KLRG1_MOUSE
ID KLRG1_MOUSE Reviewed; 188 AA.
AC O88713; Q3T1F0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1999, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Killer cell lectin-like receptor subfamily G member 1;
DE AltName: Full=Mast cell function-associated antigen 2F1;
GN Name=Klrg1; Synonyms=Mafa;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=CB-17/SCID;
RX PubMed=9862378;
RX DOI=10.1002/(sici)1521-4141(199812)28:12<4409::aid-immu4409>3.0.co;2-3;
RA Hanke T., Corral L., Vance R.E., Raulet D.H.;
RT "2F1 antigen, the mouse homolog of the rat 'mast cell function-associated
RT antigen', is a lectin-like type II transmembrane receptor expressed by
RT natural killer cells.";
RL Eur. J. Immunol. 28:4409-4417(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=9862665;
RA Blaser C., Kaufmann M., Pircher H.;
RT "Virus-activated CD8 T cells and lymphokine-activated NK cells express the
RT mast cell function-associated antigen, an inhibitory C-type lectin.";
RL J. Immunol. 161:6451-6454(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvEvTacfBr; TISSUE=Spleen;
RX PubMed=11220622; DOI=10.1007/s002510000282;
RA Voehringer D., Kaufmann M., Pircher H.;
RT "Genomic structure, alternative splicing, and physical mapping of the
RT killer cell lectin-like receptor G1 gene (KLRG1), the mouse homologue of
RT MAFA.";
RL Immunogenetics 52:206-211(2001).
RN [4]
RP INDUCTION BY VIRAL INFECTIONS.
RX PubMed=11673487; DOI=10.4049/jimmunol.167.9.4838;
RA Voehringer D., Blaser C., Brawand P., Raulet D.H., Hanke T., Pircher H.;
RT "Viral infections induce abundant numbers of senescent CD8 T cells.";
RL J. Immunol. 167:4838-4843(2001).
RN [5]
RP INDUCTION BY PATHOGENS INFECTIONS.
RX PubMed=11884419; DOI=10.4049/jimmunol.168.6.2585;
RA Robbins S.H., Nguyen K.B., Takahashi N., Mikayama T., Biron C.A.,
RA Brossay L.;
RT "Inhibitory functions of the killer cell lectin-like receptor G1 molecule
RT during the activation of mouse NK cells.";
RL J. Immunol. 168:2585-2589(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
RP LIGAND-BINDING.
RX PubMed=16424155; DOI=10.4049/jimmunol.176.3.1311;
RA Gruendemann C., Bauer M., Schweier O., von Oppen N., Laessing U.,
RA Saudan P., Becker K.-F., Karp K., Hanke T., Bachmann M.F., Pircher H.;
RT "Identification of E-cadherin as a ligand for the murine killer cell
RT lectin-like receptor G1.";
RL J. Immunol. 176:1311-1315(2006).
RN [8]
RP LIGAND-BINDING, INTERACTION WITH PTPN11 AND INPP5D, AND MUTAGENESIS OF
RP SER-5; TYR-7; SER-8 AND LEU-10.
RX PubMed=17307799; DOI=10.1093/intimm/dxm004;
RA Tessmer M.S., Fugere C., Stevenaert F., Naidenko O.V., Chong H.J.,
RA Leclercq G., Brossay L.;
RT "KLRG1 binds cadherins and preferentially associates with SHIP-1.";
RL Int. Immunol. 19:391-400(2007).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 75-188 ALONE AND IN COMPLEX WITH
RP HUMAN E-CADHERIN, FUNCTION, SUBCELLULAR LOCATION, AND DISULFIDE BONDS.
RX PubMed=19604491; DOI=10.1016/j.immuni.2009.04.019;
RA Li Y., Hofmann M., Wang Q., Teng L., Chlewicki L.K., Pircher H.,
RA Mariuzza R.A.;
RT "Structure of natural killer cell receptor KLRG1 bound to E-cadherin
RT reveals basis for MHC-independent missing self recognition.";
RL Immunity 31:35-46(2009).
CC -!- FUNCTION: Plays an inhibitory role on natural killer (NK) cells and T-
CC cell functions upon binding to their non-MHC ligands. May mediate
CC missing self recognition by binding to a highly conserved site on
CC classical cadherins, enabling it to monitor expression of E-
CC cadherin/CDH1, N-cadherin/CDH2 and R-cadherin/CDH4 on target cells.
CC {ECO:0000269|PubMed:19604491}.
CC -!- SUBUNIT: Forms a monomer and homodimer; disulfide-linked (By
CC similarity). Interacts (via ITIM motif) with PTPN11 and INPP5D.
CC {ECO:0000250, ECO:0000269|PubMed:17307799,
CC ECO:0000269|PubMed:19604491}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19604491};
CC Single-pass type II membrane protein {ECO:0000269|PubMed:19604491}.
CC -!- TISSUE SPECIFICITY: Expressed specifically on natural killer (NK) cells
CC and activated CD8 T-cells. Not detected in spleen, thymus, lymph node,
CC testis, brain or kidney. Not detected on mast cell lines, bone marrow-
CC derived mast cells, or peritoneal mast cells.
CC {ECO:0000269|PubMed:9862378, ECO:0000269|PubMed:9862665}.
CC -!- INDUCTION: By pathogens and viruses infections.
CC {ECO:0000269|PubMed:11673487, ECO:0000269|PubMed:11884419}.
CC -!- DOMAIN: Contains 1 copy 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. Upon phosphorylation of
CC ITIM motif KLRG1 associates with the two phosphatases, PTPN11 and
CC INPP5D.
CC -!- PTM: Phosphorylated in response to monoclonal antibody G63 binding and
CC antigenic stimulation. {ECO:0000250}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=MCFA;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_176";
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DR EMBL; AF097357; AAD03718.1; -; mRNA.
DR EMBL; AJ010751; CAA09342.1; -; mRNA.
DR EMBL; AF317727; AAK40082.1; -; Genomic_DNA.
DR EMBL; BC101953; AAI01954.1; -; mRNA.
DR EMBL; BC103546; AAI03547.1; -; mRNA.
DR EMBL; BC103547; AAI03548.1; -; mRNA.
DR EMBL; BC103548; AAI03549.1; -; mRNA.
DR CCDS; CCDS20492.1; -.
DR RefSeq; NP_058666.1; NM_016970.1.
DR PDB; 3FF8; X-ray; 2.00 A; C/D=75-188.
DR PDB; 3FF9; X-ray; 1.80 A; A/B=75-188.
DR PDBsum; 3FF8; -.
DR PDBsum; 3FF9; -.
DR AlphaFoldDB; O88713; -.
DR SMR; O88713; -.
DR STRING; 10090.ENSMUSP00000032207; -.
DR GlyGen; O88713; 2 sites.
DR iPTMnet; O88713; -.
DR PhosphoSitePlus; O88713; -.
DR PaxDb; O88713; -.
DR PRIDE; O88713; -.
DR Antibodypedia; 23119; 442 antibodies from 34 providers.
DR DNASU; 50928; -.
DR Ensembl; ENSMUST00000032207; ENSMUSP00000032207; ENSMUSG00000030114.
DR GeneID; 50928; -.
DR KEGG; mmu:50928; -.
DR UCSC; uc009dov.2; mouse.
DR CTD; 10219; -.
DR MGI; MGI:1355294; Klrg1.
DR VEuPathDB; HostDB:ENSMUSG00000030114; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000156296; -.
DR HOGENOM; CLU_049894_8_3_1; -.
DR InParanoid; O88713; -.
DR OMA; SCPDFWM; -.
DR OrthoDB; 1299162at2759; -.
DR PhylomeDB; O88713; -.
DR TreeFam; TF336674; -.
DR BioGRID-ORCS; 50928; 4 hits in 73 CRISPR screens.
DR EvolutionaryTrace; O88713; -.
DR PRO; PR:O88713; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; O88713; protein.
DR Bgee; ENSMUSG00000030114; Expressed in gastrula and 44 other tissues.
DR Genevisible; O88713; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030246; F:carbohydrate binding; ISO:MGI.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:MGI.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR CDD; cd03593; CLECT_NK_receptors_like; 1.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR042190; KLRG1.
DR InterPro; IPR033992; NKR-like_CTLD.
DR PANTHER; PTHR47648; PTHR47648; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein; Immunity;
KW Innate immunity; Lectin; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..188
FT /note="Killer cell lectin-like receptor subfamily G member
FT 1"
FT /id="PRO_0000331257"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..56
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..188
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 82..184
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOTIF 5..10
FT /note="ITIM motif"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 75..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:19604491"
FT DISULFID 103..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:19604491"
FT DISULFID 162..175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:19604491"
FT MUTAGEN 5
FT /note="S->A: Decreases association with PTPN11."
FT /evidence="ECO:0000269|PubMed:17307799"
FT MUTAGEN 7
FT /note="Y->F: Abolishes the formation of KLRG1/PTPN11 and
FT KLRG1/INPP5D."
FT /evidence="ECO:0000269|PubMed:17307799"
FT MUTAGEN 8
FT /note="S->A: Enhances association with PTPN11."
FT /evidence="ECO:0000269|PubMed:17307799"
FT MUTAGEN 10
FT /note="L->A: Abrogates completely INPP5D recruitment."
FT /evidence="ECO:0000269|PubMed:17307799"
FT CONFLICT 120
FT /note="Missing (in Ref. 6; AAI01954)"
FT /evidence="ECO:0000305"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:3FF9"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:3FF9"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:3FF9"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:3FF9"
FT STRAND 131..143
FT /evidence="ECO:0007829|PDB:3FF9"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:3FF9"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:3FF9"
FT STRAND 179..186
FT /evidence="ECO:0007829|PDB:3FF9"
SQ 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
