Q99PA5
uniprot
Q99PA5
canonical
amino_acid_sequence
MEPCRSLALFAGSLGLTSSLIALTTDFWIVATGPHFSAHSGLWPTSQETQVAGYIHVTQSFCILAVLWGLVSVSFLILSCIPALSAPGRGPLVSTVMAFSAALSILVAMAVYTSMRWSQTPFSQVQTFFSWSFYLGWVSFILFLFAGCLSLGAHCRTRRAEYETL
uniprot
proteins
function
FUNCTION: Regulates cytotoxic granule exocytosis in effector lymphocytes, thus acting as a critical mediator of inflammation in a broad range of infectious and non-infectious diseases (PubMed:32839608). Essential for cytotoxic degranulation of natural killer (NK) cells and CD8(+) T-cells and for the activation of CD4(+) T-cells following infection (PubMed:32839608). Plays a critical role in CD8(+) T-cell and NK cell-mediated cytolysis of target cells and contributes to the cytolytic activity via the perforin/granzyme pathway by enhancing exocytosis of LAMP1-carrying lytic granules (PubMed:32839608, PubMed:33911019). Contributes to NK cell-mediated control of cancer metastasis (PubMed:32839608). {ECO:0000269|PubMed:32839608, ECO:0000269|PubMed:33911019}.
uniprot
proteins
mass_dalton
17958
uniprot
proteins
protein_family
PMP-22/EMP/MP20 family
uniprot
proteins
pubmed
11290961
uniprot
proteins
pubmed
32839608
uniprot
proteins
pubmed
33911019
uniprot
proteins
sequence_length
165
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q16617}; Multi-pass membrane protein {ECO:0000255}. Cytolytic granule membrane {ECO:0000305|PubMed:32839608}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 9..29; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 61..81; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 92..112; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 133..153; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins