Q6QLQ4
uniprot
Q6QLQ4
canonical
amino_acid_sequence
MKYHSHIENLDEDGYTQLDFSTQDIHKRPRGSEKGSQAPSSPWRPIAVGLGILCFVVVVVAAVLGALGEYGHNSGRNPEEKDNFLSRNKENHKPTESSLDEKVAPSKASQTTGGFSQPCLPNWIMHGKSCYLFSFSGNSWYGSKRHCSQLGAHLLKIDNSKEFEFIESQTSSHRINAFWIGLSRNQSEGPWFWEDGSAFFPNSFQVRNTAPQESLLHNCVWIHGSEVYNQICNTSSYSICEKEL
uniprot
proteins
function
FUNCTION: Lectin that functions as a pattern recognizing receptor (PRR) specific for beta-1,3-linked and beta-1,6-linked glucans, which constitute cell wall constituents from pathogenic bacteria and fungi (PubMed:11544516, PubMed:15213161, PubMed:17159984). Necessary for the TLR2-mediated inflammatory response and activation of NF-kappa-B: upon beta-glucan binding, recruits SYK via its ITAM motif and promotes a signaling cascade that activates some CARD domain-BCL10-MALT1 (CBM) signalosomes, leading to the activation of NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways which stimulate expression of genes encoding pro-inflammatory cytokines and chemokines (PubMed:12719479, PubMed:15731053, PubMed:16825490, PubMed:32358020). Enhances cytokine production in macrophages and dendritic cells (PubMed:15845454). Mediates production of reactive oxygen species in the cell (PubMed:12719479, PubMed:15731053, PubMed:16825490). Mediates phagocytosis of C.albicans conidia (PubMed:15729357, PubMed:16825490). Binds T-cells in a way that does not involve their surface glycans and plays a role in T-cell activation (PubMed:10779524). Stimulates T-cell proliferation (PubMed:10779524). Induces phosphorylation of SCIMP after binding beta-glucans (PubMed:27288407). {ECO:0000269|PubMed:10779524, ECO:0000269|PubMed:11544516, ECO:0000269|PubMed:12719479, ECO:0000269|PubMed:15213161, ECO:0000269|PubMed:15729357, ECO:0000269|PubMed:15731053, ECO:0000269|PubMed:15845454, ECO:0000269|PubMed:16825490, ECO:0000269|PubMed:17159984, ECO:0000269|PubMed:27288407, ECO:0000269|PubMed:32358020}.
uniprot
proteins
mass_dalton
27420
uniprot
proteins
mutagenesis
MUTAGEN 221; /note="W->A: Loss of glucan binding. Abolishes activation of NF-kappa-B."; /evidence="ECO:0000269|PubMed:15213161"; MUTAGEN 223; /note="H->A: Loss of glucan binding. Abolishes activation of NF-kappa-B."; /evidence="ECO:0000269|PubMed:15213161"; MUTAGEN 232; /note="C->A: Abolishes cell surface expression."; /evidence="ECO:0000269|PubMed:15213161
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:10779524}.; PTM: Phosphorylated on tyrosine residues in response to beta-glucan binding. {ECO:0000269|PubMed:12719479}.
uniprot
proteins
pubmed
10779524
uniprot
proteins
pubmed
11544516
uniprot
proteins
pubmed
12719479
uniprot
proteins
pubmed
15213161
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15729357
uniprot
proteins
pubmed
15731053
uniprot
proteins
pubmed
15845454
uniprot
proteins
pubmed
16825490
uniprot
proteins
pubmed
17159984
uniprot
proteins
pubmed
17473009
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
27288407
uniprot
proteins
pubmed
32358020
uniprot
proteins
sequence_length
244
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10779524, ECO:0000269|PubMed:15213161}; Single-pass type II membrane protein {ECO:0000269|PubMed:10779524, ECO:0000269|PubMed:15213161}. Note=Enriched on zymosan phagosomes. Enrichment does not depend on opsonization.
uniprot
proteins
transmembrane_region
TRANSMEM 50..70; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins