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Leukocyte immunoglobulin-like receptor subfamily B member 3 (LIR-3) (Leukocyte immunoglobulin-like receptor 3) (Cell-surface glycoprotein p91) (Paired immunoglobulin-like receptor B) (PIR-B)

 LIRB3_MOUSE             Reviewed;         841 AA.
P97484;
14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
12-SEP-2018, entry version 118.
RecName: Full=Leukocyte immunoglobulin-like receptor subfamily B member 3;
Short=LIR-3;
Short=Leukocyte immunoglobulin-like receptor 3;
AltName: Full=Cell-surface glycoprotein p91;
AltName: Full=Paired immunoglobulin-like receptor B;
Short=PIR-B;
Flags: Precursor;
Name=Lilrb3; Synonyms=Pirb;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
STRAIN=B10.A;
PubMed=9054430; DOI=10.1074/jbc.272.11.7320;
Hayami K., Fukuta D., Nishikawa Y., Yamashita Y., Inui M., Ohyama Y.,
Hikida M., Ohmori H., Takai T.;
"Molecular cloning of a novel murine cell-surface glycoprotein
homologous to killer cell inhibitory receptors.";
J. Biol. Chem. 272:7320-7327(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
FUNCTION, MUTAGENESIS OF TYR-794 AND TYR-824, INTERACTION WITH
PTPN6/SHP-1 AND PTPN11/SHP-2, AND SUBCELLULAR LOCATION.
PubMed=9482905; DOI=10.1073/pnas.95.5.2446;
Blery M., Kubagawa H., Chen C.C., Vely F., Cooper M.D., Vivier E.;
"The paired Ig-like receptor PIR-B is an inhibitory receptor that
recruits the protein-tyrosine phosphatase SHP-1.";
Proc. Natl. Acad. Sci. U.S.A. 95:2446-2451(1998).
[4]
FUNCTION, PHOSPHORYLATION AT TYR-794 AND TYR-824 BY LYN, MUTAGENESIS
OF TYR-794 AND TYR-824, INTERACTION WITH PTPN6/SHP-1 AND PTPN11/SHP-2,
SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=10327049; DOI=10.1038/sj.onc.1202552;
Maeda A., Scharenberg A.M., Tsukada S., Bolen J.B., Kinet J.P.,
Kurosaki T.;
"Paired immunoglobulin-like receptor B (PIR-B) inhibits BCR-induced
activation of Syk and Btk by SHP-1.";
Oncogene 18:2291-2297(1999).
[5]
FUNCTION, PHOSPHORYLATION BY LYN, INTERACTION WITH LYN AND
PTPN6/SHP-1, AND TISSUE SPECIFICITY.
PubMed=10611342; DOI=10.1073/pnas.96.26.15086;
Ho L.H., Uehara T., Chen C.C., Kubagawa H., Cooper M.D.;
"Constitutive tyrosine phosphorylation of the inhibitory paired Ig-
like receptor PIR-B.";
Proc. Natl. Acad. Sci. U.S.A. 96:15086-15090(1999).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-684 AND SER-757, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
-!- FUNCTION: May act as receptor for class I MHC antigens. Becomes
activated upon coligation of LILRB3 and immune receptors, such as
FCGR2B and the B-cell receptor. Down-regulates antigen-induced B-
cell activation by recruiting phosphatases to its immunoreceptor
tyrosine-based inhibitor motifs (ITIM).
{ECO:0000269|PubMed:10327049, ECO:0000269|PubMed:10611342,
ECO:0000269|PubMed:9482905}.
-!- SUBUNIT: Interacts with LYN, PTPN6/SHP-1 and PTPN11/SHP-2.
{ECO:0000269|PubMed:10327049, ECO:0000269|PubMed:10611342,
ECO:0000269|PubMed:9482905}.
-!- INTERACTION:
P05067:APP (xeno); NbExp=8; IntAct=EBI-15728641, EBI-821758;
P35235:Ptpn11; NbExp=2; IntAct=EBI-15728641, EBI-397236;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10327049,
ECO:0000269|PubMed:9054430, ECO:0000269|PubMed:9482905}; Single-
pass type I membrane protein {ECO:0000269|PubMed:10327049,
ECO:0000269|PubMed:9054430, ECO:0000269|PubMed:9482905}.
-!- TISSUE SPECIFICITY: Detected in macrophages, splenocytes and B
lymphocytes (at protein level). Detected in macrophages, mast
cells, splenocytes, peritoneal cells and natural killer cells.
{ECO:0000269|PubMed:10611342, ECO:0000269|PubMed:9054430}.
-!- DOMAIN: Contains 3 copies of a cytoplasmic motif that is referred
to as the immunoreceptor tyrosine-based inhibitor motif (ITIM).
This motif is involved in modulation of cellular responses. The
phosphorylated ITIM motif can bind the SH2 domain of several SH2-
containing phosphatases, including PTPN6/SHP-1, resulting in the
dephosphorylation of the downstream protein kinases SYK and BTK.
{ECO:0000269|PubMed:10327049}.
-!- PTM: Phosphorylated on tyrosine residues by LYN. Phosphorylation
at Tyr-794 and Tyr-824 is important for interaction with
PTPN6/SHP-1 and PTPN11/SHP-2. {ECO:0000269|PubMed:10327049,
ECO:0000269|PubMed:10611342}.
-!- MISCELLANEOUS: Belongs to the leukocyte receptor cluster (LRC)
present on chromosome 7.
-----------------------------------------------------------------------
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EMBL; U83172; AAB40934.1; -; mRNA.
EMBL; AC130680; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC171680; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS39730.1; -.
RefSeq; NP_035225.2; NM_011095.2.
UniGene; Mm.326531; -.
UniGene; Mm.440814; -.
ProteinModelPortal; P97484; -.
SMR; P97484; -.
DIP; DIP-59889N; -.
IntAct; P97484; 7.
STRING; 10090.ENSMUSP00000077546; -.
iPTMnet; P97484; -.
PhosphoSitePlus; P97484; -.
MaxQB; P97484; -.
PaxDb; P97484; -.
PRIDE; P97484; -.
Ensembl; ENSMUST00000078451; ENSMUSP00000077546; ENSMUSG00000058818.
GeneID; 18733; -.
KEGG; mmu:18733; -.
UCSC; uc009ewb.2; mouse.
CTD; 18733; -.
MGI; MGI:894311; Lilrb3.
eggNOG; ENOG410IKJD; Eukaryota.
eggNOG; ENOG41116BR; LUCA.
GeneTree; ENSGT00760000119033; -.
HOVERGEN; HBG074353; -.
InParanoid; P97484; -.
KO; K06512; -.
OMA; ITHMADI; -.
OrthoDB; EOG091G0D6W; -.
PhylomeDB; P97484; -.
TreeFam; TF336644; -.
Reactome; R-MMU-6798695; Neutrophil degranulation.
PRO; PR:P97484; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000058818; Expressed in 118 organ(s), highest expression level in bone marrow macrophage.
Genevisible; P97484; MM.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0001540; F:amyloid-beta binding; IDA:ARUK-UCL.
GO; GO:0042803; F:protein homodimerization activity; IDA:ARUK-UCL.
GO; GO:0044877; F:protein-containing complex binding; IPI:ARUK-UCL.
GO; GO:0001782; P:B cell homeostasis; IMP:MGI.
GO; GO:0019724; P:B cell mediated immunity; IMP:MGI.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IMP:MGI.
GO; GO:0007611; P:learning or memory; IGI:ARUK-UCL.
GO; GO:0043011; P:myeloid dendritic cell differentiation; IMP:MGI.
GO; GO:0051248; P:negative regulation of protein metabolic process; IGI:ARUK-UCL.
GO; GO:1900454; P:positive regulation of long term synaptic depression; IGI:ARUK-UCL.
GO; GO:0035307; P:positive regulation of protein dephosphorylation; IGI:ARUK-UCL.
GO; GO:1900271; P:regulation of long-term synaptic potentiation; IGI:ARUK-UCL.
Gene3D; 2.60.40.10; -; 6.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013151; Immunoglobulin.
Pfam; PF00047; ig; 1.
Pfam; PF13895; Ig_2; 2.
SMART; SM00409; IG; 5.
SMART; SM00408; IGc2; 4.
SUPFAM; SSF48726; SSF48726; 6.
PROSITE; PS50835; IG_LIKE; 1.
1: Evidence at protein level;
Adaptive immunity; Cell membrane; Complete proteome; Disulfide bond;
Glycoprotein; Immunity; Immunoglobulin domain; Membrane;
Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 841 Leukocyte immunoglobulin-like receptor
subfamily B member 3.
/FTId=PRO_0000414708.
TOPO_DOM 25 642 Extracellular. {ECO:0000255}.
TRANSMEM 643 663 Helical. {ECO:0000255}.
TOPO_DOM 664 841 Cytoplasmic. {ECO:0000255}.
DOMAIN 27 116 Ig-like C2-type 1.
DOMAIN 118 220 Ig-like C2-type 2.
DOMAIN 239 297 Ig-like C2-type 3.
DOMAIN 308 428 Ig-like C2-type 4.
DOMAIN 424 513 Ig-like C2-type 5.
DOMAIN 537 618 Ig-like C2-type 6.
MOTIF 711 716 ITIM motif 1. {ECO:0000250}.
MOTIF 792 797 ITIM motif 2. {ECO:0000250}.
MOTIF 822 827 ITIM motif 3. {ECO:0000250}.
MOD_RES 684 684 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 757 757 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 794 794 Phosphotyrosine; by LYN.
{ECO:0000269|PubMed:10327049}.
MOD_RES 824 824 Phosphotyrosine; by LYN.
{ECO:0000269|PubMed:10327049}.
CARBOHYD 338 338 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 500 500 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 49 98 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 246 295 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 343 395 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 444 495 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 544 595 {ECO:0000255|PROSITE-ProRule:PRU00114}.
MUTAGEN 794 794 Y->F: Abolishes interaction with
PTPN6/SHP-1 and PTPN11/SHP-2; when
associated with F-824.
{ECO:0000269|PubMed:10327049,
ECO:0000269|PubMed:9482905}.
MUTAGEN 824 824 Y->F: Abolishes interaction with
PTPN6/SHP-1 and PTPN11/SHP-2; when
associated with F-794.
{ECO:0000269|PubMed:10327049,
ECO:0000269|PubMed:9482905}.
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


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