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FCERA_MOUSE
ID   FCERA_MOUSE             Reviewed;         250 AA.
AC   P20489; E9QLR4;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   03-AUG-2022, entry version 173.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2527850; DOI=10.1016/s0021-9258(19)84829-9;
RA   Ra C., Jouvin M.H.E., Kinet J.-P.;
RT   "Complete structure of the mouse mast cell receptor for IgE (Fc epsilon RI)
RT   and surface expression of chimeric receptors (rat-mouse-human) on
RT   transfected cells.";
RL   J. Biol. Chem. 264:15323-15327(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 125-194.
RX   PubMed=1839735; DOI=10.1159/000235511;
RA   Robertson M.W., Mehl V.S., Richards M.L., Liu F.T.;
RT   "mRNA variants encoding multiple forms of the high-affinity IgE receptor
RT   alpha subunit in transformed and nontransformed mast cells.";
RL   Int. Arch. Allergy Appl. Immunol. 96:289-295(1991).
RN   [4]
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).
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: Cell membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Expressed in bone marrow mast cells, as well as in
CC       the pineal gland at night. {ECO:0000269|PubMed:17728245}.
CC   -!- INDUCTION: Exhibits night/day variations with an increased expression
CC       at night in the pineal gland. {ECO:0000269|PubMed:17728245}.
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DR   EMBL; J05018; AAA37600.1; -; mRNA.
DR   EMBL; AC125268; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS35788.1; -.
DR   PIR; A34342; A34342.
DR   RefSeq; NP_034314.2; NM_010184.2.
DR   AlphaFoldDB; P20489; -.
DR   SMR; P20489; -.
DR   STRING; 10090.ENSMUSP00000056882; -.
DR   GlyGen; P20489; 6 sites.
DR   iPTMnet; P20489; -.
DR   PhosphoSitePlus; P20489; -.
DR   PaxDb; P20489; -.
DR   PRIDE; P20489; -.
DR   ABCD; P20489; 18 sequenced antibodies.
DR   Antibodypedia; 20472; 692 antibodies from 38 providers.
DR   DNASU; 14125; -.
DR   Ensembl; ENSMUST00000049706; ENSMUSP00000056882; ENSMUSG00000005339.
DR   GeneID; 14125; -.
DR   KEGG; mmu:14125; -.
DR   UCSC; uc007dre.2; mouse.
DR   CTD; 2205; -.
DR   MGI; MGI:95494; Fcer1a.
DR   VEuPathDB; HostDB:ENSMUSG00000005339; -.
DR   eggNOG; ENOG502RTXR; Eukaryota.
DR   GeneTree; ENSGT01050000244808; -.
DR   InParanoid; P20489; -.
DR   OMA; IRCHSWK; -.
DR   OrthoDB; 866496at2759; -.
DR   PhylomeDB; P20489; -.
DR   TreeFam; TF335097; -.
DR   Reactome; R-MMU-2454202; Fc epsilon receptor (FCERI) signaling.
DR   Reactome; R-MMU-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
DR   Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
DR   Reactome; R-MMU-2871809; FCERI mediated Ca+2 mobilization.
DR   Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR   BioGRID-ORCS; 14125; 2 hits in 75 CRISPR screens.
DR   PRO; PR:P20489; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; P20489; protein.
DR   Bgee; ENSMUSG00000005339; Expressed in granulocyte and 23 other tissues.
DR   ExpressionAtlas; P20489; baseline and differential.
DR   Genevisible; P20489; MM.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR   GO; GO:0045121; C:membrane raft; TAS:MGI.
DR   GO; GO:0019863; F:IgE binding; IDA:MGI.
DR   GO; GO:0019767; F:IgE receptor activity; IDA:MGI.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0019722; P:calcium-mediated signaling; IDA:MGI.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:MGI.
DR   GO; GO:0051649; P:establishment of localization in cell; IDA:MGI.
DR   GO; GO:0019370; P:leukotriene biosynthetic process; IDA:MGI.
DR   GO; GO:0043303; P:mast cell degranulation; IDA:MGI.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
DR   GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IDA:MGI.
DR   GO; GO:0032725; P:positive regulation of granulocyte macrophage colony-stimulating factor production; IDA:MGI.
DR   GO; GO:0032752; P:positive regulation of interleukin-3 production; IDA:MGI.
DR   GO; GO:0043507; P:positive regulation of JUN kinase activity; IDA:MGI.
DR   GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:MGI.
DR   GO; GO:0032765; P:positive regulation of mast cell cytokine production; IDA:MGI.
DR   GO; GO:0043306; P:positive regulation of mast cell degranulation; IDA:MGI.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:MGI.
DR   GO; GO:0001812; P:positive regulation of type I hypersensitivity; IMP:MGI.
DR   GO; GO:0050776; P:regulation of immune response; IBA:GO_Central.
DR   GO; GO:0001820; P:serotonin secretion; IDA:MGI.
DR   GO; GO:0007165; P:signal transduction; IDA:MGI.
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   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; IgE-binding protein;
KW   Immunoglobulin domain; Membrane; Receptor; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..23
FT   CHAIN           24..250
FT                   /note="High affinity immunoglobulin epsilon receptor
FT                   subunit alpha"
FT                   /id="PRO_0000015162"
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..250
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          28..104
FT                   /note="Ig-like 1"
FT   DOMAIN          114..181
FT                   /note="Ig-like 2"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        152
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..92
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        131..174
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   CONFLICT        121
FT                   /note="V -> I (in Ref. 1; AAA37600)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        182
FT                   /note="K -> E (in Ref. 1; AAA37600)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   250 AA;  28657 MW;  DDC9E2AD2CF42C54 CRC64;
     MVTGRSAQLC LALLFMSLDV ILTATEKSVL TLDPPWIRIF TGEKVTLSCY GNNHLQMNST
     TKWIHNGTVS EVNSSHLVIV SATVQDSGKY ICQKQGLFKS KPVYLNVTQD WLLLQTSADM
     VLVHGSFDIR CHGWKNWNVR KVIYYRNDHA FNYSYESPVS IREATLNDSG TYHCKGYLRQ
     VKYESDKFRI AVVKAYKCKY YWLQLIFPLL VAILFAVDTG LLLSTEEQFK SVLEIQKTGK
     YKKVETELLT
 
 
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