LIRB2_HUMAN
ID LIRB2_HUMAN Reviewed; 597 AA.
AC Q8N423; A2IXV5; A8MU67; C9JF29; O75017; Q8NHJ7; Q8NHJ8;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 5.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Leukocyte immunoglobulin-like receptor subfamily B member 2;
DE Short=LIR-2;
DE Short=Leukocyte immunoglobulin-like receptor 2;
DE AltName: Full=CD85 antigen-like family member D;
DE AltName: Full=Immunoglobulin-like transcript 4;
DE Short=ILT-4;
DE AltName: Full=Monocyte/macrophage immunoglobulin-like receptor 10;
DE Short=MIR-10;
DE AltName: CD_antigen=CD85d;
DE Flags: Precursor;
GN Name=LILRB2 {ECO:0000312|HGNC:HGNC:6606};
GN Synonyms=ILT4 {ECO:0000303|PubMed:12853576, ECO:0000303|PubMed:20448110},
GN LIR2, MIR10;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=9259559; DOI=10.1016/s0960-9822(06)00263-6;
RA Wagtmann N., Rojo S., Eichler E., Mohrenweiser H., Long E.O.;
RT "A new human gene complex encoding the killer cell inhibitory receptors and
RT related monocyte/macrophage receptors.";
RL Curr. Biol. 7:615-618(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND VARIANTS GLU-161; TYR-300;
RP TRP-306 AND HIS-322.
RX PubMed=9382880; DOI=10.1084/jem.186.11.1809;
RA Colonna M., Navarro F., Bellon T., Llano M., Garcia P., Samaridis J.,
RA Angman L., Cella M., Lopez-Botet M.;
RT "A common inhibitory receptor for major histocompatibility complex class I
RT molecules on human lymphoid and myelomonocytic cells.";
RL J. Exp. Med. 186:1809-1818(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION, AND
RP VARIANTS GLU-161; TYR-300; TRP-306 AND HIS-322.
RC TISSUE=Dendritic cell, and Peripheral blood monocyte;
RX PubMed=9548455;
RA Borges L., Hsu M.-L., Fanger N., Kubin M., Cosman D.;
RT "A family of human lymphoid and myeloid Ig-like receptors, some of which
RT bind to MHC class I molecules.";
RL J. Immunol. 159:5192-5196(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS GLU-161;
RP TYR-300; TRP-306 AND HIS-322.
RA Canavez F.C.;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLU-161;
RP TYR-300; TRP-306 AND HIS-322.
RC TISSUE=Peripheral blood leukocyte;
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 [7]
RP INTERACTION WITH PTPN6 AND FCGR1A, PHOSPHORYLATION, TISSUE SPECIFICITY, AND
RP FUNCTION.
RX PubMed=9842885;
RX DOI=10.1002/(sici)1521-4141(199811)28:11<3423::aid-immu3423>3.0.co;2-2;
RA Fanger N.A., Cosman D., Peterson L., Braddy S.C., Maliszewski C.R.,
RA Borges L.;
RT "The MHC class I binding proteins LIR-1 and LIR-2 inhibit Fc receptor-
RT mediated signaling in monocytes.";
RL Eur. J. Immunol. 28:3423-3434(1998).
RN [8]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH HLA-F.
RX PubMed=11169396;
RX DOI=10.1002/1521-4141(200012)30:12<3552::aid-immu3552>3.0.co;2-l;
RA Lepin E.J., Bastin J.M., Allan D.S., Roncador G., Braud V.M., Mason D.Y.,
RA van der Merwe P.A., McMichael A.J., Bell J.I., Powis S.H.,
RA O'Callaghan C.A.;
RT "Functional characterization of HLA-F and binding of HLA-F tetramers to
RT ILT2 and ILT4 receptors.";
RL Eur. J. Immunol. 30:3552-3561(2000).
RN [9]
RP FUNCTION.
RX PubMed=11875462; DOI=10.1038/ni760;
RA Chang C.C., Ciubotariu R., Manavalan J.S., Yuan J., Colovai A.I.,
RA Piazza F., Lederman S., Colonna M., Cortesini R., Dalla-Favera R.,
RA Suciu-Foca N.;
RT "Tolerization of dendritic cells by T(S) cells: the crucial role of
RT inhibitory receptors ILT3 and ILT4.";
RL Nat. Immunol. 3:237-243(2002).
RN [10]
RP INTERACTION WITH TYPE I MHC ALLELES, AND FUNCTION.
RX PubMed=12853576; DOI=10.1073/pnas.1431057100;
RA Shiroishi M., Tsumoto K., Amano K., Shirakihara Y., Colonna M., Braud V.M.,
RA Allan D.S.J., Makadzange A., Rowland-Jones S., Willcox B.E., Jones E.Y.,
RA van der Merwe P.A., Kumagai I., Maenaka K.;
RT "Human inhibitory receptors Ig-like transcript 2 (ILT2) and ILT4 compete
RT with CD8 for MHC class I binding and bind preferentially to HLA-G.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8856-8861(2003).
RN [11]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH HLA-G.
RX PubMed=16455647; DOI=10.1074/jbc.m512305200;
RA Shiroishi M., Kuroki K., Ose T., Rasubala L., Shiratori I., Arase H.,
RA Tsumoto K., Kumagai I., Kohda D., Maenaka K.;
RT "Efficient leukocyte Ig-like receptor signaling and crystal structure of
RT disulfide-linked HLA-G dimer.";
RL J. Biol. Chem. 281:10439-10447(2006).
RN [12]
RP INDUCTION.
RX PubMed=19860908; DOI=10.1186/1471-2172-10-56;
RA Brown D.P., Jones D.C., Anderson K.J., Lapaque N., Buerki R.A.,
RA Trowsdale J., Allen R.L.;
RT "The inhibitory receptor LILRB4 (ILT3) modulates antigen presenting cell
RT phenotype and, along with LILRB2 (ILT4), is upregulated in response to
RT Salmonella infection.";
RL BMC Immunol. 10:56-56(2009).
RN [13]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=20448110; DOI=10.1182/blood-2009-07-234872;
RA Gregori S., Tomasoni D., Pacciani V., Scirpoli M., Battaglia M.,
RA Magnani C.F., Hauben E., Roncarolo M.G.;
RT "Differentiation of type 1 T regulatory cells (Tr1) by tolerogenic DC-10
RT requires the IL-10-dependent ILT4/HLA-G pathway.";
RL Blood 116:935-944(2010).
RN [14]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=27859042; DOI=10.1002/eji.201646564;
RA Koestlin N., Ostermeir A.L., Spring B., Schwarz J., Marme A., Walter C.B.,
RA Poets C.F., Gille C.;
RT "HLA-G promotes myeloid-derived suppressor cell accumulation and
RT suppressive activity during human pregnancy through engagement of the
RT receptor ILT4.";
RL Eur. J. Immunol. 47:374-384(2017).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 24-219, AND DISULFIDE BONDS.
RX PubMed=12390682; DOI=10.1186/1472-6807-2-6;
RA Willcox B.E., Thomas L.M., Chapman T.L., Heikema A.P., West A.P. Jr.,
RA Bjorkman P.J.;
RT "Crystal structure of LIR-2 (ILT4) at 1.8 A: differences from LIR-1 (ILT2)
RT in regions implicated in the binding of the human cytomegalovirus class I
RT MHC homolog UL18.";
RL BMC Struct. Biol. 2:6-6(2002).
CC -!- FUNCTION: Receptor for class I MHC antigens. Recognizes a broad
CC spectrum of HLA-A, HLA-B, HLA-C, HLA-G and HLA-F alleles
CC (PubMed:11169396, PubMed:12853576, PubMed:16455647, PubMed:20448110,
CC PubMed:27859042). Involved in the down-regulation of the immune
CC response and the development of tolerance. Recognizes HLA-G in complex
CC with B2M/beta-2 microglobulin and a nonamer self-peptide (peptide-bound
CC HLA-G-B2M) triggering differentiation of type 1 regulatory T cells and
CC myeloid-derived suppressor cells, both of which actively maintain
CC maternal-fetal tolerance (PubMed:20448110, PubMed:27859042,
CC PubMed:16455647). Competes with CD8A for binding to class I MHC
CC antigens. Inhibits FCGR1A-mediated phosphorylation of cellular proteins
CC and mobilization of intracellular calcium ions (PubMed:11875462,
CC PubMed:12853576, PubMed:9548455, PubMed:9842885).
CC {ECO:0000269|PubMed:11169396, ECO:0000269|PubMed:11875462,
CC ECO:0000269|PubMed:12853576, ECO:0000269|PubMed:16455647,
CC ECO:0000269|PubMed:20448110, ECO:0000269|PubMed:27859042,
CC ECO:0000269|PubMed:9548455, ECO:0000269|PubMed:9842885}.
CC -!- SUBUNIT: Binds PTPN6 when phosphorylated. Binds FCGR1A. Interacts with
CC peptide-bound HLA-G-B2M; this interaction is direct (PubMed:16455647).
CC Interacts with peptide-bound HLA-F-B2M; this interaction is direct
CC (PubMed:11169396). {ECO:0000269|PubMed:11169396,
CC ECO:0000269|PubMed:16455647}.
CC -!- INTERACTION:
CC Q8N423; Q9UKU9: ANGPTL2; NbExp=5; IntAct=EBI-2816428, EBI-15485893;
CC Q8N423; Q86XS5: ANGPTL5; NbExp=5; IntAct=EBI-2816428, EBI-15485927;
CC Q8N423; PRO_0000000092 [P05067]: APP; NbExp=7; IntAct=EBI-2816428, EBI-821758;
CC Q8N423; P01889: HLA-B; NbExp=2; IntAct=EBI-2816428, EBI-1046513;
CC Q8N423; P17693: HLA-G; NbExp=7; IntAct=EBI-2816428, EBI-1043063;
CC Q8N423; P17693-2: HLA-G; NbExp=4; IntAct=EBI-2816428, EBI-16586375;
CC Q8N423; P17693-5: HLA-G; NbExp=2; IntAct=EBI-2816428, EBI-16586455;
CC Q8N423; P17693-6: HLA-G; NbExp=3; IntAct=EBI-2816428, EBI-16586550;
CC Q8N423; P46531: NOTCH1; NbExp=8; IntAct=EBI-2816428, EBI-636374;
CC Q8N423; P29350: PTPN6; NbExp=3; IntAct=EBI-2816428, EBI-78260;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20448110};
CC Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing, Alternative initiation; Named isoforms=4;
CC Name=2;
CC IsoId=Q8N423-2; Sequence=Displayed;
CC Name=1;
CC IsoId=Q8N423-1; Sequence=VSP_061383;
CC Name=3;
CC IsoId=Q8N423-3; Sequence=VSP_061383, VSP_061384, VSP_061385;
CC Name=4;
CC IsoId=Q8N423-4; Sequence=VSP_061382, VSP_061383;
CC -!- TISSUE SPECIFICITY: Expressed in monocytes and at lower levels in
CC myeloid and plasmacytoid dendritic cells. Expressed in tolerogenic
CC IL10-producing dendritic cells (PubMed:20448110). Expressed in myeloid-
CC derived suppressor cells during pregnancy (PubMed:27859042). Detected
CC at low levels in natural killer (NK) cells. Expressed in B cells.
CC {ECO:0000269|PubMed:20448110, ECO:0000269|PubMed:27859042,
CC ECO:0000269|PubMed:9548455, ECO:0000269|PubMed:9842885}.
CC -!- INDUCTION: Induced on monocyte-derived macrophages by S.typhimurium
CC infection. {ECO:0000269|PubMed:19860908}.
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 -!- PTM: Phosphorylated on tyrosine residues. Dephosphorylated by PTPN6.
CC {ECO:0000269|PubMed:9842885}.
CC -!- MISCELLANEOUS: [Isoform 2]: Alternative use of an acceptor site.
CC {ECO:0000305}.
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DR EMBL; AF004231; AAB67711.1; -; mRNA.
DR EMBL; AF025528; AAB87662.1; -; mRNA.
DR EMBL; AF283986; AAL36990.1; -; mRNA.
DR EMBL; AF283987; AAL36991.1; -; mRNA.
DR EMBL; AC010518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC036827; AAH36827.1; -; mRNA.
DR CCDS; CCDS12886.1; -. [Q8N423-1]
DR CCDS; CCDS42612.1; -. [Q8N423-2]
DR CCDS; CCDS62791.1; -. [Q8N423-4]
DR CCDS; CCDS62792.1; -. [Q8N423-3]
DR RefSeq; NP_001074447.2; NM_001080978.3.
DR RefSeq; NP_001265332.2; NM_001278403.2.
DR RefSeq; NP_001265333.2; NM_001278404.2.
DR RefSeq; NP_001265334.2; NM_001278405.2.
DR RefSeq; NP_001265335.2; NM_001278406.2.
DR RefSeq; NP_005865.3; NM_005874.4.
DR PDB; 2DYP; X-ray; 2.50 A; D=24-219.
DR PDB; 2GW5; X-ray; 1.80 A; A=24-219.
DR PDB; 4LLA; X-ray; 2.50 A; A/B/C=222-419.
DR PDB; 6AED; X-ray; 3.80 A; A=27-419.
DR PDB; 6BCS; X-ray; 2.10 A; A=24-220.
DR PDBsum; 2DYP; -.
DR PDBsum; 2GW5; -.
DR PDBsum; 4LLA; -.
DR PDBsum; 6AED; -.
DR PDBsum; 6BCS; -.
DR AlphaFoldDB; Q8N423; -.
DR DIP; DIP-59888N; -.
DR IntAct; Q8N423; 23.
DR STRING; 9606.ENSP00000375629; -.
DR GlyGen; Q8N423; 5 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q8N423; -.
DR PhosphoSitePlus; Q8N423; -.
DR BioMuta; LILRB2; -.
DR DMDM; 311033485; -.
DR jPOST; Q8N423; -.
DR MassIVE; Q8N423; -.
DR PaxDb; Q8N423; -.
DR PeptideAtlas; Q8N423; -.
DR PRIDE; Q8N423; -.
DR ProteomicsDB; 2083; -.
DR ProteomicsDB; 71866; -. [Q8N423-1]
DR ProteomicsDB; 71867; -. [Q8N423-2]
DR ProteomicsDB; 9927; -.
DR Antibodypedia; 32869; 301 antibodies from 27 providers.
DR DNASU; 10288; -.
DR Ensembl; ENST00000314446.10; ENSP00000319960.5; ENSG00000131042.15. [Q8N423-2]
DR Ensembl; ENST00000391746.5; ENSP00000375626.1; ENSG00000131042.15. [Q8N423-3]
DR Ensembl; ENST00000391748.5; ENSP00000375628.1; ENSG00000131042.15. [Q8N423-2]
DR Ensembl; ENST00000391749.4; ENSP00000375629.4; ENSG00000131042.15. [Q8N423-1]
DR Ensembl; ENST00000434421.5; ENSP00000410117.1; ENSG00000131042.15. [Q8N423-4]
DR Ensembl; ENST00000610886.4; ENSP00000482933.1; ENSG00000276146.4.
DR Ensembl; ENST00000614225.4; ENSP00000480841.1; ENSG00000275463.4.
DR Ensembl; ENST00000617341.4; ENSP00000484373.1; ENSG00000276146.4.
DR Ensembl; ENST00000617886.4; ENSP00000483553.1; ENSG00000276146.4.
DR Ensembl; ENST00000618392.4; ENSP00000480302.1; ENSG00000274513.4.
DR Ensembl; ENST00000618705.2; ENSP00000481208.1; ENSG00000275463.4.
DR Ensembl; ENST00000619122.3; ENSP00000483478.1; ENSG00000275463.4.
DR Ensembl; ENST00000621020.4; ENSP00000483014.1; ENSG00000275463.4.
DR GeneID; 10288; -.
DR KEGG; hsa:10288; -.
DR MANE-Select; ENST00000314446.10; ENSP00000319960.5; NM_001080978.4; NP_001074447.2.
DR UCSC; uc010eri.4; human. [Q8N423-2]
DR CTD; 10288; -.
DR GeneCards; LILRB2; -.
DR HGNC; HGNC:6606; LILRB2.
DR HPA; ENSG00000131042; Group enriched (bone marrow, lung, lymphoid tissue).
DR MIM; 604815; gene.
DR neXtProt; NX_Q8N423; -.
DR OpenTargets; ENSG00000131042; -.
DR PharmGKB; PA30380; -.
DR VEuPathDB; HostDB:ENSG00000131042; -.
DR eggNOG; ENOG502RYEX; Eukaryota.
DR GeneTree; ENSGT01000000214458; -.
DR HOGENOM; CLU_021100_2_3_1; -.
DR InParanoid; Q8N423; -.
DR OMA; WGRQADF; -.
DR OrthoDB; 1000446at2759; -.
DR PhylomeDB; Q8N423; -.
DR TreeFam; TF336644; -.
DR PathwayCommons; Q8N423; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q8N423; -.
DR SIGNOR; Q8N423; -.
DR BioGRID-ORCS; 10288; 10 hits in 1054 CRISPR screens.
DR ChiTaRS; LILRB2; human.
DR EvolutionaryTrace; Q8N423; -.
DR GenomeRNAi; 10288; -.
DR Pharos; Q8N423; Tbio.
DR PRO; PR:Q8N423; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8N423; protein.
DR Bgee; ENSG00000131042; Expressed in monocyte and 97 other tissues.
DR ExpressionAtlas; Q8N423; baseline and differential.
DR Genevisible; Q8N423; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR GO; GO:0001540; F:amyloid-beta binding; IMP:ARUK-UCL.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:BHF-UCL.
DR GO; GO:0032396; F:inhibitory MHC class I receptor activity; IDA:BHF-UCL.
DR GO; GO:0042288; F:MHC class I protein binding; IDA:UniProtKB.
DR GO; GO:0023029; F:MHC class Ib protein binding; IDA:UniProtKB.
DR GO; GO:0023025; F:MHC class Ib protein complex binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:ARUK-UCL.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IPI:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:ARUK-UCL.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:BHF-UCL.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0002774; P:Fc receptor mediated inhibitory signaling pathway; IDA:UniProtKB.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; IDA:BHF-UCL.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0002767; P:immune response-inhibiting cell surface receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0140105; P:interleukin-10-mediated signaling pathway; IEP:ARUK-UCL.
DR GO; GO:0007611; P:learning or memory; ISS:ARUK-UCL.
DR GO; GO:0002578; P:negative regulation of antigen processing and presentation; IDA:BHF-UCL.
DR GO; GO:0051926; P:negative regulation of calcium ion transport; IDA:UniProtKB.
DR GO; GO:1905875; P:negative regulation of postsynaptic density organization; IC:ARUK-UCL.
DR GO; GO:0051248; P:negative regulation of protein metabolic process; ISS:ARUK-UCL.
DR GO; GO:2000524; P:negative regulation of T cell costimulation; IMP:ARUK-UCL.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; IDA:BHF-UCL.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; NAS:BHF-UCL.
DR GO; GO:1900454; P:positive regulation of long-term synaptic depression; ISS:ARUK-UCL.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISS:ARUK-UCL.
DR GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; IMP:BHF-UCL.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:BHF-UCL.
DR GO; GO:0002666; P:positive regulation of T cell tolerance induction; IMP:BHF-UCL.
DR GO; GO:0002645; P:positive regulation of tolerance induction; IMP:UniProtKB.
DR GO; GO:2001198; P:regulation of dendritic cell differentiation; IC:BHF-UCL.
DR GO; GO:1900271; P:regulation of long-term synaptic potentiation; ISS:ARUK-UCL.
DR GO; GO:0007165; P:signal transduction; IDA:BHF-UCL.
DR Gene3D; 2.60.40.10; -; 4.
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 Pfam; PF13895; Ig_2; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SUPFAM; SSF48726; SSF48726; 4.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative initiation;
KW Alternative promoter usage; Alternative splicing; Cell membrane;
KW Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..597
FT /note="Leukocyte immunoglobulin-like receptor subfamily B
FT member 2"
FT /id="PRO_0000014821"
FT TOPO_DOM 22..460
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 461..481
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 482..597
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..110
FT /note="Ig-like C2-type 1"
FT DOMAIN 111..229
FT /note="Ig-like C2-type 2"
FT DOMAIN 230..318
FT /note="Ig-like C2-type 3"
FT DOMAIN 330..419
FT /note="Ig-like C2-type 4"
FT REGION 417..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 530..535
FT /note="ITIM motif 1"
FT MOTIF 559..564
FT /note="ITIM motif 2"
FT MOTIF 589..594
FT /note="ITIM motif 3"
FT COMPBIAS 425..439
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:12390682, ECO:0007744|PDB:2GW5"
FT DISULFID 144..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:12390682, ECO:0007744|PDB:2GW5"
FT DISULFID 156..166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:12390682, ECO:0007744|PDB:2GW5"
FT DISULFID 245..296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 345..396
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..116
FT /note="Missing (in isoform 4)"
FT /id="VSP_061382"
FT VAR_SEQ 436
FT /note="P -> PA (in isoform 1, isoform 3 and isoform 4)"
FT /id="VSP_061383"
FT VAR_SEQ 494..509
FT /note="TQRKADFQHPAGAVGP -> SPAQLPTPRKKTSMLP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9382880"
FT /id="VSP_061384"
FT VAR_SEQ 510..597
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9382880"
FT /id="VSP_061385"
FT VARIANT 20
FT /note="R -> H (in dbSNP:rs383369)"
FT /id="VAR_016997"
FT VARIANT 161
FT /note="D -> E (in dbSNP:rs373032)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9382880, ECO:0000269|PubMed:9548455,
FT ECO:0000269|Ref.4"
FT /id="VAR_016998"
FT VARIANT 235
FT /note="M -> V (in dbSNP:rs386056)"
FT /id="VAR_047432"
FT VARIANT 300
FT /note="H -> Y (in dbSNP:rs7247538)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9382880, ECO:0000269|PubMed:9548455,
FT ECO:0000269|Ref.4"
FT /id="VAR_016999"
FT VARIANT 306
FT /note="C -> W (in dbSNP:rs7247451)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9382880, ECO:0000269|PubMed:9548455,
FT ECO:0000269|Ref.4"
FT /id="VAR_017000"
FT VARIANT 322
FT /note="R -> H (in dbSNP:rs1128646)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9382880, ECO:0000269|PubMed:9548455,
FT ECO:0000269|Ref.4"
FT /id="VAR_061314"
FT VARIANT 324
FT /note="T -> R (in dbSNP:rs7247055)"
FT /id="VAR_047433"
FT VARIANT 326
FT /note="F -> S (in dbSNP:rs7246737)"
FT /id="VAR_047434"
FT VARIANT 349
FT /note="R -> G (in dbSNP:rs7247025)"
FT /id="VAR_047435"
FT VARIANT 403
FT /note="D -> N (in dbSNP:rs4993133)"
FT /id="VAR_061315"
FT CONFLICT 583
FT /note="E -> G (in Ref. 6; AAH36827)"
FT /evidence="ECO:0000305"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:2GW5"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:2GW5"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:2GW5"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:2GW5"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:6BCS"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:2GW5"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:2DYP"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:2GW5"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:2GW5"
FT STRAND 94..102
FT /evidence="ECO:0007829|PDB:2GW5"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:2GW5"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:2GW5"
FT STRAND 140..158
FT /evidence="ECO:0007829|PDB:2GW5"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:6BCS"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:2GW5"
FT STRAND 176..183
FT /evidence="ECO:0007829|PDB:2GW5"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:6BCS"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:2GW5"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:6BCS"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:6BCS"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:4LLA"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:4LLA"
FT STRAND 241..249
FT /evidence="ECO:0007829|PDB:4LLA"
FT STRAND 252..258
FT /evidence="ECO:0007829|PDB:4LLA"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:4LLA"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:4LLA"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:4LLA"
FT STRAND 292..299
FT /evidence="ECO:0007829|PDB:4LLA"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:4LLA"
FT STRAND 326..331
FT /evidence="ECO:0007829|PDB:4LLA"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:4LLA"
FT STRAND 342..349
FT /evidence="ECO:0007829|PDB:4LLA"
FT STRAND 352..361
FT /evidence="ECO:0007829|PDB:4LLA"
FT STRAND 366..369
FT /evidence="ECO:0007829|PDB:4LLA"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:4LLA"
FT STRAND 376..382
FT /evidence="ECO:0007829|PDB:4LLA"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:4LLA"
FT STRAND 392..400
FT /evidence="ECO:0007829|PDB:4LLA"
FT STRAND 403..407
FT /evidence="ECO:0007829|PDB:4LLA"
FT STRAND 414..418
FT /evidence="ECO:0007829|PDB:4LLA"
SQ SEQUENCE 597 AA; 65005 MW; F58D713858356427 CRC64;
MTPIVTVLIC LGLSLGPRTR VQTGTIPKPT LWAEPDSVIT QGSPVTLSCQ GSLEAQEYRL
YREKKSASWI TRIRPELVKN GQFHIPSITW EHTGRYGCQY YSRARWSELS DPLVLVMTGA
YPKPTLSAQP SPVVTSGGRV TLQCESQVAF GGFILCKEGE DEHPQCLNSQ PHARGSSRAI
FSVGPVSPNR RWSHRCYGYD LNSPYVWSSP SDLLELLVPG VSKKPSLSVQ PGPVMAPGES
LTLQCVSDVG YDRFVLYKEG ERDLRQLPGR QPQAGLSQAN FTLGPVSRSY GGQYRCYGAH
NLSSECSAPS DPLDILITGQ IRGTPFISVQ PGPTVASGEN VTLLCQSWRQ FHTFLLTKAG
AADAPLRLRS IHEYPKYQAE FPMSPVTSAH AGTYRCYGSL NSDPYLLSHP SEPLELVVSG
PSMGSSPPPT GPISTPGPED QPLTPTGSDP QSGLGRHLGV VIGILVAVVL LLLLLLLLFL
ILRHRRQGKH WTSTQRKADF QHPAGAVGPE PTDRGLQWRS SPAADAQEEN LYAAVKDTQP
EDGVEMDTRA AASEAPQDVT YAQLHSLTLR RKATEPPPSQ EREPPAEPSI YATLAIH
