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Leukocyte immunoglobulin-like receptor subfamily A member 3 (CD85 antigen-like family member E) (Immunoglobulin-like transcript 6) (ILT-6) (Leukocyte immunoglobulin-like receptor 4) (LIR-4) (Monocyte inhibitory receptor HM43/HM31) (CD antigen CD85e)

 LIRA3_HUMAN             Reviewed;         439 AA.
Q8N6C8; J3KPM2; O15469; O15470; O75016; Q8N151; Q8N154; Q8NHJ1;
Q8NHJ2; Q8NHJ3; Q8NHJ4;
03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
04-APR-2006, sequence version 3.
20-JUN-2018, entry version 139.
RecName: Full=Leukocyte immunoglobulin-like receptor subfamily A member 3;
AltName: Full=CD85 antigen-like family member E;
AltName: Full=Immunoglobulin-like transcript 6;
Short=ILT-6;
AltName: Full=Leukocyte immunoglobulin-like receptor 4;
Short=LIR-4;
AltName: Full=Monocyte inhibitory receptor HM43/HM31;
AltName: CD_antigen=CD85e;
Flags: Precursor;
Name=LILRA3; Synonyms=ILT6, LIR4;
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), VARIANT SER-3, AND TISSUE
SPECIFICITY.
TISSUE=Lung, and 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), VARIANT SER-3, AND TISSUE
SPECIFICITY.
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 [MRNA] (ISOFORM 2).
PubMed=9079806; DOI=10.1002/eji.1830270313;
Samaridis J., Colonna M.;
"Cloning of novel immunoglobulin superfamily receptors expressed on
human myeloid and lymphoid cells: structural evidence for new
stimulatory and inhibitory pathways.";
Eur. J. Immunol. 27:660-665(1997).
[4]
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-3.
TISSUE=Peripheral blood leukocyte;
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).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-420, AND VARIANTS ARG-107 AND
HIS-301.
PubMed=12750859; DOI=10.1007/s00251-003-0561-1;
Norman P.J., Carey B.S., Stephens H.A., Vaughan R.W.;
"DNA sequence variation and molecular genotyping of natural killer
leukocyte immunoglobulin-like receptor, LILRA3.";
Immunogenetics 55:165-171(2003).
[7]
PROTEIN SEQUENCE OF 24-38.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[8]
GLYCOSYLATION AT ASN-140; ASN-281; ASN-302; ASN-341 AND ASN-431, AND
FUNCTION.
PubMed=24085305; DOI=10.1074/jbc.M113.478578;
Lee T.H., Mitchell A., Liu Lau S., An H., Rajeaskariah P.,
Wasinger V., Raftery M., Bryant K., Tedla N.;
"Glycosylation in a mammalian expression system is critical for the
production of functionally active leukocyte immunoglobulin-like
receptor A3 protein.";
J. Biol. Chem. 288:32873-32885(2013).
[9]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 24-120, DISULFIDE BOND, AND
FUNCTION.
PubMed=21559424; DOI=10.1371/journal.pone.0019245;
Ryu M., Chen Y., Qi J., Liu J., Fan Z., Nam G., Shi Y., Cheng H.,
Gao G.F.;
"LILRA3 binds both classical and non-classical HLA class I molecules
but with reduced affinities compared to LILRB1/LILRB2: structural
evidence.";
PLoS ONE 6:E19245-E19245(2011).
-!- FUNCTION: Acts as soluble receptor for class I MHC antigens. Binds
both classical and non-classical HLA class I molecules but with
reduced affinities compared to LILRB1 or LILRB2. Binds with high
affinity to the surface of monocytes, leading to abolish LPS-
induced TNF-alpha production by monocytes.
{ECO:0000269|PubMed:21559424, ECO:0000269|PubMed:24085305}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8N6C8-1; Sequence=Displayed;
Name=2;
IsoId=Q8N6C8-2; Sequence=VSP_045887;
Name=3;
IsoId=Q8N6C8-3; Sequence=VSP_045886;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Detected in B-cells, and at lower levels in
natural killer (NK) cells. Detected in peripheral blood monocytes
and lung. {ECO:0000269|PubMed:9278324,
ECO:0000269|PubMed:9548455}.
-!- PTM: N-glycosylation is required for ligand binding.
{ECO:0000269|PubMed:24085305}.
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EMBL; U91926; AAB68666.1; -; mRNA.
EMBL; U91927; AAB68667.1; -; mRNA.
EMBL; AF025527; AAB87661.1; -; mRNA.
EMBL; AF014924; AAC51886.1; -; mRNA.
EMBL; AC008984; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC010518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC028208; AAH28208.1; -; mRNA.
EMBL; AF482762; AAM18035.1; -; Genomic_DNA.
EMBL; AF482763; AAM18036.1; -; Genomic_DNA.
EMBL; AF482764; AAM18037.1; -; Genomic_DNA.
EMBL; AF482765; AAM18038.1; -; Genomic_DNA.
EMBL; AF482766; AAM18039.1; -; Genomic_DNA.
EMBL; AF482767; AAM18040.1; -; Genomic_DNA.
EMBL; AF482768; AAM18041.1; -; Genomic_DNA.
EMBL; AF482769; AAM18042.1; -; Genomic_DNA.
RefSeq; NP_001166125.1; NM_001172654.2. [Q8N6C8-2]
RefSeq; NP_006856.3; NM_006865.4. [Q8N6C8-1]
UniGene; Hs.113277; -.
UniGene; Hs.624711; -.
PDB; 3Q2C; X-ray; 2.50 A; A=24-120.
PDBsum; 3Q2C; -.
ProteinModelPortal; Q8N6C8; -.
SMR; Q8N6C8; -.
BioGrid; 116216; 7.
IntAct; Q8N6C8; 1.
STRING; 9606.ENSP00000251390; -.
iPTMnet; Q8N6C8; -.
PhosphoSitePlus; Q8N6C8; -.
BioMuta; LILRA3; -.
DMDM; 92090611; -.
PaxDb; Q8N6C8; -.
PeptideAtlas; Q8N6C8; -.
PRIDE; Q8N6C8; -.
ProteomicsDB; 72158; -.
DNASU; 11026; -.
Ensembl; ENST00000612127; ENSP00000484119; ENSG00000278046. [Q8N6C8-1]
Ensembl; ENST00000615652; ENSP00000482971; ENSG00000273884. [Q8N6C8-1]
Ensembl; ENST00000617541; ENSP00000477708; ENSG00000275841. [Q8N6C8-2]
Ensembl; ENST00000619638; ENSP00000481818; ENSG00000275841. [Q8N6C8-1]
Ensembl; ENST00000620589; ENSP00000480386; ENSG00000276175. [Q8N6C8-1]
GeneID; 11026; -.
KEGG; hsa:11026; -.
UCSC; uc032ini.2; human. [Q8N6C8-1]
CTD; 11026; -.
DisGeNET; 11026; -.
GeneCards; LILRA3; -.
HGNC; HGNC:6604; LILRA3.
MIM; 604818; gene.
neXtProt; NX_Q8N6C8; -.
PharmGKB; PA30378; -.
eggNOG; ENOG410IKJD; Eukaryota.
eggNOG; ENOG41116BR; LUCA.
HOVERGEN; HBG074353; -.
InParanoid; Q8N6C8; -.
KO; K06512; -.
PhylomeDB; Q8N6C8; -.
TreeFam; TF336644; -.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-6798695; Neutrophil degranulation.
GeneWiki; LILRA3; -.
GenomeRNAi; 11026; -.
PRO; PR:Q8N6C8; -.
Proteomes; UP000005640; Chromosome 19.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
GO; GO:0003823; F:antigen binding; TAS:ProtInc.
GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0006952; P:defense response; TAS:ProtInc.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
Gene3D; 2.60.40.10; -; 4.
InterPro; IPR016332; A1B_glyco/leuk_Ig-like_rcpt.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
Pfam; PF13895; Ig_2; 2.
PIRSF; PIRSF001979; Alpha_1B_glycoprot_prd; 1.
SMART; SM00409; IG; 3.
SMART; SM00408; IGc2; 3.
SUPFAM; SSF48726; SSF48726; 4.
PROSITE; PS50835; IG_LIKE; 3.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Alternative splicing;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Immunity; Immunoglobulin domain; Polymorphism; Receptor;
Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 23 {ECO:0000269|PubMed:15340161}.
CHAIN 24 439 Leukocyte immunoglobulin-like receptor
subfamily A member 3.
/FTId=PRO_0000014818.
DOMAIN 27 108 Ig-like C2-type 1.
DOMAIN 119 224 Ig-like C2-type 2.
DOMAIN 226 315 Ig-like C2-type 3.
DOMAIN 326 415 Ig-like C2-type 4.
CARBOHYD 140 140 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:24085305}.
CARBOHYD 281 281 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:24085305}.
CARBOHYD 302 302 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:24085305}.
CARBOHYD 341 341 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:24085305}.
CARBOHYD 431 431 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:24085305}.
DISULFID 49 98 {ECO:0000244|PDB:3Q2C,
ECO:0000269|PubMed:21559424}.
DISULFID 145 197 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 157 167 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 246 297 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 346 397 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 1 1 M -> MHRGLIHPQSSAVGGDAM (in isoform 3).
{ECO:0000305}.
/FTId=VSP_045886.
VAR_SEQ 158 221 Missing (in isoform 2).
{ECO:0000303|PubMed:9079806}.
/FTId=VSP_045887.
VARIANT 3 3 P -> S (in dbSNP:rs11574606).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9278324,
ECO:0000269|PubMed:9548455}.
/FTId=VAR_016990.
VARIANT 107 107 L -> R (in dbSNP:rs6509862).
{ECO:0000269|PubMed:12750859}.
/FTId=VAR_016991.
VARIANT 301 301 Y -> H (in dbSNP:rs4473306).
{ECO:0000269|PubMed:12750859}.
/FTId=VAR_016992.
CONFLICT 105 105 A -> V (in Ref. 5; AAH28208).
{ECO:0000305}.
CONFLICT 223 223 S -> P (in Ref. 1; AAB68667).
{ECO:0000305}.
CONFLICT 250 250 A -> T (in Ref. 6; AAM18037).
{ECO:0000305}.
CONFLICT 371 371 S -> L (in Ref. 1; AAB68667).
{ECO:0000305}.
STRAND 30 35 {ECO:0000244|PDB:3Q2C}.
STRAND 37 40 {ECO:0000244|PDB:3Q2C}.
STRAND 45 50 {ECO:0000244|PDB:3Q2C}.
STRAND 52 56 {ECO:0000244|PDB:3Q2C}.
STRAND 58 65 {ECO:0000244|PDB:3Q2C}.
HELIX 68 72 {ECO:0000244|PDB:3Q2C}.
HELIX 75 79 {ECO:0000244|PDB:3Q2C}.
STRAND 82 87 {ECO:0000244|PDB:3Q2C}.
HELIX 90 92 {ECO:0000244|PDB:3Q2C}.
STRAND 94 102 {ECO:0000244|PDB:3Q2C}.
TURN 103 105 {ECO:0000244|PDB:3Q2C}.
STRAND 106 108 {ECO:0000244|PDB:3Q2C}.
STRAND 114 119 {ECO:0000244|PDB:3Q2C}.
SEQUENCE 439 AA; 47472 MW; 3932C6DA202ED5F5 CRC64;
MTPILTVLIC LGLSLDPRTH VQAGPLPKPT LWAEPGSVIT QGSPVTLRCQ GSLETQEYHL
YREKKTALWI TRIPQELVKK GQFPILSITW EHAGRYCCIY GSHTAGLSES SDPLELVVTG
AYSKPTLSAL PSPVVTSGGN VTIQCDSQVA FDGFILCKEG EDEHPQCLNS HSHARGSSRA
IFSVGPVSPS RRWSYRCYGY DSRAPYVWSL PSDLLGLLVP GVSKKPSLSV QPGPVVAPGE
KLTFQCGSDA GYDRFVLYKE WGRDFLQRPG RQPQAGLSQA NFTLGPVSRS YGGQYTCSGA
YNLSSEWSAP SDPLDILITG QIRARPFLSV RPGPTVASGE NVTLLCQSQG GMHTFLLTKE
GAADSPLRLK SKRQSHKYQA EFPMSPVTSA HAGTYRCYGS LSSNPYLLTH PSDPLELVVS
GAAETLSPPQ NKSDSKAGE


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