LRB4B_MOUSE
ID LRB4B_MOUSE Reviewed; 303 AA.
AC Q61450; Q549E3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Leukocyte immunoglobulin-like receptor subfamily B member 4B {ECO:0000312|MGI:MGI:102702};
DE Short=Mast cell surface glycoprotein Gp49A;
DE Flags: Precursor;
GN Name=Lilrb4b {ECO:0000312|MGI:MGI:102702};
GN Synonyms=Gp49 {ECO:0000303|PubMed:1714901},
GN Gp49a {ECO:0000303|PubMed:10630292};
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], AND PROTEIN SEQUENCE OF 24-45.
RC STRAIN=BALB/cJ; TISSUE=Mast cell;
RX PubMed=1714901; DOI=10.1016/s0021-9258(18)98502-9;
RA Arm J.P., Gurish M.F., Reynolds D.S., Scott H.C., Gartner C.S.,
RA Austen K.F., Katz H.R.;
RT "Molecular cloning of gp49, a cell-surface antigen that is preferentially
RT expressed by mouse mast cell progenitors and is a new member of the
RT immunoglobulin superfamily.";
RL J. Biol. Chem. 266:15966-15973(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DOMAIN.
RC STRAIN=BALB/cJ;
RX PubMed=10630292; DOI=10.1007/s002510050604;
RA McCormick M.J., Castells M.C., Austen K.F., Katz H.R.;
RT "The gp49A gene has extensive sequence conservation with the gp49B gene and
RT provides gp49A protein, a unique member of a large family of activating and
RT inhibitory receptors of the immunoglobulin superfamily.";
RL Immunogenetics 50:286-294(1999).
RN [3]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-226.
RX PubMed=11046024; DOI=10.4049/jimmunol.165.9.4970;
RA Lee K.H., Ono M., Inui M., Yuasa T., Takai T.;
RT "Stimulatory function of gp49A, a murine Ig-like receptor, in rat
RT basophilic leukemia cells.";
RL J. Immunol. 165:4970-4977(2000).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: Plays a role in mast cell activation.
CC {ECO:0000269|PubMed:11046024}.
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000269|PubMed:11046024}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10630292,
CC ECO:0000269|PubMed:10982834, ECO:0000269|PubMed:11046024}; Single-pass
CC type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed on mast cells (at protein level)
CC (PubMed:10630292, PubMed:10982834). Also expressed at much lower levels
CC on natural killer cells (at protein level) (PubMed:10982834).
CC {ECO:0000269|PubMed:10630292, ECO:0000269|PubMed:10982834}.
CC -!- DOMAIN: In contrast to the related Lilrb4a protein, does not contain
CC any copies of a cytoplasmic motif that is referred to as the
CC immunoreceptor tyrosine-based inhibitor motif (ITIM).
CC {ECO:0000269|PubMed:10630292}.
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DR EMBL; M65027; AAA37479.1; -; mRNA.
DR EMBL; AF141314; AAF32156.2; -; Genomic_DNA.
DR CCDS; CCDS23831.1; -.
DR PIR; A40807; A40807.
DR RefSeq; NP_032173.1; NM_008147.2.
DR AlphaFoldDB; Q61450; -.
DR SMR; Q61450; -.
DR STRING; 10090.ENSMUSP00000099958; -.
DR GlyGen; Q61450; 3 sites.
DR MaxQB; Q61450; -.
DR PaxDb; Q61450; -.
DR PRIDE; Q61450; -.
DR ProteomicsDB; 271032; -.
DR DNASU; 14727; -.
DR Ensembl; ENSMUST00000102894; ENSMUSP00000099958; ENSMUSG00000112023.
DR GeneID; 14727; -.
DR KEGG; mmu:14727; -.
DR UCSC; uc007fam.2; mouse.
DR CTD; 14727; -.
DR MGI; MGI:102702; Lilrb4b.
DR VEuPathDB; HostDB:ENSMUSG00000112023; -.
DR eggNOG; ENOG502RU0A; Eukaryota.
DR GeneTree; ENSGT01000000214458; -.
DR HOGENOM; CLU_021100_0_0_1; -.
DR InParanoid; Q61450; -.
DR OMA; PLENRNK; -.
DR OrthoDB; 1000446at2759; -.
DR PhylomeDB; Q61450; -.
DR TreeFam; TF336644; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 14727; 0 hits in 38 CRISPR screens.
DR PRO; PR:Q61450; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q61450; protein.
DR Bgee; ENSMUSG00000112023; Expressed in granulocyte and 45 other tissues.
DR ExpressionAtlas; Q61450; baseline and differential.
DR Genevisible; Q61450; MM.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
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; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
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:0002774; P:Fc receptor mediated inhibitory signaling pathway; ISO:MGI.
DR GO; GO:0045576; P:mast cell activation; IDA:UniProtKB.
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: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:1902894; P:negative regulation of miRNA transcription; ISO:MGI.
DR GO; GO:0150102; P:negative regulation of monocyte activation; ISO:MGI.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; ISO:MGI.
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: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:0002507; P:tolerance induction; ISO: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; IPR013151; Immunoglobulin.
DR Pfam; PF00047; ig; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunity; Immunoglobulin domain; Membrane; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:1714901"
FT CHAIN 24..303
FT /note="Leukocyte immunoglobulin-like receptor subfamily B
FT member 4B"
FT /id="PRO_0000014767"
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..303
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 42..123
FT /note="Ig-like C2-type 1"
FT DOMAIN 124..212
FT /note="Ig-like C2-type 2"
FT REGION 275..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 MUTAGEN 226
FT /note="C->F: Abolishes mast cell activation and
FT homodimerization."
FT /evidence="ECO:0000269|PubMed:11046024"
SQ SEQUENCE 303 AA; 34194 MW; D165659BFAB9C40D CRC64;
MIAMLTVLLY LALILEPRTA VQAGHLPKPI IWAEPGSVIA AYTSVIIWCW GSWEAQYYYL
DKEKSVNPWD TEVPLENRNK TKFKIRFMTA SYAGIYNCYY KSAAGFSEHS DAMELVMTGA
YENPSLSVYP SSNVTSGVSI SFKCSSSTLF GRFILIQEGK HGLSWTLDSQ HQANQPTHAT
FVLDAVAPNH NGTFRCYGFF RNEPQVWSKP SNSLDLMISE TKEQSCTPTE DGLETYQKIL
IGVLVSFLLL FFLLLFLILI GYQCRHKNKA NASVKNTQSE DNAELNSWNP QNEDPPRELC
TPR
