Klrd1
entrez
16643
canonical
uniprot
O54707
canonical
ensembl
ENSMUSG00000030165
resolver
ensp
ENSMUSP00000107694
resolver
enst
ENSMUST00000112063
resolver
genesymbol
Klrd1
resolver
genesymbol_syn
Cd94
resolver
uniprot
O54708
resolver
uniprot_entry
KLRD1_MOUSE
resolver
uniprot_sec
O54708
resolver
amino_acid_sequence
MAVSRITRWRLMSVIFGIKCLFLMVTLGVLLINSFTIQNIQSTPSPTTTVEFQEVSECCVCLDKWVGHQCNCYFISKEEKSWKRSRDFCASQNSSLLQPQSRNELSFMNFSQTFFWIGMHYSEKRNAWLWEDGTVPSKDLFPEFSVIRPEHCIVYSPSKSVSAESCENKNRYICKKLPI
uniprot
proteins
function
FUNCTION: Immune receptor involved in self-nonself discrimination. In complex with KLRC1 or KLRC2 on cytotoxic and regulatory lymphocyte subsets, recognizes non-classical major histocompatibility (MHC) class Ib molecule MHC-E loaded with self-peptides derived from the signal sequence of classical MHC class Ia and non-classical MHC class Ib molecules. Enables cytotoxic cells to monitor the expression of MHC class I molecules in healthy cells and to tolerate self. Primarily functions as a ligand binding subunit as it lacks the capacity to signal. {ECO:0000250|UniProtKB:Q13241}.; FUNCTION: KLRD1-KLRC1 acts as an immune inhibitory receptor. Key inhibitory receptor on natural killer (NK) cells that regulates their activation and effector functions. Dominantly counteracts T cell receptor signaling on a subset of memory/effector CD8-positive T cells as part of an antigen-driven response to avoid autoimmunity. On intraepithelial CD8-positive gamma-delta regulatory T cells triggers TGFB1 secretion, which in turn limits the cytotoxic programming of intraepithelial CD8-positive alpha-beta T cells, distinguishing harmless from pathogenic antigens. In MHC-E-rich tumor microenvironment, acts as an immune inhibitory checkpoint and may contribute to progressive loss of effector functions of NK cells and tumor-specific T cells, a state known as cell exhaustion. Upon MHC-E-peptide binding, transmits intracellular signals through KLRC1 immunoreceptor tyrosine-based inhibition motifs (ITIMs) by recruiting INPP5D/SHIP-1 and INPPL1/SHIP-2 tyrosine phosphatases to ITIMs, and ultimately opposing signals transmitted by activating receptors through dephosphorylation of proximal signaling molecules. {ECO:0000250|UniProtKB:Q13241}.; FUNCTION: KLRD1-KLRC2 acts as an immune activating receptor. On cytotoxic lymphocyte subsets recognizes MHC-E loaded with signal sequence-derived peptides from non-classical MHC class Ib MHC-G molecules, likely playing a role in the generation and effector functions of adaptive NK cells and in maternal-fetal tolerance during pregnancy. Regulates the effector functions of terminally differentiated cytotoxic lymphocyte subsets, and in particular may play a role in adaptive NK cell response to viral infection. Upon MHC-E-peptide binding, transmits intracellular signals via the adapter protein TYROBP/DAP12, triggering the phosphorylation of proximal signaling molecules and cell activation. {ECO:0000250|UniProtKB:Q13241}.
uniprot
proteins
mass_dalton
20808
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
9464811
uniprot
proteins
pubmed
9600963
uniprot
proteins
sequence_length
179
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q13241}; Single-pass type II membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 11..31; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins