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Leukocyte immunoglobulin-like receptor subfamily B member 4 (CD85 antigen-like family member K) (Immunoglobulin-like transcript 3) (ILT-3) (Leukocyte immunoglobulin-like receptor 5) (LIR-5) (Monocyte inhibitory receptor HM18) (CD antigen CD85k)

 LIRB4_HUMAN             Reviewed;         448 AA.
Q8NHJ6; A8MVL8; O15468; O75021; Q6FGQ9; Q8N1C7; Q8NHL5;
03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
08-FEB-2011, sequence version 3.
25-OCT-2017, entry version 146.
RecName: Full=Leukocyte immunoglobulin-like receptor subfamily B member 4;
AltName: Full=CD85 antigen-like family member K;
AltName: Full=Immunoglobulin-like transcript 3;
Short=ILT-3;
AltName: Full=Leukocyte immunoglobulin-like receptor 5;
Short=LIR-5;
AltName: Full=Monocyte inhibitory receptor HM18;
AltName: CD_antigen=CD85k;
Flags: Precursor;
Name=LILRB4; Synonyms=ILT3, LIR5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
VARIANT GLY-223.
TISSUE=Monocyte;
PubMed=9278324;
Arm J.P., Nwankwo C., Austen K.F.;
"Molecular identification of a novel family of human Ig superfamily
members that possess immunoreceptor tyrosine-based inhibition motifs
and homology to the mouse gp49B1 inhibitory receptor.";
J. Immunol. 159:2342-2349(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLY-223 AND ARG-414,
AND TISSUE SPECIFICITY.
TISSUE=Peripheral blood leukocyte;
PubMed=9548455;
Borges L., Hsu M.-L., Fanger N., Kubin M., Cosman D.;
"A family of human lymphoid and myeloid Ig-like receptors, some of
which bind to MHC class I molecules.";
J. Immunol. 159:5192-5196(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANTS LEU-5;
GLY-223 AND GLU-362.
PubMed=10941837; DOI=10.1007/s002510000183;
Liu W.R., Kim J., Nwankwo C., Ashworth L.K., Arm J.P.;
"Genomic organization of the human leukocyte immunoglobulin-like
receptors within the leukocyte receptor complex on chromosome
19q13.4.";
Immunogenetics 51:659-669(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Canavez F.C.;
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Placenta;
Li W.B., Gruber C., Jessee J., Polayes D.;
"Full-length cDNA libraries and normalization.";
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
ASP-20; GLY-223 AND ARG-414.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
FUNCTION, INTERACTION WITH PTPN6, PHOSPHORYLATION, TISSUE SPECIFICITY,
AND SUBCELLULAR LOCATION.
PubMed=9151699; DOI=10.1084/jem.185.10.1743;
Cella M., Doehring C., Samaridis J., Dessing M., Brockhaus M.,
Lanzavecchia A., Colonna M.;
"A novel inhibitory receptor (ILT3) expressed on monocytes,
macrophages, and dendritic cells involved in antigen processing.";
J. Exp. Med. 185:1743-1751(1997).
[10]
FUNCTION.
PubMed=11875462; DOI=10.1038/ni760;
Chang C.C., Ciubotariu R., Manavalan J.S., Yuan J., Colovai A.I.,
Piazza F., Lederman S., Colonna M., Cortesini R., Dalla-Favera R.,
Suciu-Foca N.;
"Tolerization of dendritic cells by T(S) cells: the crucial role of
inhibitory receptors ILT3 and ILT4.";
Nat. Immunol. 3:237-243(2002).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[12]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 24-219, AND DISULFIDE BONDS.
PubMed=21454581; DOI=10.1074/jbc.M111.221028;
Cheng H., Mohammed F., Nam G., Chen Y., Qi J., Garner L.I.,
Allen R.L., Yan J., Willcox B.E., Gao G.F.;
"Crystal structure of leukocyte Ig-like receptor LILRB4 (ILT3/LIR-
5/CD85k): a myeloid inhibitory receptor involved in immune
tolerance.";
J. Biol. Chem. 286:18013-18025(2011).
-!- FUNCTION: Receptor for class I MHC antigens. Recognizes a broad
spectrum of HLA-A, HLA-B, HLA-C and HLA-G alleles. Involved in the
down-regulation of the immune response and the development of
tolerance, e.g. towards transplants. Interferes with TNFRSF5-
signaling and NF-kappa-B up-regulation. Inhibits receptor-mediated
phosphorylation of cellular proteins and mobilization of
intracellular calcium ions. {ECO:0000269|PubMed:11875462,
ECO:0000269|PubMed:9151699}.
-!- SUBUNIT: Binds PTPN6 when phosphorylated.
-!- INTERACTION:
P29350:PTPN6; NbExp=4; IntAct=EBI-2805248, EBI-78260;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9151699};
Single-pass type I membrane protein {ECO:0000269|PubMed:9151699}.
Note=Ligand binding leads to internalization and translocation to
an antigen-processing compartment.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8NHJ6-1; Sequence=Displayed;
Name=2;
IsoId=Q8NHJ6-2; Sequence=VSP_008460;
Note=Alternative use of an acceptor site. No experimental
confirmation available.;
Name=3;
IsoId=Q8NHJ6-3; Sequence=VSP_035939;
-!- TISSUE SPECIFICITY: Detected in monocytes, macrophages, dendritic
cells, lung, natural killer cells and B-cells.
{ECO:0000269|PubMed:9151699, ECO:0000269|PubMed:9278324,
ECO:0000269|PubMed:9548455}.
-!- INDUCTION: Upon contact with CD8(+)CD28(-) alloantigen-specific T
suppressor (Ts) cells.
-!- 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.
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EMBL; U91925; AAB68665.1; -; mRNA.
EMBL; AF025532; AAB87666.1; -; mRNA.
EMBL; AF189768; AAG02024.1; -; Genomic_DNA.
EMBL; AF283988; AAL36992.1; -; mRNA.
EMBL; CR542048; CAG46845.1; -; mRNA.
EMBL; CR609786; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC009892; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC011515; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC026309; AAH26309.1; -; mRNA.
CCDS; CCDS12902.1; -. [Q8NHJ6-1]
CCDS; CCDS42618.1; -. [Q8NHJ6-2]
RefSeq; NP_001265355.2; NM_001278426.3.
RefSeq; NP_001265356.2; NM_001278427.3.
RefSeq; NP_001265357.2; NM_001278428.3.
RefSeq; NP_001265358.2; NM_001278429.3.
RefSeq; NP_001265359.2; NM_001278430.3.
UniGene; Hs.67846; -.
UniGene; Hs.731841; -.
PDB; 3P2T; X-ray; 1.70 A; A=24-219.
PDBsum; 3P2T; -.
ProteinModelPortal; Q8NHJ6; -.
SMR; Q8NHJ6; -.
BioGrid; 116197; 16.
IntAct; Q8NHJ6; 2.
STRING; 9606.ENSP00000270452; -.
iPTMnet; Q8NHJ6; -.
PhosphoSitePlus; Q8NHJ6; -.
DMDM; 322510117; -.
PaxDb; Q8NHJ6; -.
PeptideAtlas; Q8NHJ6; -.
PRIDE; Q8NHJ6; -.
DNASU; 11006; -.
Ensembl; ENST00000391736; ENSP00000375616; ENSG00000186818.
Ensembl; ENST00000612454; ENSP00000479829; ENSG00000275730. [Q8NHJ6-1]
Ensembl; ENST00000614699; ENSP00000478542; ENSG00000275730. [Q8NHJ6-3]
Ensembl; ENST00000621693; ENSP00000482234; ENSG00000275730. [Q8NHJ6-2]
GeneID; 11006; -.
KEGG; hsa:11006; -.
UCSC; uc002qgp.5; human. [Q8NHJ6-1]
CTD; 11006; -.
DisGeNET; 11006; -.
EuPathDB; HostDB:ENSG00000186818.12; -.
GeneCards; LILRB4; -.
H-InvDB; HIX0202844; -.
HGNC; HGNC:6608; LILRB4.
HPA; HPA052807; -.
MIM; 604821; gene.
neXtProt; NX_Q8NHJ6; -.
PharmGKB; PA30382; -.
eggNOG; ENOG410IHKK; Eukaryota.
eggNOG; ENOG411142H; LUCA.
HOVERGEN; HBG074353; -.
InParanoid; Q8NHJ6; -.
KO; K06512; -.
PhylomeDB; Q8NHJ6; -.
TreeFam; TF336644; -.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
ChiTaRS; LILRB4; human.
GeneWiki; LILRB4; -.
GenomeRNAi; 11006; -.
PRO; PR:Q8NHJ6; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000186818; -.
CleanEx; HS_LILRB4; -.
ExpressionAtlas; Q8NHJ6; baseline and differential.
Genevisible; Q8NHJ6; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; NAS:ProtInc.
GO; GO:0003823; F:antigen binding; TAS:ProtInc.
GO; GO:0004872; F:receptor activity; TAS:ProtInc.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0045671; P:negative regulation of osteoclast differentiation; IDA:UniProtKB.
GO; GO:1902894; P:negative regulation of pri-miRNA transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:1900181; P:negative regulation of protein localization to nucleus; IDA:BHF-UCL.
GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; IDA:BHF-UCL.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013151; Immunoglobulin.
Pfam; PF00047; ig; 1.
Pfam; PF13895; Ig_2; 1.
SUPFAM; SSF48726; SSF48726; 2.
PROSITE; PS50835; IG_LIKE; 2.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Alternative splicing; Cell membrane;
Complete proteome; Disulfide bond; Immunity; Immunoglobulin domain;
Membrane; Phosphoprotein; Polymorphism; Receptor; Reference proteome;
Repeat; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 448 Leukocyte immunoglobulin-like receptor
subfamily B member 4.
/FTId=PRO_0000014823.
TOPO_DOM 22 259 Extracellular. {ECO:0000255}.
TRANSMEM 260 280 Helical. {ECO:0000255}.
TOPO_DOM 281 448 Cytoplasmic. {ECO:0000255}.
DOMAIN 27 118 Ig-like C2-type 1.
DOMAIN 124 218 Ig-like C2-type 2.
MOTIF 358 363 ITIM motif 1.
MOTIF 410 415 ITIM motif 2.
MOTIF 440 445 ITIM motif 3.
MOD_RES 319 319 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
DISULFID 49 98 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:21454581}.
DISULFID 144 195 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:21454581}.
VAR_SEQ 330 330 C -> SG (in isoform 3).
{ECO:0000303|Ref.6}.
/FTId=VSP_035939.
VAR_SEQ 348 348 Missing (in isoform 2).
{ECO:0000303|Ref.4, ECO:0000303|Ref.5}.
/FTId=VSP_008460.
VARIANT 5 5 F -> L (in dbSNP:rs28366008).
{ECO:0000269|PubMed:10941837}.
/FTId=VAR_025501.
VARIANT 18 18 R -> S (in dbSNP:rs11574570).
/FTId=VAR_025502.
VARIANT 20 20 H -> D (in dbSNP:rs11540762).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_047846.
VARIANT 223 223 D -> G (in dbSNP:rs731170).
{ECO:0000269|PubMed:10941837,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9278324,
ECO:0000269|PubMed:9548455}.
/FTId=VAR_017014.
VARIANT 330 330 C -> Y (in dbSNP:rs11574575).
/FTId=VAR_025503.
VARIANT 335 335 N -> D (in dbSNP:rs11574576).
/FTId=VAR_025504.
VARIANT 362 362 K -> E (in dbSNP:rs2764337).
{ECO:0000269|PubMed:10941837}.
/FTId=VAR_017015.
VARIANT 362 362 K -> T (in dbSNP:rs11574589).
/FTId=VAR_030939.
VARIANT 414 414 Q -> R (in dbSNP:rs1048801).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9548455}.
/FTId=VAR_025505.
STRAND 30 35 {ECO:0000244|PDB:3P2T}.
STRAND 37 40 {ECO:0000244|PDB:3P2T}.
STRAND 45 50 {ECO:0000244|PDB:3P2T}.
STRAND 57 62 {ECO:0000244|PDB:3P2T}.
STRAND 69 72 {ECO:0000244|PDB:3P2T}.
STRAND 76 87 {ECO:0000244|PDB:3P2T}.
HELIX 90 92 {ECO:0000244|PDB:3P2T}.
STRAND 94 102 {ECO:0000244|PDB:3P2T}.
STRAND 105 107 {ECO:0000244|PDB:3P2T}.
STRAND 113 118 {ECO:0000244|PDB:3P2T}.
STRAND 125 130 {ECO:0000244|PDB:3P2T}.
STRAND 132 135 {ECO:0000244|PDB:3P2T}.
STRAND 140 157 {ECO:0000244|PDB:3P2T}.
HELIX 163 165 {ECO:0000244|PDB:3P2T}.
STRAND 166 182 {ECO:0000244|PDB:3P2T}.
HELIX 187 189 {ECO:0000244|PDB:3P2T}.
STRAND 191 198 {ECO:0000244|PDB:3P2T}.
HELIX 200 202 {ECO:0000244|PDB:3P2T}.
STRAND 213 218 {ECO:0000244|PDB:3P2T}.
SEQUENCE 448 AA; 49356 MW; C18C21694F283FBB CRC64;
MIPTFTALLC LGLSLGPRTH MQAGPLPKPT LWAEPGSVIS WGNSVTIWCQ GTLEAREYRL
DKEESPAPWD RQNPLEPKNK ARFSIPSMTE DYAGRYRCYY RSPVGWSQPS DPLELVMTGA
YSKPTLSALP SPLVTSGKSV TLLCQSRSPM DTFLLIKERA AHPLLHLRSE HGAQQHQAEF
PMSPVTSVHG GTYRCFSSHG FSHYLLSHPS DPLELIVSGS LEDPRPSPTR SVSTAAGPED
QPLMPTGSVP HSGLRRHWEV LIGVLVVSIL LLSLLLFLLL QHWRQGKHRT LAQRQADFQR
PPGAAEPEPK DGGLQRRSSP AADVQGENFC AAVKNTQPED GVEMDTRQSP HDEDPQAVTY
AKVKHSRPRR EMASPPSPLS GEFLDTKDRQ AEEDRQMDTE AAASEAPQDV TYAQLHSFTL
RQKATEPPPS QEGASPAEPS VYATLAIH


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