LIRB3_MOUSE
ID LIRB3_MOUSE Reviewed; 841 AA.
AC P97484;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Leukocyte immunoglobulin-like receptor subfamily B member 3;
DE Short=LIR-3;
DE Short=Leukocyte immunoglobulin-like receptor 3;
DE AltName: Full=Cell-surface glycoprotein p91;
DE AltName: Full=Paired immunoglobulin-like receptor B;
DE Short=PIR-B;
DE Flags: Precursor;
GN Name=Lilrb3; Synonyms=Pirb;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=B10.A;
RX PubMed=9054430; DOI=10.1074/jbc.272.11.7320;
RA Hayami K., Fukuta D., Nishikawa Y., Yamashita Y., Inui M., Ohyama Y.,
RA Hikida M., Ohmori H., Takai T.;
RT "Molecular cloning of a novel murine cell-surface glycoprotein homologous
RT to killer cell inhibitory receptors.";
RL J. Biol. Chem. 272:7320-7327(1997).
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 FUNCTION, MUTAGENESIS OF TYR-794 AND TYR-824, INTERACTION WITH PTPN6/SHP-1
RP AND PTPN11/SHP-2, AND SUBCELLULAR LOCATION.
RX PubMed=9482905; DOI=10.1073/pnas.95.5.2446;
RA Blery M., Kubagawa H., Chen C.C., Vely F., Cooper M.D., Vivier E.;
RT "The paired Ig-like receptor PIR-B is an inhibitory receptor that recruits
RT the protein-tyrosine phosphatase SHP-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:2446-2451(1998).
RN [4]
RP FUNCTION, PHOSPHORYLATION AT TYR-794 AND TYR-824 BY LYN, MUTAGENESIS OF
RP TYR-794 AND TYR-824, INTERACTION WITH PTPN6/SHP-1 AND PTPN11/SHP-2,
RP SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=10327049; DOI=10.1038/sj.onc.1202552;
RA Maeda A., Scharenberg A.M., Tsukada S., Bolen J.B., Kinet J.P.,
RA Kurosaki T.;
RT "Paired immunoglobulin-like receptor B (PIR-B) inhibits BCR-induced
RT activation of Syk and Btk by SHP-1.";
RL Oncogene 18:2291-2297(1999).
RN [5]
RP FUNCTION, PHOSPHORYLATION BY LYN, INTERACTION WITH LYN AND PTPN6/SHP-1, AND
RP TISSUE SPECIFICITY.
RX PubMed=10611342; DOI=10.1073/pnas.96.26.15086;
RA Ho L.H., Uehara T., Chen C.C., Kubagawa H., Cooper M.D.;
RT "Constitutive tyrosine phosphorylation of the inhibitory paired Ig-like
RT receptor PIR-B.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:15086-15090(1999).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-684 AND SER-757, AND
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).
CC -!- FUNCTION: May act as receptor for class I MHC antigens. Becomes
CC activated upon coligation of LILRB3 and immune receptors, such as
CC FCGR2B and the B-cell receptor. Down-regulates antigen-induced B-cell
CC activation by recruiting phosphatases to its immunoreceptor tyrosine-
CC based inhibitor motifs (ITIM). {ECO:0000269|PubMed:10327049,
CC ECO:0000269|PubMed:10611342, ECO:0000269|PubMed:9482905}.
CC -!- SUBUNIT: Interacts with LYN, PTPN6/SHP-1 and PTPN11/SHP-2.
CC {ECO:0000269|PubMed:10327049, ECO:0000269|PubMed:10611342,
CC ECO:0000269|PubMed:9482905}.
CC -!- INTERACTION:
CC P97484; P35235: Ptpn11; NbExp=2; IntAct=EBI-15728641, EBI-397236;
CC P97484; PRO_0000000092 [P05067]: APP; Xeno; NbExp=8; IntAct=EBI-15728641, EBI-821758;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10327049,
CC ECO:0000269|PubMed:9054430, ECO:0000269|PubMed:9482905}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:10327049,
CC ECO:0000269|PubMed:9054430, ECO:0000269|PubMed:9482905}.
CC -!- TISSUE SPECIFICITY: Detected in macrophages, splenocytes and B
CC lymphocytes (at protein level). Detected in macrophages, mast cells,
CC splenocytes, peritoneal cells and natural killer cells.
CC {ECO:0000269|PubMed:10611342, ECO:0000269|PubMed:9054430}.
CC -!- DOMAIN: Contains 3 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 including PTPN6/SHP-1, resulting in the dephosphorylation of the
CC downstream protein kinases SYK and BTK. {ECO:0000269|PubMed:10327049}.
CC -!- PTM: Phosphorylated on tyrosine residues by LYN. Phosphorylation at
CC Tyr-794 and Tyr-824 is important for interaction with PTPN6/SHP-1 and
CC PTPN11/SHP-2. {ECO:0000269|PubMed:10327049,
CC ECO:0000269|PubMed:10611342}.
CC -!- MISCELLANEOUS: Belongs to the leukocyte receptor cluster (LRC) present
CC on chromosome 7.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U83172; AAB40934.1; -; mRNA.
DR EMBL; AC130680; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC171680; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS39730.1; -.
DR RefSeq; NP_035225.2; NM_011095.2.
DR AlphaFoldDB; P97484; -.
DR SMR; P97484; -.
DR DIP; DIP-59889N; -.
DR IntAct; P97484; 7.
DR STRING; 10090.ENSMUSP00000077546; -.
DR GlyGen; P97484; 2 sites.
DR iPTMnet; P97484; -.
DR PhosphoSitePlus; P97484; -.
DR MaxQB; P97484; -.
DR PaxDb; P97484; -.
DR PRIDE; P97484; -.
DR ProteomicsDB; 286209; -.
DR DNASU; 18733; -.
DR Ensembl; ENSMUST00000078451; ENSMUSP00000077546; ENSMUSG00000058818.
DR GeneID; 18733; -.
DR KEGG; mmu:18733; -.
DR UCSC; uc009ewb.2; mouse.
DR CTD; 18733; -.
DR MGI; MGI:894311; Lilrb3.
DR VEuPathDB; HostDB:ENSMUSG00000058818; -.
DR eggNOG; ENOG502RYEX; Eukaryota.
DR GeneTree; ENSGT01000000214458; -.
DR HOGENOM; CLU_021100_2_3_1; -.
DR InParanoid; P97484; -.
DR OMA; ITHMADI; -.
DR OrthoDB; 1000446at2759; -.
DR PhylomeDB; P97484; -.
DR TreeFam; TF336644; -.
DR BioGRID-ORCS; 18733; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Pirb; mouse.
DR PRO; PR:P97484; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P97484; protein.
DR Bgee; ENSMUSG00000058818; Expressed in granulocyte and 82 other tissues.
DR Genevisible; P97484; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001540; F:amyloid-beta binding; IDA:ARUK-UCL.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR GO; GO:0030107; F:HLA-A specific inhibitory MHC class I receptor activity; ISO:MGI.
DR GO; GO:0030109; F:HLA-B specific inhibitory MHC class I receptor activity; ISO:MGI.
DR GO; GO:0001791; F:IgM binding; ISO:MGI.
DR GO; GO:0032396; F:inhibitory MHC class I receptor activity; ISO:MGI.
DR GO; GO:0042288; F:MHC class I protein binding; ISO:MGI.
DR GO; GO:0032393; F:MHC class I receptor activity; ISO:MGI.
DR GO; GO:0023029; F:MHC class Ib protein binding; ISO:MGI.
DR GO; GO:0023025; F:MHC class Ib protein complex binding; ISO:MGI.
DR GO; GO:0032394; F:MHC class Ib receptor activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:ARUK-UCL.
DR GO; GO:0008157; F:protein phosphatase 1 binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:ARUK-UCL.
DR GO; GO:0042169; F:SH2 domain binding; ISO:MGI.
DR GO; GO:0001782; P:B cell homeostasis; IMP:MGI.
DR GO; GO:0019724; P:B cell mediated immunity; IMP:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IMP:MGI.
DR GO; GO:0007611; P:learning or memory; IGI:ARUK-UCL.
DR GO; GO:0043011; P:myeloid dendritic cell differentiation; IMP:MGI.
DR GO; GO:0051248; P:negative regulation of protein metabolic process; IGI:ARUK-UCL.
DR GO; GO:1900454; P:positive regulation of long-term synaptic depression; IGI:ARUK-UCL.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; IGI:ARUK-UCL.
DR GO; GO:1900271; P:regulation of long-term synaptic potentiation; IGI:ARUK-UCL.
DR Gene3D; 2.60.40.10; -; 6.
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 InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13895; Ig_2; 2.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; SSF48726; 6.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Cell membrane; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..841
FT /note="Leukocyte immunoglobulin-like receptor subfamily B
FT member 3"
FT /id="PRO_0000414708"
FT TOPO_DOM 25..642
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 643..663
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 664..841
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..116
FT /note="Ig-like C2-type 1"
FT DOMAIN 118..220
FT /note="Ig-like C2-type 2"
FT DOMAIN 239..297
FT /note="Ig-like C2-type 3"
FT DOMAIN 308..428
FT /note="Ig-like C2-type 4"
FT DOMAIN 424..513
FT /note="Ig-like C2-type 5"
FT DOMAIN 537..618
FT /note="Ig-like C2-type 6"
FT REGION 683..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 711..716
FT /note="ITIM motif 1"
FT /evidence="ECO:0000250"
FT MOTIF 792..797
FT /note="ITIM motif 2"
FT /evidence="ECO:0000250"
FT MOTIF 822..827
FT /note="ITIM motif 3"
FT /evidence="ECO:0000250"
FT COMPBIAS 760..808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 794
FT /note="Phosphotyrosine; by LYN"
FT /evidence="ECO:0000269|PubMed:10327049"
FT MOD_RES 824
FT /note="Phosphotyrosine; by LYN"
FT /evidence="ECO:0000269|PubMed:10327049"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 246..295
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 343..395
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 444..495
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 544..595
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MUTAGEN 794
FT /note="Y->F: Abolishes interaction with PTPN6/SHP-1 and
FT PTPN11/SHP-2; when associated with F-824."
FT /evidence="ECO:0000269|PubMed:10327049,
FT ECO:0000269|PubMed:9482905"
FT MUTAGEN 824
FT /note="Y->F: Abolishes interaction with PTPN6/SHP-1 and
FT PTPN11/SHP-2; when associated with F-794."
FT /evidence="ECO:0000269|PubMed:10327049,
FT ECO:0000269|PubMed:9482905"
SQ SEQUENCE 841 AA; 93054 MW; 33E9B3C51F44FF3C CRC64;
MSCTFTALLR LGLTLSLWIP VLTGSLPKPI LRVQPDSVVS RRTKVTFLCE ETIGANEYRL
YKDGKLYKTV TKNKQKPENK AEFSFSNVDL SNAGQYRCSY STQYKSSGYS DLLELVVTGH
YWTPSLLAQA SPVVTSGGYV TLQCESWHND HKFILTVEGP QKLSWTQDSQ YNYSTRKYHA
LFSVGPVTPN QRWICRCYSY DRNRPYVWSP PSESVELLVS GNLQKPTIKA EPGSVITSKR
AMTIWCQGNL DAEVYFLHNE KSQKTQSTQT LQEPGNKGKF FIPSVTLQHA GQYRCYCYGS
AGWSQPSDTL ELVVTGIYEY YEPRLSVLPS PVVTAGGNMT LHCASDFPYD KFILTKEDKK
FGNSLDTEHI SSSGQYRALF IIGPTTPTHT GAFRCYGYYK NAPQLWSVPS ALQQILISGL
SKKPSLLTHQ GHILDPGMTL TLQCFSDINY DRFALHKVGG ADIMQHSSQQ TDTGFSVANF
TLGYVSSSTG GQYRCYGAHN LSSEWSASSE PLDILITGQL PLTPSLSVQP NHTVHSGETV
SLLCWSMDSV DTFILSKEGS AQQPLRLKSK SHDQQSQAEF SMSAVTSHLS GTYRCYGAQD
SSFYLLSSAS APVELTVSGP IETSTPPPTM SMPLGGLHMY LKALIGVSVA FILFLFIFIF
ILLRRRHRGK FRKDVQKEKD LQLSSGAEEP ITRKGELQKR PNPAAATQEE SLYASVEDMQ
TEDGVELNSW TPPEEDPQGE TYAQVKPSRL RKAGHVSPSV MSREQLNTEY EQAEEGQGAN
NQAAESGESQ DVTYAQLCSR TLRQGAAASP LSQAGEAPEE PSVYATLAAA RPEAVPKDME
Q
