LIRB1_HUMAN
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 03-AUG-2022, entry version 179.
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},
GN LIR1 {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=5; 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}.
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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 SMR; Q8NHL6; -.
DR BioGRID; 116070; 12.
DR IntAct; Q8NHL6; 14.
DR MINT; Q8NHL6; -.
DR STRING; 9606.ENSP00000315997; -.
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; Q8NHL6; -.
DR PeptideAtlas; Q8NHL6; -.
DR PRIDE; 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 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; 1000446at2759; -.
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 1044 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; Chromosome 19.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0032689; P:negative regulation of interferon-gamma 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: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:0032729; P:positive regulation of interferon-gamma production; 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: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 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 InterPro; IPR013151; Immunoglobulin.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13895; Ig_2; 1.
DR SMART; SM00409; IG; 4.
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 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
