alpha.
/FTId=PRO_0000015163.
TOPO_DOM 24 204 Extracellular. {ECO:0000255}.
TRANSMEM 205 223 Helical. {ECO:0000255}.
TOPO_DOM 224 245 Cytoplasmic. {ECO:0000255}.
DOMAIN 28 103 Ig-like 1.
DOMAIN 113 181 Ig-like 2.
CARBOHYD 52 52 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 53 53 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 58 58 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 65 65 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 123 123 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 158 158 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 167 167 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 49 91 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 130 174 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 141 157 VIYYKDDIAFKYSYDSN -> ITQLSIVGYNSFSHHWR
(in isoform 2).
{ECO:0000303|PubMed:2969594}.
/FTId=VSP_012760.
VAR_SEQ 158 245 Missing (in isoform 2).
{ECO:0000303|PubMed:2969594}.
/FTId=VSP_012761.
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


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