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Killer cell lectin-like receptor subfamily B member 1 (C-type lectin domain family 5 member B) (HNKR-P1a) (NKR-P1A) (Natural killer cell surface protein P1A) (CD antigen CD161)

 KLRB1_HUMAN             Reviewed;         225 AA.
Q12918; Q24K24;
14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
16-OCT-2019, entry version 133.
RecName: Full=Killer cell lectin-like receptor subfamily B member 1;
AltName: Full=C-type lectin domain family 5 member B;
AltName: Full=HNKR-P1a;
Short=NKR-P1A;
AltName: Full=Natural killer cell surface protein P1A;
AltName: CD_antigen=CD161;
Name=KLRB1; Synonyms=CLEC5B, NKRP1A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], GLYCOSYLATION, HOMODIMERIZATION, TISSUE
SPECIFICITY, AND FUNCTION.
PubMed=8077657;
Lanier L.L., Chang C., Phillips J.H.;
"Human NKR-P1A: a disulfide-linked homodimer of the C-type lectin
superfamily expressed by a subset of NK and T lymphocytes.";
J. Immunol. 153:2417-2428(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-168.
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).
[3]
INDUCTION BY IL12.
PubMed=9603467;
DOI=10.1002/(sici)1521-4141(199805)28:05<1611::aid-immu1611>3.0.co;2-6;
Poggi A., Costa P., Tomasello E., Moretta L.;
"IL-12-induced up-regulation of NKRP1A expression in human NK cells
and consequent NKRP1A-mediated down-regulation of NK cell
activation.";
Eur. J. Immunol. 28:1611-1616(1998).
[4]
TISSUE SPECIFICITY.
PubMed=12100027; DOI=10.1046/j.1365-2249.2002.01886.x;
Iiai T., Watanabe H., Suda T., Okamoto H., Abo T., Hatakeyama K.;
"CD161+ T (NT) cells exist predominantly in human intestinal
epithelium as well as in liver.";
Clin. Exp. Immunol. 129:92-98(2002).
[5]
INTERACTION WITH CLEC2D.
PubMed=16339512; DOI=10.4049/jimmunol.175.12.7791;
Aldemir H., Prod'homme V., Dumaurier M.-J., Retiere C., Poupon G.,
Cazareth J., Bihl F., Braud V.M.;
"Lectin-like transcript 1 is a ligand for the CD161 receptor.";
J. Immunol. 175:7791-7795(2005).
[6]
INTERACTION WITH CLEC2D.
PubMed=16339513; DOI=10.4049/jimmunol.175.12.7796;
Rosen D.B., Bettadapura J., Alsharifi M., Mathew P.A., Warren H.S.,
Lanier L.L.;
"Lectin-like transcript-1 is a ligand for the inhibitory human NKR-P1A
receptor.";
J. Immunol. 175:7796-7799(2005).
[7]
FUNCTION, AND INTERACTION WITH SMPD1.
PubMed=16455998; DOI=10.4049/jimmunol.176.4.2397;
Pozo D., Vales-Gomez M., Mavaddat N., Williamson S.C., Chisholm S.E.,
Reyburn H.;
"CD161 (human NKR-P1A) signaling in NK cells involves the activation
of acid sphingomyelinase.";
J. Immunol. 176:2397-2406(2006).
[8]
FUNCTION AS A LECTIN.
PubMed=16925668; DOI=10.1111/j.1399-3089.2006.00332.x;
Christiansen D., Mouhtouris E., Milland J., Zingoni A., Santoni A.,
Sandrin M.S.;
"Recognition of a carbohydrate xenoepitope by human NKRP1A (CD161).";
Xenotransplantation 13:440-446(2006).
[9]
INTERACTION WITH CLEC2D.
PubMed=20843815; DOI=10.1074/jbc.m110.179622;
Germain C., Bihl F., Zahn S., Poupon G., Dumaurier M.J.,
Rampanarivo H.H., Padkjaer S.B., Spee P., Braud V.M.;
"Characterization of alternatively spliced transcript variants of
CLEC2D gene.";
J. Biol. Chem. 285:36207-36215(2010).
-!- FUNCTION: Plays an inhibitory role on natural killer (NK) cells
cytotoxicity. Activation results in specific acid
sphingomyelinase/SMPD1 stimulation with subsequent marked
elevation of intracellular ceramide. Activation also leads to
AKT1/PKB and RPS6KA1/RSK1 kinases stimulation as well as markedly
enhanced T-cell proliferation induced by anti-CD3. Acts as a
lectin that binds to the terminal carbohydrate Gal-alpha(1,3)Gal
epitope as well as to the N-acetyllactosamine epitope. Binds also
to CLEC2D/LLT1 as a ligand and inhibits NK cell-mediated
cytotoxicity as well as interferon-gamma secretion in target
cells. {ECO:0000269|PubMed:16455998, ECO:0000269|PubMed:16925668,
ECO:0000269|PubMed:8077657}.
-!- SUBUNIT: Homodimer; disulfide-linked. Interacts with acid
sphingomyelinase/SMPD1. {ECO:0000269|PubMed:16339512,
ECO:0000269|PubMed:16339513, ECO:0000269|PubMed:16455998,
ECO:0000269|PubMed:20843815}.
-!- INTERACTION:
Q9UHP7-1:CLEC2D; NbExp=2; IntAct=EBI-2805465, EBI-13640978;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed in a subset of NK cells
predominantly in intestinal epithelium and liver. Detected in
peripheral blood T-cells and preferentially in adult T-cells with
a memory antigenic phenotype. {ECO:0000269|PubMed:12100027,
ECO:0000269|PubMed:8077657}.
-!- INDUCTION: By IL12/interleukin-12 in NK cells.
{ECO:0000269|PubMed:9603467}.
-!- PTM: N-glycosylated. Contains sialic acid residues.
{ECO:0000269|PubMed:8077657}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=NKRP1;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_248";
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EMBL; U11276; AAA21605.1; -; mRNA.
EMBL; BC113997; AAI13998.1; -; mRNA.
EMBL; BC114516; AAI14517.1; -; mRNA.
CCDS; CCDS8601.1; -.
PIR; I38700; I38700.
RefSeq; NP_002249.1; NM_002258.2.
PDB; 5MGR; X-ray; 1.80 A; A/B=90-225.
PDB; 5MGS; X-ray; 1.90 A; A/B/C/D/E/F/G/H=90-225.
PDB; 5MGT; X-ray; 1.90 A; C/D/E/F=90-225.
PDBsum; 5MGR; -.
PDBsum; 5MGS; -.
PDBsum; 5MGT; -.
SMR; Q12918; -.
IntAct; Q12918; 2.
STRING; 9606.ENSP00000229402; -.
BioMuta; KLRB1; -.
DMDM; 74722301; -.
MassIVE; Q12918; -.
PaxDb; Q12918; -.
PeptideAtlas; Q12918; -.
PRIDE; Q12918; -.
ProteomicsDB; 59026; -.
DNASU; 3820; -.
Ensembl; ENST00000229402; ENSP00000229402; ENSG00000111796.
GeneID; 3820; -.
KEGG; hsa:3820; -.
UCSC; uc010sgt.3; human.
CTD; 3820; -.
DisGeNET; 3820; -.
GeneCards; KLRB1; -.
HGNC; HGNC:6373; KLRB1.
HPA; HPA039113; -.
MIM; 602890; gene.
neXtProt; NX_Q12918; -.
OpenTargets; ENSG00000111796; -.
PharmGKB; PA30162; -.
eggNOG; KOG4297; Eukaryota.
eggNOG; ENOG410XPJ1; LUCA.
GeneTree; ENSGT00940000154685; -.
HOGENOM; HOG000074586; -.
InParanoid; Q12918; -.
KO; K06543; -.
OMA; TEIRWIC; -.
OrthoDB; 1341815at2759; -.
PhylomeDB; Q12918; -.
TreeFam; TF337735; -.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
GeneWiki; KLRB1; -.
GenomeRNAi; 3820; -.
Pharos; Q12918; -.
PRO; PR:Q12918; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000111796; Expressed in 130 organ(s), highest expression level in mononuclear cell.
Genevisible; Q12918; HS.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0030246; F:carbohydrate binding; TAS:ProtInc.
GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
CDD; cd03593; CLECT_NK_receptors_like; 1.
Gene3D; 3.10.100.10; -; 1.
InterPro; IPR001304; C-type_lectin-like.
InterPro; IPR016186; C-type_lectin-like/link_sf.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR033992; NKR-like_CTLD.
Pfam; PF00059; Lectin_C; 1.
SMART; SM00034; CLECT; 1.
SUPFAM; SSF56436; SSF56436; 1.
PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Disulfide bond; Glycoprotein; Lectin;
Membrane; Polymorphism; Receptor; Reference proteome; Signal-anchor;
Transmembrane; Transmembrane helix.
CHAIN 1 225 Killer cell lectin-like receptor
subfamily B member 1.
/FTId=PRO_0000260000.
TOPO_DOM 1 45 Cytoplasmic. {ECO:0000255}.
TRANSMEM 46 66 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 67 225 Extracellular. {ECO:0000255}.
DOMAIN 101 211 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
CARBOHYD 157 157 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 94 105 {ECO:0000255|PROSITE-ProRule:PRU00040}.
DISULFID 122 210 {ECO:0000255|PROSITE-ProRule:PRU00040}.
DISULFID 189 202 {ECO:0000255|PROSITE-ProRule:PRU00040}.
VARIANT 168 168 I -> T (in dbSNP:rs1135816).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_028981.
STRAND 92 94 {ECO:0000244|PDB:5MGR}.
STRAND 99 101 {ECO:0000244|PDB:5MGR}.
STRAND 104 108 {ECO:0000244|PDB:5MGR}.
HELIX 115 124 {ECO:0000244|PDB:5MGR}.
HELIX 135 142 {ECO:0000244|PDB:5MGR}.
STRAND 152 159 {ECO:0000244|PDB:5MGR}.
TURN 160 163 {ECO:0000244|PDB:5MGR}.
STRAND 164 167 {ECO:0000244|PDB:5MGR}.
STRAND 188 192 {ECO:0000244|PDB:5MGR}.
STRAND 197 201 {ECO:0000244|PDB:5MGR}.
STRAND 206 213 {ECO:0000244|PDB:5MGR}.
SEQUENCE 225 AA; 25415 MW; 01BFA925445B83B0 CRC64;
MDQQAIYAEL NLPTDSGPES SSPSSLPRDV CQGSPWHQFA LKLSCAGIIL LVLVVTGLSV
SVTSLIQKSS IEKCSVDIQQ SRNKTTERPG LLNCPIYWQQ LREKCLLFSH TVNPWNNSLA
DCSTKESSLL LIRDKDELIH TQNLIRDKAI LFWIGLNFSL SEKNWKWING SFLNSNDLEI
RGDAKENSCI SISQTSVYSE YCSTEIRWIC QKELTPVRNK VYPDS


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