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Protein

Killer cell lectin-like receptor subfamily G member 1

Gene

Klrg1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  • carbohydrate binding Source: MGI

GO - Biological processi

  • cell surface receptor signaling pathway Source: MGI
  • innate immune response Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Immunity, Innate immunity

Keywords - Ligandi

Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
Killer cell lectin-like receptor subfamily G member 1
Alternative name(s):
Mast cell function-associated antigen 2F1
Gene namesi
Name:Klrg1
Synonyms:Mafa
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1355294. Klrg1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3333CytoplasmicSequence analysisAdd
BLAST
Transmembranei34 – 5623Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini57 – 188132ExtracellularSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi5 – 51S → A: Decreases association with PTPN11. 1 Publication
Mutagenesisi7 – 71Y → F: Abolishes the formation of KLRG1/PTPN11 and KLRG1/INPP5D. 1 Publication
Mutagenesisi8 – 81S → A: Enhances association with PTPN11. 1 Publication
Mutagenesisi10 – 101L → A: Abrogates completely INPP5D recruitment. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 188188Killer cell lectin-like receptor subfamily G member 1PRO_0000331257Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi75 ↔ 86PROSITE-ProRule annotation1 Publication
Glycosylationi82 – 821N-linked (GlcNAc...)Sequence analysis
Glycosylationi97 – 971N-linked (GlcNAc...)Sequence analysis
Disulfide bondi103 ↔ 183PROSITE-ProRule annotation1 Publication
Disulfide bondi162 ↔ 175PROSITE-ProRule annotation1 Publication

Post-translational modificationi

Phosphorylated in response to monoclonal antibody G63 binding and antigenic stimulation.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiO88713.
PRIDEiO88713.

PTM databases

PhosphoSiteiO88713.

Expressioni

Tissue specificityi

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.2 Publications

Inductioni

By pathogens and viruses infections.2 Publications

Gene expression databases

BgeeiO88713.
GenevisibleiO88713. MM.

Interactioni

Subunit structurei

Forms a monomer and homodimer; disulfide-linked (By similarity). Interacts (via ITIM motif) with PTPN11 and INPP5D.By similarity2 Publications

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000032207.

Structurei

Secondary structure

1
188
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi80 – 823Combined sources
Beta strandi85 – 895Combined sources
Helixi96 – 10510Combined sources
Helixi119 – 1235Combined sources
Beta strandi131 – 14313Combined sources
Beta strandi162 – 1665Combined sources
Beta strandi169 – 1735Combined sources
Beta strandi179 – 1868Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FF8X-ray2.00C/D75-188[»]
3FF9X-ray1.80A/B75-188[»]
ProteinModelPortaliO88713.
SMRiO88713. Positions 75-188.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO88713.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini82 – 184103C-type lectinPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi5 – 106ITIM motif

Domaini

Sequence similaritiesi

Contains 1 C-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4297. Eukaryota.
ENOG410XPJ1. LUCA.
GeneTreeiENSGT00840000129990.
HOGENOMiHOG000082429.
HOVERGENiHBG103557.
InParanoidiO88713.
KOiK10076.
OMAiFCLARDS.
OrthoDBiEOG70KGR1.
PhylomeDBiO88713.
TreeFamiTF336674.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O88713-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADSSIYSTL ELPEAPQVQD ESRWKLKAVL HRPHLSRFAM VALGLLTVIL
60 70 80 90 100
MSLLMYQRIL CCGSKDSTCS HCPSCPILWT RNGSHCYYFS MEKKDWNSSL
110 120 130 140 150
KFCADKGSHL LTFPDNQGVK LFGEYLGQDF YWIGLRNIDG WRWEGGPALS
160 170 180
LRILTNSLIQ RCGAIHRNGL QASSCEVALQ WICKKVLY
Length:188
Mass (Da):21,396
Last modified:August 1, 1999 - v2
Checksum:i876336802EA134F1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti120 – 1201Missing in AAI01954 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF097357 mRNA. Translation: AAD03718.1.
AJ010751 mRNA. Translation: CAA09342.1.
AF317727 Genomic DNA. Translation: AAK40082.1.
BC101953 mRNA. Translation: AAI01954.1.
BC103546 mRNA. Translation: AAI03547.1.
BC103547 mRNA. Translation: AAI03548.1.
BC103548 mRNA. Translation: AAI03549.1.
CCDSiCCDS20492.1.
RefSeqiNP_058666.1. NM_016970.1.
UniGeneiMm.20434.

Genome annotation databases

EnsembliENSMUST00000032207; ENSMUSP00000032207; ENSMUSG00000030114.
GeneIDi50928.
KEGGimmu:50928.
UCSCiuc009dov.2. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

MCFA

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF097357 mRNA. Translation: AAD03718.1.
AJ010751 mRNA. Translation: CAA09342.1.
AF317727 Genomic DNA. Translation: AAK40082.1.
BC101953 mRNA. Translation: AAI01954.1.
BC103546 mRNA. Translation: AAI03547.1.
BC103547 mRNA. Translation: AAI03548.1.
BC103548 mRNA. Translation: AAI03549.1.
CCDSiCCDS20492.1.
RefSeqiNP_058666.1. NM_016970.1.
UniGeneiMm.20434.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FF8X-ray2.00C/D75-188[»]
3FF9X-ray1.80A/B75-188[»]
ProteinModelPortaliO88713.
SMRiO88713. Positions 75-188.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000032207.

PTM databases

PhosphoSiteiO88713.

Proteomic databases

PaxDbiO88713.
PRIDEiO88713.

Protocols and materials databases

DNASUi50928.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032207; ENSMUSP00000032207; ENSMUSG00000030114.
GeneIDi50928.
KEGGimmu:50928.
UCSCiuc009dov.2. mouse.

Organism-specific databases

CTDi10219.
MGIiMGI:1355294. Klrg1.

Phylogenomic databases

eggNOGiKOG4297. Eukaryota.
ENOG410XPJ1. LUCA.
GeneTreeiENSGT00840000129990.
HOGENOMiHOG000082429.
HOVERGENiHBG103557.
InParanoidiO88713.
KOiK10076.
OMAiFCLARDS.
OrthoDBiEOG70KGR1.
PhylomeDBiO88713.
TreeFamiTF336674.

Miscellaneous databases

EvolutionaryTraceiO88713.
NextBioi307943.
PROiO88713.
SOURCEiSearch...

Gene expression databases

BgeeiO88713.
GenevisibleiO88713. MM.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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."
    Hanke T., Corral L., Vance R.E., Raulet D.H.
    Eur. J. Immunol. 28:4409-4417(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: CB-17/SCID.
  2. "Virus-activated CD8 T cells and lymphokine-activated NK cells express the mast cell function-associated antigen, an inhibitory C-type lectin."
    Blaser C., Kaufmann M., Pircher H.
    J. Immunol. 161:6451-6454(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  3. "Genomic structure, alternative splicing, and physical mapping of the killer cell lectin-like receptor G1 gene (KLRG1), the mouse homologue of MAFA."
    Voehringer D., Kaufmann M., Pircher H.
    Immunogenetics 52:206-211(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/SvEvTacfBr.
    Tissue: Spleen.
  4. "Viral infections induce abundant numbers of senescent CD8 T cells."
    Voehringer D., Blaser C., Brawand P., Raulet D.H., Hanke T., Pircher H.
    J. Immunol. 167:4838-4843(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY VIRAL INFECTIONS.
  5. "Inhibitory functions of the killer cell lectin-like receptor G1 molecule during the activation of mouse NK cells."
    Robbins S.H., Nguyen K.B., Takahashi N., Mikayama T., Biron C.A., Brossay L.
    J. Immunol. 168:2585-2589(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY PATHOGENS INFECTIONS.
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. "Identification of E-cadherin as a ligand for the murine killer cell lectin-like receptor G1."
    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.
    J. Immunol. 176:1311-1315(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: LIGAND-BINDING.
  8. Cited for: LIGAND-BINDING, INTERACTION WITH PTPN11 AND INPP5D, MUTAGENESIS OF SER-5; TYR-7; SER-8 AND LEU-10.
  9. "Structure of natural killer cell receptor KLRG1 bound to E-cadherin reveals basis for MHC-independent missing self recognition."
    Li Y., Hofmann M., Wang Q., Teng L., Chlewicki L.K., Pircher H., Mariuzza R.A.
    Immunity 31:35-46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 75-188 ALONE AND IN COMPLEX WITH HUMAN E-CADHERIN, FUNCTION, SUBCELLULAR LOCATION, DISULFIDE BONDS.

Entry informationi

Entry nameiKLRG1_MOUSE
AccessioniPrimary (citable) accession number: O88713
Secondary accession number(s): Q3T1F0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: August 1, 1999
Last modified: May 11, 2016
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.