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Killer cell lectin-like receptor subfamily G member 1 (Mast cell function-associated antigen 2F1)

 KLRG1_MOUSE             Reviewed;         188 AA.
O88713; Q3T1F0;
29-APR-2008, integrated into UniProtKB/Swiss-Prot.
01-AUG-1999, sequence version 2.
12-SEP-2018, entry version 131.
RecName: Full=Killer cell lectin-like receptor subfamily G member 1;
AltName: Full=Mast cell function-associated antigen 2F1;
Name=Klrg1; Synonyms=Mafa;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=CB-17/SCID;
PubMed=9862378;
DOI=10.1002/(SICI)1521-4141(199812)28:12<4409::AID-IMMU4409>3.0.CO;2-3;
Hanke T., Corral L., Vance R.E., Raulet D.H.;
"2F1 antigen, the mouse homolog of the rat 'mast cell function-
associated antigen', is a lectin-like type II transmembrane receptor
expressed by natural killer cells.";
Eur. J. Immunol. 28:4409-4417(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=9862665;
Blaser C., Kaufmann M., Pircher H.;
"Virus-activated CD8 T cells and lymphokine-activated NK cells express
the mast cell function-associated antigen, an inhibitory C-type
lectin.";
J. Immunol. 161:6451-6454(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/SvEvTacfBr; TISSUE=Spleen;
PubMed=11220622; DOI=10.1007/s002510000282;
Voehringer D., Kaufmann M., Pircher H.;
"Genomic structure, alternative splicing, and physical mapping of the
killer cell lectin-like receptor G1 gene (KLRG1), the mouse homologue
of MAFA.";
Immunogenetics 52:206-211(2001).
[4]
INDUCTION BY VIRAL INFECTIONS.
PubMed=11673487; DOI=10.4049/jimmunol.167.9.4838;
Voehringer D., Blaser C., Brawand P., Raulet D.H., Hanke T.,
Pircher H.;
"Viral infections induce abundant numbers of senescent CD8 T cells.";
J. Immunol. 167:4838-4843(2001).
[5]
INDUCTION BY PATHOGENS INFECTIONS.
PubMed=11884419; DOI=10.4049/jimmunol.168.6.2585;
Robbins S.H., Nguyen K.B., Takahashi N., Mikayama T., Biron C.A.,
Brossay L.;
"Inhibitory functions of the killer cell lectin-like receptor G1
molecule during the activation of mouse NK cells.";
J. Immunol. 168:2585-2589(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[7]
LIGAND-BINDING.
PubMed=16424155; DOI=10.4049/jimmunol.176.3.1311;
Gruendemann C., Bauer M., Schweier O., von Oppen N., Laessing U.,
Saudan P., Becker K.-F., Karp K., Hanke T., Bachmann M.F., Pircher H.;
"Identification of E-cadherin as a ligand for the murine killer cell
lectin-like receptor G1.";
J. Immunol. 176:1311-1315(2006).
[8]
LIGAND-BINDING, INTERACTION WITH PTPN11 AND INPP5D, AND MUTAGENESIS OF
SER-5; TYR-7; SER-8 AND LEU-10.
PubMed=17307799; DOI=10.1093/intimm/dxm004;
Tessmer M.S., Fugere C., Stevenaert F., Naidenko O.V., Chong H.J.,
Leclercq G., Brossay L.;
"KLRG1 binds cadherins and preferentially associates with SHIP-1.";
Int. Immunol. 19:391-400(2007).
[9]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 75-188 ALONE AND IN COMPLEX
WITH HUMAN E-CADHERIN, FUNCTION, SUBCELLULAR LOCATION, AND DISULFIDE
BONDS.
PubMed=19604491; DOI=10.1016/j.immuni.2009.04.019;
Li Y., Hofmann M., Wang Q., Teng L., Chlewicki L.K., Pircher H.,
Mariuzza R.A.;
"Structure of natural killer cell receptor KLRG1 bound to E-cadherin
reveals basis for MHC-independent missing self recognition.";
Immunity 31:35-46(2009).
-!- FUNCTION: Plays an inhibitory role on natural killer (NK) cells
and T-cell functions upon binding to their non-MHC ligands. May
mediate missing self recognition by binding to a highly conserved
site on classical cadherins, enabling it to monitor expression of
E-cadherin/CDH1, N-cadherin/CDH2 and R-cadherin/CDH4 on target
cells. {ECO:0000269|PubMed:19604491}.
-!- SUBUNIT: Forms a monomer and homodimer; disulfide-linked (By
similarity). Interacts (via ITIM motif) with PTPN11 and INPP5D.
{ECO:0000250, ECO:0000269|PubMed:17307799,
ECO:0000269|PubMed:19604491}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19604491};
Single-pass type II membrane protein
{ECO:0000269|PubMed:19604491}.
-!- TISSUE SPECIFICITY: Expressed specifically on natural killer (NK)
cells and activated CD8 T-cells. Not detected in spleen, thymus,
lymph node, testis, brain or kidney. Not detected on mast cell
lines, bone marrow-derived mast cells, or peritoneal mast cells.
{ECO:0000269|PubMed:9862378, ECO:0000269|PubMed:9862665}.
-!- INDUCTION: By pathogens and viruses infections.
{ECO:0000269|PubMed:11673487, ECO:0000269|PubMed:11884419}.
-!- DOMAIN: Contains 1 copy 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. Upon
phosphorylation of ITIM motif KLRG1 associates with the two
phosphatases, PTPN11 and INPP5D.
-!- PTM: Phosphorylated in response to monoclonal antibody G63 binding
and antigenic stimulation. {ECO:0000250}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=MCFA;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_176";
-----------------------------------------------------------------------
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EMBL; AF097357; AAD03718.1; -; mRNA.
EMBL; AJ010751; CAA09342.1; -; mRNA.
EMBL; AF317727; AAK40082.1; -; Genomic_DNA.
EMBL; BC101953; AAI01954.1; -; mRNA.
EMBL; BC103546; AAI03547.1; -; mRNA.
EMBL; BC103547; AAI03548.1; -; mRNA.
EMBL; BC103548; AAI03549.1; -; mRNA.
CCDS; CCDS20492.1; -.
RefSeq; NP_058666.1; NM_016970.1.
UniGene; Mm.20434; -.
PDB; 3FF8; X-ray; 2.00 A; C/D=75-188.
PDB; 3FF9; X-ray; 1.80 A; A/B=75-188.
PDBsum; 3FF8; -.
PDBsum; 3FF9; -.
ProteinModelPortal; O88713; -.
SMR; O88713; -.
STRING; 10090.ENSMUSP00000032207; -.
iPTMnet; O88713; -.
PhosphoSitePlus; O88713; -.
PaxDb; O88713; -.
PRIDE; O88713; -.
DNASU; 50928; -.
Ensembl; ENSMUST00000032207; ENSMUSP00000032207; ENSMUSG00000030114.
GeneID; 50928; -.
KEGG; mmu:50928; -.
UCSC; uc009dov.2; mouse.
CTD; 10219; -.
MGI; MGI:1355294; Klrg1.
eggNOG; KOG4297; Eukaryota.
eggNOG; ENOG410XPJ1; LUCA.
GeneTree; ENSGT00710000106527; -.
HOGENOM; HOG000082429; -.
HOVERGEN; HBG103557; -.
InParanoid; O88713; -.
KO; K10076; -.
OMA; NSGWRWE; -.
OrthoDB; EOG091G0MK5; -.
PhylomeDB; O88713; -.
TreeFam; TF336674; -.
EvolutionaryTrace; O88713; -.
PRO; PR:O88713; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000030114; Expressed in 68 organ(s), highest expression level in decidua.
Genevisible; O88713; MM.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0030246; F:carbohydrate binding; ISO:MGI.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:MGI.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
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; Cell membrane; Complete proteome; Disulfide bond;
Glycoprotein; Immunity; Innate immunity; Lectin; Membrane;
Phosphoprotein; Receptor; Reference proteome; Signal-anchor;
Transmembrane; Transmembrane helix.
CHAIN 1 188 Killer cell lectin-like receptor
subfamily G member 1.
/FTId=PRO_0000331257.
TOPO_DOM 1 33 Cytoplasmic. {ECO:0000255}.
TRANSMEM 34 56 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 57 188 Extracellular. {ECO:0000255}.
DOMAIN 82 184 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
MOTIF 5 10 ITIM motif.
CARBOHYD 82 82 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 97 97 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 75 86 {ECO:0000255|PROSITE-ProRule:PRU00040,
ECO:0000269|PubMed:19604491}.
DISULFID 103 183 {ECO:0000255|PROSITE-ProRule:PRU00040,
ECO:0000269|PubMed:19604491}.
DISULFID 162 175 {ECO:0000255|PROSITE-ProRule:PRU00040,
ECO:0000269|PubMed:19604491}.
MUTAGEN 5 5 S->A: Decreases association with PTPN11.
{ECO:0000269|PubMed:17307799}.
MUTAGEN 7 7 Y->F: Abolishes the formation of
KLRG1/PTPN11 and KLRG1/INPP5D.
{ECO:0000269|PubMed:17307799}.
MUTAGEN 8 8 S->A: Enhances association with PTPN11.
{ECO:0000269|PubMed:17307799}.
MUTAGEN 10 10 L->A: Abrogates completely INPP5D
recruitment.
{ECO:0000269|PubMed:17307799}.
CONFLICT 120 120 Missing (in Ref. 6; AAI01954).
{ECO:0000305}.
STRAND 80 82 {ECO:0000244|PDB:3FF9}.
STRAND 85 89 {ECO:0000244|PDB:3FF9}.
HELIX 96 105 {ECO:0000244|PDB:3FF9}.
HELIX 119 123 {ECO:0000244|PDB:3FF9}.
STRAND 131 143 {ECO:0000244|PDB:3FF9}.
STRAND 162 166 {ECO:0000244|PDB:3FF9}.
STRAND 169 173 {ECO:0000244|PDB:3FF9}.
STRAND 179 186 {ECO:0000244|PDB:3FF9}.
SEQUENCE 188 AA; 21396 MW; 876336802EA134F1 CRC64;
MADSSIYSTL ELPEAPQVQD ESRWKLKAVL HRPHLSRFAM VALGLLTVIL MSLLMYQRIL
CCGSKDSTCS HCPSCPILWT RNGSHCYYFS MEKKDWNSSL KFCADKGSHL LTFPDNQGVK
LFGEYLGQDF YWIGLRNIDG WRWEGGPALS LRILTNSLIQ RCGAIHRNGL QASSCEVALQ
WICKKVLY


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