LRB4A_MOUSE
ID LRB4A_MOUSE Reviewed; 335 AA.
AC Q64281; Q64312;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Leukocyte immunoglobulin-like receptor subfamily B member 4A {ECO:0000312|MGI:MGI:102701};
DE AltName: Full=Mast cell surface glycoprotein Gp49B;
DE AltName: CD_antigen=CD85k;
DE Flags: Precursor;
GN Name=Lilrb4a {ECO:0000312|MGI:MGI:102701};
GN Synonyms=Gp49b {ECO:0000303|PubMed:8132564};
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] (ISOFORMS 1 AND 2).
RC STRAIN=BALB/cJ, and C3H/HeJ; TISSUE=Bone marrow;
RX PubMed=8132564; DOI=10.1016/s0021-9258(17)37207-1;
RA Castells M.C., Wu X., Arm J.P., Austen K.F., Katz H.R.;
RT "Cloning of the gp49B gene of the immunoglobulin superfamily and
RT demonstration that one of its two products is an early-expressed mast cell
RT surface protein originally described as gp49.";
RL J. Biol. Chem. 269:8393-8401(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND ITIM MOTIFS.
RX PubMed=8855262; DOI=10.1073/pnas.93.20.10809;
RA Katz H.R., Vivier E., Castells M.C., McCormick M.J., Chambers J.M.,
RA Austen K.F.;
RT "Mouse mast cell gp49B1 contains two immunoreceptor tyrosine-based
RT inhibition motifs and suppresses mast cell activation when coligated with
RT the high-affinity Fc receptor for IgE.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:10809-10814(1996).
RN [4]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=9338594; DOI=10.1046/j.1440-169x.1997.t01-4-00006.x;
RA Matsumoto Y., Handa S., Taki T.;
RT "gp49B1, an inhibitory signaling receptor gene of hematopoietic cells, is
RT induced by leukemia inhibitory factor in the uterine endometrium just
RT before implantation.";
RL Dev. Growth Differ. 39:591-597(1997).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=8977169;
RA Rojo S., Burshtyn D.N., Long E.O., Wagtmann N.;
RT "Type I transmembrane receptor with inhibitory function in mouse mast cells
RT and NK cells.";
RL J. Immunol. 158:9-12(1997).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=8977170;
RA Wang L.L., Mehta I.K., LeBlanc P.A., Yokoyama W.M.;
RT "Mouse natural killer cells express gp49B1, a structural homologue of human
RT killer inhibitory receptors.";
RL J. Immunol. 158:13-17(1997).
RN [7]
RP ITIM MOTIFS.
RX PubMed=9422771; DOI=10.1074/jbc.273.2.1070;
RA Kuroiwa A., Yamashita Y., Inui M., Yuasa T., Ono M., Nagabukuro A.,
RA Matsuda Y., Takai T.;
RT "Association of tyrosine phosphatases SHP-1 and SHP-2, inositol 5-
RT phosphatase SHIP with gp49B1, and chromosomal assignment of the gene.";
RL J. Biol. Chem. 273:1070-1074(1998).
RN [8]
RP FUNCTION, INTERACTION WITH PTPN6 AND PTPN11, PHOSPHORYLATION, AND
RP MUTAGENESIS OF TYR-300 AND TYR-322.
RX PubMed=10026201; DOI=10.1074/jbc.274.9.5791;
RA Lu-Kuo J.M., Joyal D.M., Austen K.F., Katz H.R.;
RT "gp49B1 inhibits IgE-initiated mast cell activation through both
RT immunoreceptor tyrosine-based inhibitory motifs, recruitment of src
RT homology 2 domain-containing phosphatase-1, and suppression of early and
RT late calcium mobilization.";
RL J. Biol. Chem. 274:5791-5796(1999).
RN [9]
RP INTERACTION WITH PTPN6, ITIM MOTIFS, AND PHOSPHORYLATION.
RX PubMed=9973385;
RA Wang L.L., Blasioli J., Plas D.R., Thomas M.L., Yokoyama W.M.;
RT "Specificity of the SH2 domains of SHP-1 in the interaction with the
RT immunoreceptor tyrosine-based inhibitory motif-bearing receptor gp49B.";
RL J. Immunol. 162:1318-1323(1999).
RN [10]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=10982834; DOI=10.1128/mcb.20.19.7178-7182.2000;
RA Rojo S., Stebbins C.C., Peterson M.E., Dombrowicz D., Wagtmann N.,
RA Long E.O.;
RT "Natural killer cells and mast cells from gp49B null mutant mice are
RT functional.";
RL Mol. Cell. Biol. 20:7178-7182(2000).
RN [11]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=11457897; DOI=10.1084/jem.194.2.227;
RA Daheshia M., Friend D.S., Grusby M.J., Austen K.F., Katz H.R.;
RT "Increased severity of local and systemic anaphylactic reactions in gp49B1-
RT deficient mice.";
RL J. Exp. Med. 194:227-234(2001).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11323698; DOI=10.1038/87749;
RA Castells M.C., Klickstein L.B., Hassani K., Cumplido J.A., Lacouture M.E.,
RA Austen K.F., Katz H.R.;
RT "gp49B1-alpha(v)beta3 interaction inhibits antigen-induced mast cell
RT activation.";
RL Nat. Immunol. 2:436-442(2001).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12884301; DOI=10.1002/eji.200323978;
RA Feldweg A.M., Friend D.S., Zhou J.S., Kanaoka Y., Daheshia M., Li L.,
RA Austen K.F., Katz H.R.;
RT "gp49B1 suppresses stem cell factor-induced mast cell activation-secretion
RT and attendant inflammation in vivo.";
RL Eur. J. Immunol. 33:2262-2268(2003).
RN [14]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14557414; DOI=10.1084/jem.20030906;
RA Zhou J.S., Friend D.S., Feldweg A.M., Daheshia M., Li L., Austen K.F.,
RA Katz H.R.;
RT "Prevention of lipopolysaccharide-induced microangiopathy by gp49B1:
RT evidence for an important role for gp49B1 expression on neutrophils.";
RL J. Exp. Med. 198:1243-1251(2003).
RN [15]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=12682239; DOI=10.4049/jimmunol.170.8.4095;
RA Gu X., Laouar A., Wan J., Daheshia M., Lieberman J., Yokoyama W.M.,
RA Katz H.R., Manjunath N.;
RT "The gp49B1 inhibitory receptor regulates the IFN-gamma responses of T
RT cells and NK cells.";
RL J. Immunol. 170:4095-4101(2003).
RN [16]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17761953; DOI=10.1189/jlb.1106667;
RA Norris H.H., Peterson M.E., Stebbins C.C., McConchie B.W., Bundoc V.G.,
RA Trivedi S., Hodges M.G., Anthony R.M., Urban J.F. Jr., Long E.O.,
RA Keane-Myers A.M.;
RT "Inhibitory receptor gp49B regulates eosinophil infiltration during
RT allergic inflammation.";
RL J. Leukoc. Biol. 82:1531-1541(2007).
RN [17]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18792399; DOI=10.1002/eji.200737550;
RA Kasai S., Inui M., Nakamura K., Kakizaki Y., Endo S., Nakamura A., Ito S.,
RA Takai T.;
RT "A novel regulatory role of gp49B on dendritic cells in T-cell priming.";
RL Eur. J. Immunol. 38:2426-2437(2008).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [19]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=24935931; DOI=10.4049/jimmunol.1302772;
RA Fukao S., Haniuda K., Nojima T., Takai T., Kitamura D.;
RT "gp49B-mediated negative regulation of antibody production by memory and
RT marginal zone B cells.";
RL J. Immunol. 193:635-644(2014).
RN [20]
RP FUNCTION.
RX PubMed=34089617; DOI=10.1093/intimm/dxab028;
RA Su M.T., Inui M., Wong Y.L., Takahashi M., Sugahara-Tobinai A., Ono K.,
RA Miyamoto S., Murakami K., Itoh-Nakadai A., Kezuka D., Itoi S., Endo S.,
RA Hirayasu K., Arase H., Takai T.;
RT "Blockade of checkpoint ILT3/LILRB4/gp49B binding to fibronectin
RT ameliorates autoimmune disease in BXSB/Yaa mice.";
RL Int. Immunol. 33:447-458(2021).
CC -!- FUNCTION: Inhibitory receptor involved in the down-regulation of the
CC immune response (PubMed:10026201, PubMed:24935931). Receptor for FN1
CC (PubMed:34089617). Receptor for integrin ITGAV/ITGB3 (PubMed:11323698).
CC Inhibits IgE-mediated mast cell activation, at least in part through
CC interaction with ITGAV/ITGB3 (PubMed:8855262, PubMed:10026201,
CC PubMed:11457897, PubMed:11323698). Also inhibits KITLG/SCF-mediated
CC mast cell activation (PubMed:12884301). Through interaction with
CC ITGAV/ITGB3, inhibits antibody production by memory and marginal zone B
CC cells, probably by suppressing their differentiation into plasma cells
CC (PubMed:24935931). Inhibits IFNG production by CD8 T cells, CD4 T cells
CC and natural killer cells (PubMed:12682239). Inhibits antigen
CC presentation by dendritic cells to T cells, preventing T cell
CC activation (PubMed:18792399). Inhibits lipopolysaccharide-mediated
CC neutrophil-dependent vascular injury (PubMed:14557414). Suppresses the
CC allergic inflammatory response by inhibiting infiltration of
CC neutrophils and eosinophils and preventing mast cell degranulation
CC (PubMed:17761953). Inhibits lysis by natural killer cells
CC (PubMed:8977169). {ECO:0000269|PubMed:10026201,
CC ECO:0000269|PubMed:11323698, ECO:0000269|PubMed:11457897,
CC ECO:0000269|PubMed:12682239, ECO:0000269|PubMed:12884301,
CC ECO:0000269|PubMed:14557414, ECO:0000269|PubMed:17761953,
CC ECO:0000269|PubMed:18792399, ECO:0000269|PubMed:24935931,
CC ECO:0000269|PubMed:34089617, ECO:0000269|PubMed:8855262,
CC ECO:0000269|PubMed:8977169}.
CC -!- SUBUNIT: Interacts (when tyrosine phosphorylated) with SH2 domain-
CC containing phosphatases PTPN6/SHP-1 and PTPN11/SHP-2; interaction with
CC PTPN6 enhances inhibition of mast cell activation.
CC {ECO:0000269|PubMed:10026201, ECO:0000269|PubMed:9973385}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10982834,
CC ECO:0000269|PubMed:11323698, ECO:0000269|PubMed:8855262,
CC ECO:0000269|PubMed:8977169}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=GP49B1 {ECO:0000303|PubMed:8132564};
CC IsoId=Q64281-1; Sequence=Displayed;
CC Name=2; Synonyms=GP49B2 {ECO:0000303|PubMed:8132564};
CC IsoId=Q64281-2; Sequence=VSP_002510, VSP_002511;
CC -!- TISSUE SPECIFICITY: Expressed on mast cells and natural killer cells
CC (at protein level) (PubMed:8977169, PubMed:8977170, PubMed:11457897).
CC Expressed on neutrophils (at protein level) (PubMed:14557414).
CC Expressed on eosinophils (at protein level) (PubMed:17761953).
CC Expressed on dendritic cells (at protein level) (PubMed:18792399).
CC Expressed on memory and marginal zone B cells (at protein level)
CC (PubMed:24935931). Expressed on CD8 T cells (at protein level)
CC (PubMed:12682239). Expressed in the uterus of pregnant mice where it is
CC detected at day 4.0 of pregnancy with levels dropping at day 4.5
CC (PubMed:9338594). Highly expressed in the luminal epithelium of uterine
CC endometrium with lower levels in the glandular epithelium
CC (PubMed:9338594). {ECO:0000269|PubMed:11457897,
CC ECO:0000269|PubMed:12682239, ECO:0000269|PubMed:14557414,
CC ECO:0000269|PubMed:17761953, ECO:0000269|PubMed:18792399,
CC ECO:0000269|PubMed:24935931, ECO:0000269|PubMed:8977169,
CC ECO:0000269|PubMed:8977170, ECO:0000269|PubMed:9338594}.
CC -!- INDUCTION: Induced by lipopolysaccharide on neutrophils (at protein
CC level) (PubMed:14557414). Induced by IL6 and LIF (PubMed:9338594).
CC {ECO:0000269|PubMed:14557414, ECO:0000269|PubMed:9338594}.
CC -!- DOMAIN: Contains 2 copies of a cytoplasmic motif that is referred to as
CC the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is
CC involved in modulation of cellular responses. The phosphorylated ITIM
CC motif can bind the SH2 domain of several SH2-containing phosphatases.
CC {ECO:0000269|PubMed:8855262, ECO:0000269|PubMed:9422771,
CC ECO:0000269|PubMed:9973385}.
CC -!- PTM: Tyrosine phosphorylated. {ECO:0000269|PubMed:10026201,
CC ECO:0000269|PubMed:9973385}.
CC -!- DISRUPTION PHENOTYPE: No effect on fertility or litter size
CC (PubMed:10982834, PubMed:11457897). Normal development of mast cells
CC and natural killer cells (PubMed:10982834). Increased severity of local
CC and systemic anaphylactic reactions (PubMed:11457897). Significantly
CC increased sensitivity to IgE-dependent passive cutaneous anaphylaxis
CC with greater tissue swelling and mast cell degranulation, and
CC significantly greater and faster death rate in active systemic
CC anaphylaxis (PubMed:11457897). However, another study found no effect
CC on mast cell activity with no increase in mast cell degranulation
CC (PubMed:10982834). Macroscopic hemorrhages following intradermal
CC injection of E.coli lipopolysaccharide with increased neutrophil
CC numbers around the site of injection (PubMed:14557414). Normal B cell
CC development and memory B cell formation but increased production by
CC marginal zone and memory B cells of IgM after a primary immunization
CC and of IgM, IgG1 and IgE after a secondary immunization
CC (PubMed:24935931). Reduced ERK activation and reduced Prdm1/Blimp1
CC expression, indicative of suppression of plasma cell differentiation
CC (PubMed:24935931). No effect on antigen uptake or cytokine production
CC by dendritic cells but dendritic cells show enhanced antigen
CC presentation to T cells and induce increased T cell stimulation
CC (PubMed:18792399). Increased neutrophilia, eosinophilia and mast cell
CC degranulation following ocular ragweed (RW) sensitization and
CC challenge, and increased lung inflammation following RW sensitization
CC and challenge (PubMed:17761953). Increased Kitlg/SCF-induced mast cell
CC degranulation and tissue swelling (PubMed:12884301). Enhanced IFNG
CC production by CD8 T cells, CD4 T cells and NK cells following viral
CC infection (PubMed:12682239). {ECO:0000269|PubMed:10982834,
CC ECO:0000269|PubMed:11457897, ECO:0000269|PubMed:12682239,
CC ECO:0000269|PubMed:12884301, ECO:0000269|PubMed:14557414,
CC ECO:0000269|PubMed:17761953, ECO:0000269|PubMed:18792399,
CC ECO:0000269|PubMed:24935931}.
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DR EMBL; U05266; AAA17799.1; -; mRNA.
DR EMBL; U05265; AAA17797.1; -; Unassigned_DNA.
DR EMBL; U05265; AAA17798.1; -; Unassigned_DNA.
DR EMBL; U05264; AAA17796.1; -; mRNA.
DR EMBL; BC006591; AAH06591.1; -; mRNA.
DR CCDS; CCDS23832.1; -. [Q64281-1]
DR PIR; A53434; A53434.
DR PIR; B53434; B53434.
DR RefSeq; NP_038560.1; NM_013532.3. [Q64281-1]
DR AlphaFoldDB; Q64281; -.
DR SMR; Q64281; -.
DR BioGRID; 200008; 2.
DR DIP; DIP-46122N; -.
DR IntAct; Q64281; 2.
DR STRING; 10090.ENSMUSP00000101121; -.
DR MEROPS; I43.951; -.
DR GlyGen; Q64281; 2 sites.
DR iPTMnet; Q64281; -.
DR PhosphoSitePlus; Q64281; -.
DR EPD; Q64281; -.
DR MaxQB; Q64281; -.
DR PaxDb; Q64281; -.
DR PeptideAtlas; Q64281; -.
DR PRIDE; Q64281; -.
DR ProteomicsDB; 290039; -. [Q64281-2]
DR DNASU; 14728; -.
DR Ensembl; ENSMUST00000078778; ENSMUSP00000077833; ENSMUSG00000112148. [Q64281-1]
DR Ensembl; ENSMUST00000217706; ENSMUSP00000151978; ENSMUSG00000062593. [Q64281-2]
DR Ensembl; ENSMUST00000219696; ENSMUSP00000151486; ENSMUSG00000062593. [Q64281-1]
DR Ensembl; ENSMUST00000220182; ENSMUSP00000151694; ENSMUSG00000112148. [Q64281-2]
DR GeneID; 14728; -.
DR KEGG; mmu:14728; -.
DR UCSC; uc007far.2; mouse. [Q64281-1]
DR UCSC; uc011xdq.2; mouse. [Q64281-2]
DR CTD; 14728; -.
DR MGI; MGI:102701; Lilrb4a.
DR VEuPathDB; HostDB:ENSMUSG00000062593; -.
DR VEuPathDB; HostDB:ENSMUSG00000112148; -.
DR eggNOG; ENOG502RU0A; Eukaryota.
DR GeneTree; ENSGT01000000214458; -.
DR HOGENOM; CLU_021100_0_0_1; -.
DR InParanoid; Q64281; -.
DR OMA; DIMITAF; -.
DR OrthoDB; 1000446at2759; -.
DR PhylomeDB; Q64281; -.
DR TreeFam; TF336644; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 14728; 3 hits in 41 CRISPR screens.
DR PRO; PR:Q64281; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q64281; protein.
DR Bgee; ENSMUSG00000062593; Expressed in granulocyte and 35 other tissues.
DR ExpressionAtlas; Q64281; baseline and differential.
DR Genevisible; Q64281; MM.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0034185; F:apolipoprotein binding; ISO:MGI.
DR GO; GO:0001968; F:fibronectin binding; IDA:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IDA:ARUK-UCL.
DR GO; GO:0019902; F:phosphatase binding; IPI:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR GO; GO:0030547; F:signaling receptor inhibitor activity; ISO:MGI.
DR GO; GO:0030293; F:transmembrane receptor protein tyrosine kinase inhibitor activity; ISO:MGI.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0007596; P:blood coagulation; IMP:MGI.
DR GO; GO:0035739; P:CD4-positive, alpha-beta T cell proliferation; IMP:MGI.
DR GO; GO:0035740; P:CD8-positive, alpha-beta T cell proliferation; IMP:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:MGI.
DR GO; GO:0002774; P:Fc receptor mediated inhibitory signaling pathway; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR GO; GO:0002437; P:inflammatory response to antigenic stimulus; IMP:MGI.
DR GO; GO:0046007; P:negative regulation of activated T cell proliferation; ISO:MGI.
DR GO; GO:0032682; P:negative regulation of chemokine production; ISO:MGI.
DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; ISO:MGI.
DR GO; GO:0045584; P:negative regulation of cytotoxic T cell differentiation; ISO:MGI.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0002638; P:negative regulation of immunoglobulin production; IMP:UniProtKB.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; ISO:MGI.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; ISO:MGI.
DR GO; GO:0032693; P:negative regulation of interleukin-10 production; ISO:MGI.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; ISO:MGI.
DR GO; GO:0032714; P:negative regulation of interleukin-5 production; ISO:MGI.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; ISO:MGI.
DR GO; GO:0071659; P:negative regulation of IP-10 production; ISO:MGI.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; ISO:MGI.
DR GO; GO:0033004; P:negative regulation of mast cell activation; IMP:UniProtKB.
DR GO; GO:0033007; P:negative regulation of mast cell activation involved in immune response; IDA:UniProtKB.
DR GO; GO:1902894; P:negative regulation of miRNA transcription; ISO:MGI.
DR GO; GO:0150102; P:negative regulation of monocyte activation; IDA:UniProtKB.
DR GO; GO:0032815; P:negative regulation of natural killer cell activation; IDA:UniProtKB.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; ISO:MGI.
DR GO; GO:1900099; P:negative regulation of plasma cell differentiation; IMP:UniProtKB.
DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; ISO:MGI.
DR GO; GO:0061099; P:negative regulation of protein tyrosine kinase activity; ISO:MGI.
DR GO; GO:2000272; P:negative regulation of signaling receptor activity; ISO:MGI.
DR GO; GO:2000524; P:negative regulation of T cell costimulation; ISO:MGI.
DR GO; GO:0002725; P:negative regulation of T cell cytokine production; ISO:MGI.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISO:MGI.
DR GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; ISO:MGI.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:MGI.
DR GO; GO:0001780; P:neutrophil homeostasis; IMP:MGI.
DR GO; GO:0043378; P:positive regulation of CD8-positive, alpha-beta T cell differentiation; ISO:MGI.
DR GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; ISO:MGI.
DR GO; GO:0002669; P:positive regulation of T cell anergy; ISO:MGI.
DR GO; GO:0031623; P:receptor internalization; ISO:MGI.
DR GO; GO:0009991; P:response to extracellular stimulus; IMP:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
DR GO; GO:0009624; P:response to nematode; IMP:MGI.
DR GO; GO:0051707; P:response to other organism; IMP:MGI.
DR GO; GO:0009611; P:response to wounding; IMP:MGI.
DR GO; GO:0002507; P:tolerance induction; ISO:MGI.
DR GO; GO:0042092; P:type 2 immune response; IMP: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 Pfam; PF13895; Ig_2; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunity; Immunoglobulin domain; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..335
FT /note="Leukocyte immunoglobulin-like receptor subfamily B
FT member 4A"
FT /id="PRO_0000014824"
FT TOPO_DOM 24..238
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..335
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 42..125
FT /note="Ig-like C2-type 1"
FT DOMAIN 124..212
FT /note="Ig-like C2-type 2"
FT MOTIF 298..303
FT /note="ITIM motif 1"
FT MOTIF 320..325
FT /note="ITIM motif 2"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 144..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 232
FT /note="G -> D (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8132564"
FT /id="VSP_002510"
FT VAR_SEQ 233..271
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8132564"
FT /id="VSP_002511"
FT MUTAGEN 300
FT /note="Y->F: Partially suppresses inhibition of mast cell
FT activation. Abolishes inhibition of mast cell activation;
FT when associated with F-322."
FT /evidence="ECO:0000269|PubMed:10026201"
FT MUTAGEN 322
FT /note="Y->F: Partially suppresses inhibition of mast cell
FT activation. Abolishes inhibition of mast cell activation;
FT when associated with F-300."
FT /evidence="ECO:0000269|PubMed:10026201"
SQ SEQUENCE 335 AA; 37544 MW; 6005186D524E7876 CRC64;
MIAMLTVLLY LGLILEPRTA VQAGHLPKPI IWAEPGSVIA AYTSVITWCQ GSWEAQYYHL
YKEKSVNPWD TQVPLETRNK AKFNIPSMTT SYAGIYKCYY ESAAGFSEHS DAMELVMTGA
YENPSLSVYP SSNVTSGVSI SFSCSSSIVF GRFILIQEGK HGLSWTLDSQ HQANQPSYAT
FVLDAVTPNH NGTFRCYGYF RNEPQVWSKP SNSLDLMISE TKDQSSTPTE DGLETYQKIL
IGVLVSFLLL FFLLLFLILI GYQYGHKKKA NASVKNTQSE NNAELNSWNP QNEDPQGIVY
AQVKPSRLQK DTACKETQDV TYAQLCIRTQ EQNNS
