PILRB_MOUSE
ID PILRB_MOUSE Reviewed; 224 AA.
AC Q2YFS2;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Paired immunoglobulin-like type 2 receptor beta;
DE AltName: Full=Activating receptor PILR-beta;
DE AltName: Full=Cell surface receptor FDFACT;
DE Flags: Precursor;
GN Name=Pilrb; Synonyms=Fdfact, Pilrb1;
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], FUNCTION, INTERACTION WITH CD99, AND TISSUE
RP SPECIFICITY.
RX PubMed=14970179; DOI=10.1084/jem.20031885;
RA Shiratori I., Ogasawara K., Saito T., Lanier L.L., Arase H.;
RT "Activation of natural killer cells and dendritic cells upon recognition of
RT a novel CD99-like ligand by paired immunoglobulin-like type 2 receptor.";
RL J. Exp. Med. 199:525-533(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bates E.E.;
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RA Wilson M.D., McKinnel L., Danby A., Schnupf P., Hunt P., Martindale D.,
RA Koop B.F.;
RT "Comparative genomic analysis of the paired immunoglobin-like receptor
RT locus at 7q22: duplications, conversions, inversions and the birth of new
RT genes.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Paired receptors consist of highly related activating and
CC inhibitory receptors and are widely involved in the regulation of the
CC immune system. PILRB is thought to act as a cellular signaling
CC activating receptor that associates with ITAM-bearing adapter molecules
CC on the cell surface. Seems to associate with DAP12 and is a receptor
CC for CD99. May be involved in target cell recognition by natural killer
CC cells and in activation of dendritic cells.
CC {ECO:0000269|PubMed:14970179}.
CC -!- SUBUNIT: Interacts with CD99. Probably associates with DAP12.
CC {ECO:0000269|PubMed:14970179}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in spleen,
CC liver and lung. Predominantly expressed by natural killer cells,
CC macrophages, and granulocytes and dendritic cells (BM-DC).
CC {ECO:0000269|PubMed:14970179}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC19332.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB122024; BAD12395.2; -; mRNA.
DR EMBL; AJ400847; CAC19332.1; ALT_INIT; mRNA.
DR EMBL; AY823670; AAX39495.1; -; Genomic_DNA.
DR CCDS; CCDS51675.1; -.
DR RefSeq; NP_573472.2; NM_133209.2.
DR AlphaFoldDB; Q2YFS2; -.
DR SMR; Q2YFS2; -.
DR IntAct; Q2YFS2; 1.
DR STRING; 10090.ENSMUSP00000106606; -.
DR GlyGen; Q2YFS2; 3 sites.
DR MaxQB; Q2YFS2; -.
DR PaxDb; Q2YFS2; -.
DR PRIDE; Q2YFS2; -.
DR ABCD; Q2YFS2; 22 sequenced antibodies.
DR DNASU; 170741; -.
DR Ensembl; ENSMUST00000110978; ENSMUSP00000106606; ENSMUSG00000066684.
DR GeneID; 170741; -.
DR KEGG; mmu:170741; -.
DR UCSC; uc009aec.2; mouse.
DR CTD; 170741; -.
DR MGI; MGI:2450532; Pilrb1.
DR VEuPathDB; HostDB:ENSMUSG00000066684; -.
DR eggNOG; ENOG502SUHR; Eukaryota.
DR GeneTree; ENSGT00390000008831; -.
DR HOGENOM; CLU_070832_0_0_1; -.
DR InParanoid; Q2YFS2; -.
DR OMA; NCFSEAP; -.
DR OrthoDB; 1325787at2759; -.
DR PhylomeDB; Q2YFS2; -.
DR TreeFam; TF338478; -.
DR BioGRID-ORCS; 170741; 0 hits in 41 CRISPR screens.
DR PRO; PR:Q2YFS2; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q2YFS2; protein.
DR Bgee; ENSMUSG00000066684; Expressed in granulocyte and 32 other tissues.
DR ExpressionAtlas; Q2YFS2; baseline and differential.
DR Genevisible; Q2YFS2; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0042288; F:MHC class I protein binding; IDA:UniProtKB.
DR GO; GO:0001773; P:myeloid dendritic cell activation; IDA:MGI.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IMP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..224
FT /note="Paired immunoglobulin-like type 2 receptor beta"
FT /id="PRO_0000226824"
FT TOPO_DOM 29..195
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 224 AA; 25200 MW; 0BB15D5E0A6D08CE CRC64;
MALLISLPGG TPAMAQVLLL LSSGCLHAGN SERYNRKNGF GVNQPERCSG VQGGSIDIPF
SFYFPWKLAK DPQMSIAWKW KDFHGEVIYN SSLPFIHEHF KGRLILNWTQ GQTSGVLRIL
NLKESDQAQY FSRVNLQSTE GMKLWQSIPG TQLNVTQALN TTMRSPFIVT SEFTTAGLEH
TSDQRNPSLM NLGAMVTMLL AKVLVIVLVY GWMIFLRWKQ RPAH
