ID LIRB1_HUMAN Reviewed; 650 AA. AC Q8NHL6; A2IXV4; A8MXT0; O75024; O75025; Q8NHJ9; Q8NHK0; DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 24-JAN-2024, entry version 185. DE RecName: Full=Leukocyte immunoglobulin-like receptor subfamily B member 1; DE Short=LIR-1 {ECO:0000303|PubMed:11114384}; DE Short=Leukocyte immunoglobulin-like receptor 1; DE AltName: Full=CD85 antigen-like family member J; DE AltName: Full=Immunoglobulin-like transcript 2; DE Short=ILT-2 {ECO:0000303|PubMed:11114384}; DE AltName: Full=Monocyte/macrophage immunoglobulin-like receptor 7; DE Short=MIR-7; DE AltName: CD_antigen=CD85j {ECO:0000303|PubMed:11907092, ECO:0000303|PubMed:24453251}; DE Flags: Precursor; GN Name=LILRB1 {ECO:0000303|PubMed:20600445, ECO:0000312|HGNC:HGNC:6605}; GN Synonyms=ILT2 {ECO:0000303|PubMed:24453251}, LIR1 GN {ECO:0000303|PubMed:28636952}, MIR7; 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 4). 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] (ISOFORMS 1 AND 3), VARIANTS PRO-68; THR-142; RP ILE-155 AND LYS-625, INTERACTION WITH H301 AND PTPN6, PHOSPHORYLATION, RP TISSUE SPECIFICITY, AND FUNCTION. RC TISSUE=Lymphoblast; RX PubMed=9285411; DOI=10.1016/s1074-7613(00)80529-4; RA Cosman D., Fanger N., Borges L., Kubin M., Chin W., Peterson L., Hsu M.-L.; RT "A novel immunoglobulin superfamily receptor for cellular and viral MHC RT class I molecules."; RL Immunity 7:273-282(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). RX PubMed=10941837; DOI=10.1007/s002510000183; RA Liu W.R., Kim J., Nwankwo C., Ashworth L.K., Arm J.P.; RT "Genomic organization of the human leukocyte immunoglobulin-like receptors RT within the leukocyte receptor complex on chromosome 19q13.4."; RL Immunogenetics 51:659-669(2000). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), ALTERNATIVE SPLICING, SUBCELLULAR RP LOCATION (ISOFORM 5), AND VARIANTS PRO-68; THR-93; THR-142 AND ILE-155. RX PubMed=19658091; DOI=10.1002/eji.200839080; RA Jones D.C., Roghanian A., Brown D.P., Chang C., Allen R.L., Trowsdale J., RA Young N.T.; RT "Alternative mRNA splicing creates transcripts encoding soluble proteins RT from most LILR genes."; RL Eur. J. Immunol. 39:3195-3206(2009). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-68; THR-93; THR-142; RP ILE-155 AND LYS-625. RX PubMed=20600445; DOI=10.1016/j.humimm.2010.06.015; RA Davidson C.L., Li N.L., Burshtyn D.N.; RT "LILRB1 polymorphism and surface phenotypes of natural killer cells."; RL Hum. Immunol. 71:942-949(2010). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA Canavez F.C.; RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases. RN [7] 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS PRO-68; RP THR-142; ILE-155 AND LYS-625. RC TISSUE=B-cell; 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 [9] 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 [10] RP INTERACTION WITH HHV-5 PROTEIN UL18. RX PubMed=10591185; DOI=10.1016/s1074-7613(00)80135-1; RA Chapman T.L., Heikeman A.P., Bjorkman P.J.; RT "The inhibitory receptor LIR-1 uses a common binding interaction to RT recognize class I MHC molecules and the viral homolog UL18."; RL Immunity 11:603-613(1999). RN [11] RP PHOSPHORYLATION AT TYR-533; TYR-614 AND TYR-644, MUTAGENESIS OF TYR-533; RP TYR-562; TYR-614 AND TYR-644, INTERACTION WITH FCER1A, AND FUNCTION. RX PubMed=11907092; DOI=10.4049/jimmunol.168.7.3351; RA Bellon T., Kitzig F., Sayos J., Lopez-Botet M.; RT "Mutational analysis of immunoreceptor tyrosine-based inhibition motifs of RT the Ig-like transcript 2 (CD85j) leukocyte receptor."; RL J. Immunol. 168:3351-3359(2002). RN [12] 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 [13] RP TISSUE SPECIFICITY, AND FUNCTION. RX PubMed=19304799; DOI=10.1073/pnas.0901173106; RA Li C., Houser B.L., Nicotra M.L., Strominger J.L.; RT "HLA-G homodimer-induced cytokine secretion through HLA-G receptors on RT human decidual macrophages and natural killer cells."; RL Proc. Natl. Acad. Sci. U.S.A. 106:5767-5772(2009). RN [14] RP 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 [15] RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=24453251; DOI=10.4049/jimmunol.1300438; RA Naji A., Menier C., Morandi F., Agaugue S., Maki G., Ferretti E., Bruel S., RA Pistoia V., Carosella E.D., Rouas-Freiss N.; RT "Binding of HLA-G to ITIM-bearing Ig-like transcript 2 receptor suppresses RT B cell responses."; RL J. Immunol. 192:1536-1546(2014). RN [16] RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=29262349; DOI=10.1016/j.immuni.2017.11.018; RA Fu B., Zhou Y., Ni X., Tong X., Xu X., Dong Z., Sun R., Tian Z., Wei H.; RT "Natural Killer Cells Promote Fetal Development through the Secretion of RT Growth-Promoting Factors."; RL Immunity 47:1100-1113(2017). RN [17] RP FUNCTION, SUBUNIT, AND INTERACTION WITH HLA-F. RX PubMed=28636952; DOI=10.1016/j.immuni.2017.06.002; RA Dulberger C.L., McMurtrey C.P., Holzemer A., Neu K.E., Liu V., RA Steinbach A.M., Garcia-Beltran W.F., Sulak M., Jabri B., Lynch V.J., RA Altfeld M., Hildebrand W.H., Adams E.J.; RT "Human Leukocyte Antigen F Presents Peptides and Regulates Immunity through RT Interactions with NK Cell Receptors."; RL Immunity 46:1018-1029(2017). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 25-221, AND DISULFIDE BONDS. RX PubMed=11114384; DOI=10.1016/s1074-7613(00)00071-6; RA Chapman T.L., Heikema A.P., West A.P. Jr., Bjorkman P.J.; RT "Crystal structure and ligand binding properties of the D1D2 region of the RT inhibitory receptor LIR-1 (ILT2)."; RL Immunity 13:727-736(2000). 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:16455647, PubMed:28636952). Receptor for H301/UL18, a human CC cytomegalovirus class I MHC homolog. Ligand binding results in CC inhibitory signals and down-regulation of the immune response. CC Engagement of LILRB1 present on natural killer cells or T-cells by CC class I MHC molecules protects the target cells from lysis. Interaction CC with HLA-B or HLA-E leads to inhibition of FCER1A signaling and CC serotonin release. Inhibits FCGR1A-mediated phosphorylation of cellular CC proteins and mobilization of intracellular calcium ions CC (PubMed:11907092, PubMed:9285411, PubMed:9842885). Recognizes HLA-G in CC complex with B2M/beta-2 microglobulin and a nonamer self-peptide CC (PubMed:16455647). Upon interaction with peptide-bound HLA-G-B2M CC complex, triggers secretion of growth-promoting factors by decidual NK CC cells (PubMed:29262349, PubMed:19304799). Reprograms B cells toward an CC immune suppressive phenotype (PubMed:24453251). CC {ECO:0000269|PubMed:11907092, ECO:0000269|PubMed:16455647, CC ECO:0000269|PubMed:19304799, ECO:0000269|PubMed:24453251, CC ECO:0000269|PubMed:28636952, ECO:0000269|PubMed:29262349, CC ECO:0000269|PubMed:9285411, ECO:0000269|PubMed:9842885}. CC -!- SUBUNIT: Binds PTPN6 when phosphorylated (PubMed:9285411). Binds FCER1A CC and FCGR1A (PubMed:9842885, PubMed:11907092). Interacts with human CC cytomegalovirus/HHV-5 protein UL18 (PubMed:10591185). Interacts with CC peptide-bound HLA-G-B2M complex (PubMed:16455647). Interacts with CC peptide-bound HLA-F-B2M complex but not with peptide-free HLA-F open CC conformer. It does not probe the peptide sequence directly CC (PubMed:28636952). {ECO:0000269|PubMed:10591185, CC ECO:0000269|PubMed:11907092, ECO:0000269|PubMed:16455647, CC ECO:0000269|PubMed:28636952, ECO:0000269|PubMed:9285411, CC ECO:0000269|PubMed:9842885}. CC -!- INTERACTION: CC Q8NHL6; P17693: HLA-G; NbExp=8; IntAct=EBI-2805262, EBI-1043063; CC Q8NHL6; P29350: PTPN6; NbExp=4; IntAct=EBI-2805262, EBI-78260; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20448110, CC ECO:0000269|PubMed:24453251, ECO:0000269|PubMed:29262349, CC ECO:0000305|PubMed:19658091}; Single-pass type I membrane protein CC {ECO:0000255}. CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Secreted CC {ECO:0000269|PubMed:19658091}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=Q8NHL6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8NHL6-2; Sequence=VSP_008456; CC Name=3; CC IsoId=Q8NHL6-3; Sequence=VSP_008456, VSP_008457; CC Name=4; CC IsoId=Q8NHL6-4; Sequence=VSP_008457; CC Name=5; Synonyms=65 Kda, sLILRB1; CC IsoId=Q8NHL6-5; Sequence=VSP_008456, VSP_057087, VSP_057088; CC -!- TISSUE SPECIFICITY: Expressed in B cells, monocytes and various CC dendritic cell (DC) subsets including myeloid, plasmacytoid and CC tolerogenic DCs (at protein level) (PubMed:20448110, PubMed:9285411, CC PubMed:9842885, PubMed:24453251). Expressed in decidual macrophages (at CC protein level) (PubMed:19304799). Expressed in decidual NK cells (at CC protein level) (PubMed:29262349). {ECO:0000269|PubMed:19304799, CC ECO:0000269|PubMed:20448110, ECO:0000269|PubMed:24453251, CC ECO:0000269|PubMed:29262349, ECO:0000269|PubMed:9285411, CC ECO:0000269|PubMed:9842885}. CC -!- DOMAIN: Contains 4 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:11907092, ECO:0000269|PubMed:9285411, CC ECO:0000269|PubMed:9842885}. CC -!- MISCELLANEOUS: [Isoform 5]: May act as dominant negative regulator and CC block the interaction between membrane-associated isoforms and HLA- CC class I. {ECO:0000269|PubMed:19658091}. 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; AF004230; AAB67710.1; -; mRNA. DR EMBL; AF009220; AAB63521.1; -; mRNA. DR EMBL; AF009221; AAB63522.1; -; mRNA. DR EMBL; AF189277; AAG08984.1; -; Genomic_DNA. DR EMBL; EU915608; ACK56074.1; -; mRNA. DR EMBL; HM135394; ADJ55944.1; -; Genomic_DNA. DR EMBL; HM135401; ADJ55951.1; -; Genomic_DNA. DR EMBL; AF283984; AAL36988.1; -; mRNA. DR EMBL; AF283985; AAL36989.1; -; mRNA. DR EMBL; AC009892; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC015731; AAH15731.1; -; mRNA. DR CCDS; CCDS42614.1; -. [Q8NHL6-3] DR CCDS; CCDS42615.1; -. [Q8NHL6-2] DR CCDS; CCDS42616.1; -. [Q8NHL6-4] DR CCDS; CCDS42617.1; -. [Q8NHL6-1] DR RefSeq; NP_001075106.2; NM_001081637.2. DR RefSeq; NP_001075107.2; NM_001081638.3. DR RefSeq; NP_001075108.2; NM_001081639.3. DR RefSeq; NP_001265327.2; NM_001278398.2. DR RefSeq; NP_001265328.2; NM_001278399.2. DR RefSeq; NP_006660.4; NM_006669.6. DR PDB; 1G0X; X-ray; 2.10 A; A=25-221. DR PDB; 1P7Q; X-ray; 3.40 A; D=25-221. DR PDB; 1UFU; X-ray; 3.00 A; A=25-221. DR PDB; 1UGN; X-ray; 1.80 A; A=24-221. DR PDB; 1VDG; X-ray; 2.80 A; A/B=24-220. DR PDB; 3D2U; X-ray; 2.21 A; D/H=24-221. DR PDB; 4LL9; X-ray; 2.69 A; A/B/C=222-417. DR PDB; 4NO0; X-ray; 2.70 A; D=27-221. DR PDB; 5KNM; X-ray; 3.30 A; D=24-221. DR PDB; 6AEE; X-ray; 3.30 A; G/H=25-417. DR PDB; 6EWA; X-ray; 2.39 A; D/H=27-221. DR PDB; 6EWC; X-ray; 3.20 A; D/H=27-221. DR PDB; 6EWO; X-ray; 2.30 A; D/H=27-221. DR PDB; 6K60; X-ray; 3.15 A; D/H=24-220. DR PDB; 6ZDX; X-ray; 3.00 A; B=25-420. DR PDB; 7KFK; X-ray; 2.63 A; A/B=222-421. DR PDBsum; 1G0X; -. DR PDBsum; 1P7Q; -. DR PDBsum; 1UFU; -. DR PDBsum; 1UGN; -. DR PDBsum; 1VDG; -. DR PDBsum; 3D2U; -. DR PDBsum; 4LL9; -. DR PDBsum; 4NO0; -. DR PDBsum; 5KNM; -. DR PDBsum; 6AEE; -. DR PDBsum; 6EWA; -. DR PDBsum; 6EWC; -. DR PDBsum; 6EWO; -. DR PDBsum; 6K60; -. DR PDBsum; 6ZDX; -. DR PDBsum; 7KFK; -. DR AlphaFoldDB; Q8NHL6; -. DR EMDB; EMD-22879; -. DR SMR; Q8NHL6; -. DR BioGRID; 116070; 12. DR IntAct; Q8NHL6; 16. DR MINT; Q8NHL6; -. DR STRING; 9606.ENSP00000315997; -. DR GlyCosmos; Q8NHL6; 3 sites, No reported glycans. DR GlyGen; Q8NHL6; 3 sites. DR iPTMnet; Q8NHL6; -. DR PhosphoSitePlus; Q8NHL6; -. DR BioMuta; LILRB1; -. DR DMDM; 37537910; -. DR jPOST; Q8NHL6; -. DR MassIVE; Q8NHL6; -. DR PaxDb; 9606-ENSP00000315997; -. DR PeptideAtlas; Q8NHL6; -. DR ProteomicsDB; 73718; -. [Q8NHL6-1] DR ProteomicsDB; 73719; -. [Q8NHL6-2] DR ProteomicsDB; 73720; -. [Q8NHL6-3] DR ProteomicsDB; 73721; -. [Q8NHL6-4] DR DNASU; 10859; -. DR Ensembl; ENST00000612636.4; ENSP00000479887.1; ENSG00000277807.5. [Q8NHL6-3] DR Ensembl; ENST00000616408.4; ENSP00000481700.1; ENSG00000274669.5. DR Ensembl; ENST00000617686.4; ENSP00000478282.1; ENSG00000277807.5. [Q8NHL6-4] DR Ensembl; ENST00000618055.4; ENSP00000480365.1; ENSG00000277807.5. [Q8NHL6-1] DR Ensembl; ENST00000618681.4; ENSP00000479753.1; ENSG00000277807.5. [Q8NHL6-2] DR GeneID; 10859; -. DR KEGG; hsa:10859; -. DR UCSC; uc032iow.2; human. [Q8NHL6-1] DR AGR; HGNC:6605; -. DR CTD; 10859; -. DR DisGeNET; 10859; -. DR GeneCards; LILRB1; -. DR HGNC; HGNC:6605; LILRB1. DR MIM; 604811; gene. DR neXtProt; NX_Q8NHL6; -. DR PharmGKB; PA30379; -. DR eggNOG; ENOG502RYEX; Eukaryota. DR InParanoid; Q8NHL6; -. DR OrthoDB; 5321028at2759; -. DR PhylomeDB; Q8NHL6; -. DR TreeFam; TF336644; -. DR PathwayCommons; Q8NHL6; -. DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell. DR SignaLink; Q8NHL6; -. DR SIGNOR; Q8NHL6; -. DR BioGRID-ORCS; 10859; 12 hits in 1121 CRISPR screens. DR ChiTaRS; LILRB1; human. DR EvolutionaryTrace; Q8NHL6; -. DR GeneWiki; LILRB1; -. DR GenomeRNAi; 10859; -. DR Pharos; Q8NHL6; Tbio. DR PRO; PR:Q8NHL6; -. DR Proteomes; UP000005640; Unplaced. DR RNAct; Q8NHL6; Protein. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0030107; F:HLA-A specific inhibitory MHC class I receptor activity; IDA:UniProtKB. DR GO; GO:0030109; F:HLA-B specific inhibitory MHC class I receptor activity; IDA:UniProtKB. DR GO; GO:0032396; F:inhibitory MHC class I receptor activity; IBA:GO_Central. DR GO; GO:0042288; F:MHC class I protein binding; IDA:UniProtKB. DR GO; GO:0032393; F:MHC class I receptor activity; 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:0032394; F:MHC class Ib receptor activity; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB. DR GO; GO:0008157; F:protein phosphatase 1 binding; IPI:UniProtKB. DR GO; GO:0042169; F:SH2 domain binding; IDA:UniProtKB. DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:UniProtKB. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central. DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB. DR GO; GO:0097028; P:dendritic cell differentiation; IEP:UniProtKB. DR GO; GO:0002774; P:Fc receptor mediated inhibitory signaling pathway; IDA:UniProtKB. DR GO; GO:0002767; P:immune response-inhibiting cell surface receptor signaling pathway; NAS:BHF-UCL. DR GO; GO:0046636; P:negative regulation of alpha-beta T cell activation; IDA:UniProtKB. DR GO; GO:0051926; P:negative regulation of calcium ion transport; IDA:UniProtKB. DR GO; GO:2001186; P:negative regulation of CD8-positive, alpha-beta T cell activation; IDA:UniProtKB. DR GO; GO:0045786; P:negative regulation of cell cycle; IDA:UniProtKB. DR GO; GO:0002719; P:negative regulation of cytokine production involved in immune response; IDA:UniProtKB. DR GO; GO:2000669; P:negative regulation of dendritic cell apoptotic process; IDA:UniProtKB. DR GO; GO:2001199; P:negative regulation of dendritic cell differentiation; IMP:UniProtKB. DR GO; GO:0045806; P:negative regulation of endocytosis; IDA:UniProtKB. DR GO; GO:0032688; P:negative regulation of interferon-beta production; IDA:UniProtKB. DR GO; GO:0032693; P:negative regulation of interleukin-10 production; IDA:UniProtKB. DR GO; GO:0032695; P:negative regulation of interleukin-12 production; IDA:UniProtKB. DR GO; GO:0032945; P:negative regulation of mononuclear cell proliferation; IDA:UniProtKB. DR GO; GO:0045953; P:negative regulation of natural killer cell mediated cytotoxicity; IDA:UniProtKB. DR GO; GO:2001205; P:negative regulation of osteoclast development; IDA:UniProtKB. DR GO; GO:0014063; P:negative regulation of serotonin secretion; IDA:UniProtKB. DR GO; GO:2001189; P:negative regulation of T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell; IDA:UniProtKB. DR GO; GO:0001915; P:negative regulation of T cell mediated cytotoxicity; IDA:UniProtKB. DR GO; GO:0042130; P:negative regulation of T cell proliferation; IDA:UniProtKB. DR GO; GO:0071635; P:negative regulation of transforming growth factor beta production; IDA:UniProtKB. DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:UniProtKB. DR GO; GO:0032689; P:negative regulation of type II interferon production; IDA:UniProtKB. DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB. DR GO; GO:0002230; P:positive regulation of defense response to virus by host; IDA:UniProtKB. DR GO; GO:2001193; P:positive regulation of gamma-delta T cell activation involved in immune response; IDA:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB. DR GO; GO:0060907; P:positive regulation of macrophage cytokine production; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; NAS:BHF-UCL. DR GO; GO:0032729; P:positive regulation of type II interferon production; IDA:UniProtKB. DR GO; GO:0031623; P:receptor internalization; TAS:UniProtKB. DR GO; GO:0009615; P:response to virus; IDA:UniProtKB. DR GO; GO:0007165; P:signal transduction; IDA:UniProtKB. DR GO; GO:0002309; P:T cell proliferation involved in immune response; IDA:UniProtKB. DR CDD; cd05751; IgC2_D1_LILR_KIR_like; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 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 InterPro; IPR013151; Immunoglobulin. DR PANTHER; PTHR11738:SF165; LEUKOCYTE IMMUNOGLOBULIN-LIKE RECEPTOR SUBFAMILY A MEMBER 1-RELATED; 1. DR PANTHER; PTHR11738; MHC CLASS I NK CELL RECEPTOR; 1. DR Pfam; PF00047; ig; 1. DR Pfam; PF13895; Ig_2; 1. DR SMART; SM00409; IG; 4. DR SMART; SM00408; IGc2; 3. DR SUPFAM; SSF48726; Immunoglobulin; 4. DR PROSITE; PS50835; IG_LIKE; 2. PE 1: Evidence at protein level; KW 3D-structure; Adaptive immunity; Alternative splicing; Cell membrane; KW Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain; Membrane; KW Phosphoprotein; Receptor; Reference proteome; Repeat; Secreted; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..23 FT /evidence="ECO:0000255" FT CHAIN 24..650 FT /note="Leukocyte immunoglobulin-like receptor subfamily B FT member 1" FT /id="PRO_0000014820" FT TOPO_DOM 24..461 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 462..482 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 483..650 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 27..115 FT /note="Ig-like C2-type 1" FT DOMAIN 116..221 FT /note="Ig-like C2-type 2" FT DOMAIN 222..312 FT /note="Ig-like C2-type 3" FT DOMAIN 313..409 FT /note="Ig-like C2-type 4" FT REGION 415..451 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 491..524 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 563..650 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 531..536 FT /note="ITIM motif 1" FT MOTIF 560..565 FT /note="ITIM motif 2" FT MOTIF 612..617 FT /note="ITIM motif 3" FT MOTIF 642..647 FT /note="ITIM motif 4" FT COMPBIAS 423..451 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 587..602 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 533 FT /note="Phosphotyrosine" FT /evidence="ECO:0000305|PubMed:11907092" FT MOD_RES 614 FT /note="Phosphotyrosine" FT /evidence="ECO:0000305|PubMed:11907092" FT MOD_RES 644 FT /note="Phosphotyrosine" FT /evidence="ECO:0000305|PubMed:11907092" FT CARBOHYD 281 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 302 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 341 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 49..98 FT /evidence="ECO:0000269|PubMed:11114384, FT ECO:0007744|PDB:1G0X" FT DISULFID 145..197 FT /evidence="ECO:0000269|PubMed:11114384, FT ECO:0007744|PDB:1G0X" FT DISULFID 157..167 FT /evidence="ECO:0000269|PubMed:11114384, FT ECO:0007744|PDB:1G0X" FT DISULFID 246..297 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:11114384, ECO:0007744|PDB:1G0X" FT DISULFID 346..397 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:11114384, ECO:0007744|PDB:1G0X" FT VAR_SEQ 437 FT /note="S -> SA (in isoform 2, isoform 3 and isoform 5)" FT /evidence="ECO:0000303|PubMed:19658091, FT ECO:0000303|PubMed:9285411" FT /id="VSP_008456" FT VAR_SEQ 455 FT /note="L -> E (in isoform 5)" FT /evidence="ECO:0000303|PubMed:19658091" FT /id="VSP_057087" FT VAR_SEQ 456..650 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:19658091" FT /id="VSP_057088" FT VAR_SEQ 550 FT /note="R -> RQ (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:20600445, FT ECO:0000303|PubMed:9259559, ECO:0000303|PubMed:9285411" FT /id="VSP_008457" FT VARIANT 68 FT /note="L -> P (in dbSNP:rs1061679)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:19658091, ECO:0000269|PubMed:20600445, FT ECO:0000269|PubMed:9285411" FT /id="VAR_016993" FT VARIANT 93 FT /note="A -> T (in dbSNP:rs12460501)" FT /evidence="ECO:0000269|PubMed:19658091, FT ECO:0000269|PubMed:20600445" FT /id="VAR_049888" FT VARIANT 142 FT /note="I -> T (in dbSNP:rs1061680)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:19658091, ECO:0000269|PubMed:20600445, FT ECO:0000269|PubMed:9285411" FT /id="VAR_016994" FT VARIANT 155 FT /note="S -> I (in dbSNP:rs1061681)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:19658091, ECO:0000269|PubMed:20600445, FT ECO:0000269|PubMed:9285411" FT /id="VAR_016995" FT VARIANT 301 FT /note="H -> Y (in dbSNP:rs1045818)" FT /id="VAR_059398" FT VARIANT 459 FT /note="L -> V (in dbSNP:rs1138737)" FT /id="VAR_067316" FT VARIANT 620 FT /note="L -> F (in dbSNP:rs634222)" FT /id="VAR_016996" FT VARIANT 625 FT /note="E -> K (in dbSNP:rs16985478)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:20600445, ECO:0000269|PubMed:9285411" FT /id="VAR_067317" FT MUTAGEN 533 FT /note="Y->F: Impairs receptor phosphorylation and abolishes FT inhibition of serotonin release. No effect on PTPN6 FT binding; when associated with F-562." FT /evidence="ECO:0000269|PubMed:11907092" FT MUTAGEN 562 FT /note="Y->F: No effect on PTPN6 binding; when associated FT with F-533." FT /evidence="ECO:0000269|PubMed:11907092" FT MUTAGEN 614 FT /note="Y->F: No effect on PTPN6 binding. Abolishes PTPN6 FT binding; when associated with F-644." FT /evidence="ECO:0000269|PubMed:11907092" FT MUTAGEN 644 FT /note="Y->F: Reduces PTPN6 binding. Abolishes PTPN6 FT binding; when associated with F-614." FT /evidence="ECO:0000269|PubMed:11907092" FT CONFLICT 557 FT /note="P -> L (in Ref. 6; AAL36989)" FT /evidence="ECO:0000305" FT STRAND 30..35 FT /evidence="ECO:0007829|PDB:1UGN" FT STRAND 37..40 FT /evidence="ECO:0007829|PDB:1UGN" FT STRAND 45..50 FT /evidence="ECO:0007829|PDB:1UGN" FT STRAND 52..54 FT /evidence="ECO:0007829|PDB:1VDG" FT STRAND 58..65 FT /evidence="ECO:0007829|PDB:1UGN" FT HELIX 68..71 FT /evidence="ECO:0007829|PDB:1UGN" FT HELIX 75..78 FT /evidence="ECO:0007829|PDB:1UGN" FT TURN 79..81 FT /evidence="ECO:0007829|PDB:1UGN" FT STRAND 82..87 FT /evidence="ECO:0007829|PDB:1UGN" FT HELIX 90..92 FT /evidence="ECO:0007829|PDB:1UGN" FT STRAND 94..102 FT /evidence="ECO:0007829|PDB:1UGN" FT TURN 103..105 FT /evidence="ECO:0007829|PDB:1UGN" FT STRAND 114..119 FT /evidence="ECO:0007829|PDB:1UGN" FT STRAND 126..131 FT /evidence="ECO:0007829|PDB:1UGN" FT STRAND 133..136 FT /evidence="ECO:0007829|PDB:1UGN" FT STRAND 141..146 FT /evidence="ECO:0007829|PDB:1UGN" FT STRAND 152..159 FT /evidence="ECO:0007829|PDB:1UGN" FT STRAND 161..163 FT /evidence="ECO:0007829|PDB:6ZDX" FT STRAND 167..169 FT /evidence="ECO:0007829|PDB:1UGN" FT HELIX 172..174 FT /evidence="ECO:0007829|PDB:1G0X" FT HELIX 175..177 FT /evidence="ECO:0007829|PDB:6ZDX" FT STRAND 179..184 FT /evidence="ECO:0007829|PDB:1UGN" FT STRAND 189..191 FT /evidence="ECO:0007829|PDB:6EWA" FT STRAND 193..200 FT /evidence="ECO:0007829|PDB:1UGN" FT STRAND 204..208 FT /evidence="ECO:0007829|PDB:3D2U" FT STRAND 215..220 FT /evidence="ECO:0007829|PDB:1UGN" FT STRAND 227..232 FT /evidence="ECO:0007829|PDB:7KFK" FT STRAND 234..236 FT /evidence="ECO:0007829|PDB:7KFK" FT STRAND 243..250 FT /evidence="ECO:0007829|PDB:7KFK" FT STRAND 253..259 FT /evidence="ECO:0007829|PDB:7KFK" FT STRAND 266..270 FT /evidence="ECO:0007829|PDB:7KFK" FT STRAND 274..276 FT /evidence="ECO:0007829|PDB:6ZDX" FT STRAND 277..283 FT /evidence="ECO:0007829|PDB:7KFK" FT HELIX 289..291 FT /evidence="ECO:0007829|PDB:7KFK" FT STRAND 293..305 FT /evidence="ECO:0007829|PDB:7KFK" FT STRAND 314..318 FT /evidence="ECO:0007829|PDB:7KFK" FT STRAND 326..332 FT /evidence="ECO:0007829|PDB:7KFK" FT STRAND 334..336 FT /evidence="ECO:0007829|PDB:7KFK" FT STRAND 340..350 FT /evidence="ECO:0007829|PDB:7KFK" FT STRAND 353..361 FT /evidence="ECO:0007829|PDB:7KFK" FT STRAND 367..370 FT /evidence="ECO:0007829|PDB:7KFK" FT STRAND 372..374 FT /evidence="ECO:0007829|PDB:7KFK" FT STRAND 377..386 FT /evidence="ECO:0007829|PDB:7KFK" FT HELIX 389..391 FT /evidence="ECO:0007829|PDB:7KFK" FT STRAND 393..400 FT /evidence="ECO:0007829|PDB:7KFK" FT STRAND 404..408 FT /evidence="ECO:0007829|PDB:4LL9" FT STRAND 415..420 FT /evidence="ECO:0007829|PDB:7KFK" SQ SEQUENCE 650 AA; 70819 MW; 549196EA4ED2767C CRC64; MTPILTVLIC LGLSLGPRTH VQAGHLPKPT LWAEPGSVIT QGSPVTLRCQ GGQETQEYRL YREKKTALWI TRIPQELVKK GQFPIPSITW EHAGRYRCYY GSDTAGRSES SDPLELVVTG AYIKPTLSAQ PSPVVNSGGN VILQCDSQVA FDGFSLCKEG EDEHPQCLNS QPHARGSSRA IFSVGPVSPS RRWWYRCYAY DSNSPYEWSL PSDLLELLVL GVSKKPSLSV QPGPIVAPEE TLTLQCGSDA GYNRFVLYKD GERDFLQLAG AQPQAGLSQA NFTLGPVSRS YGGQYRCYGA HNLSSEWSAP SDPLDILIAG QFYDRVSLSV QPGPTVASGE NVTLLCQSQG WMQTFLLTKE GAADDPWRLR STYQSQKYQA EFPMGPVTSA HAGTYRCYGS QSSKPYLLTH PSDPLELVVS GPSGGPSSPT TGPTSTSGPE DQPLTPTGSD PQSGLGRHLG VVIGILVAVI LLLLLLLLLF LILRHRRQGK HWTSTQRKAD FQHPAGAVGP EPTDRGLQWR SSPAADAQEE NLYAAVKHTQ PEDGVEMDTR SPHDEDPQAV TYAEVKHSRP RREMASPPSP LSGEFLDTKD RQAEEDRQMD TEAAASEAPQ DVTYAQLHSL TLRREATEPP PSQEGPSPAV PSIYATLAIH //