CLEC4E
entrez
26253
canonical
uniprot
Q9ULY5
canonical
ensembl
ENSG00000166523
resolver
ensp
ENSP00000299663
resolver
ensp
ENSP00000443034
resolver
enst
ENST00000299663
resolver
enst
ENST00000545274
resolver
genesymbol
CLEC4E
resolver
genesymbol_syn
CLECSF9
resolver
genesymbol_syn
MINCLE
resolver
hgnc
HGNC:14555
resolver
uniprot
B2R6Q6
resolver
uniprot
F5H5X7
resolver
uniprot_entry
CLC4E_HUMAN
resolver
uniprot_entry
F5H5X7_HUMAN
resolver
uniprot_sec
B2R6Q6
resolver
amino_acid_sequence
MNSSKSSETQCTERGCFSSQMFLWTVAGIPILFLSACFITRCVVTFRIFQTCDEKKFQLPENFTELSCYNYGSGSVKNCCPLNWEYFQSSCYFFSTDTISWALSLKNCSAMGAHLVVINSQEEQEFLSYKKPKMREFFIGLSDQVVEGQWQWVDGTPLTKSLSFWDVGEPNNIATLEDCATMRDSSNPRQNWNDVTCFLNYFRICEMVGINPLNKGKSL
uniprot
proteins
function
FUNCTION: Calcium-dependent lectin that acts as a pattern recognition receptor (PRR) of the innate immune system: recognizes damage-associated molecular patterns (DAMPs) of abnormal self and pathogen-associated molecular patterns (PAMPs) of bacteria and fungi (PubMed:18509109, PubMed:23602766). The PAMPs notably include mycobacterial trehalose 6,6'-dimycolate (TDM), a cell wall glycolipid with potent adjuvant immunomodulatory functions (PubMed:23602766, PubMed:24101491). Interacts with signaling adapter Fc receptor gamma chain/FCER1G to form a functional complex in myeloid cells (By similarity). Binding of mycobacterial trehalose 6,6'-dimycolate (TDM) to this receptor complex leads to phosphorylation of the immunoreceptor tyrosine-based activation motif (ITAM) of FCER1G, triggering activation of SYK, CARD9 and NF-kappa-B, consequently driving maturation of antigen-presenting cells and shaping antigen-specific priming of T-cells toward effector T-helper 1 and T-helper 17 cell subtypes (By similarity). Also recognizes alpha-mannose residues on pathogenic fungi of the genus Malassezia and mediates macrophage activation (By similarity). Through recognition of DAMPs released upon nonhomeostatic cell death, enables immune sensing of damaged self and promotes inflammatory cell infiltration into the damaged tissue (By similarity). {ECO:0000250|UniProtKB:Q9R0Q8, ECO:0000269|PubMed:18509109, ECO:0000269|PubMed:23602766, ECO:0000269|PubMed:24101491}.
uniprot
proteins
mass_dalton
25073
uniprot
proteins
mutagenesis
MUTAGEN 169..171; /note="EPN->QPD,EPD: Impairs binding to trehalose-6,6'-dimycolate."; /evidence="ECO:0000269|PubMed:24101491"; MUTAGEN 172; /note="N->Q: Impairs trehalose-6,6'-dimycolate (TDM)-induced NF-kappa-B activation."; /evidence="ECO:0000269|PubMed:24101491"; MUTAGEN 183; /note="R->V: Reduces trehalose-6,6'-dimycolate (TDM)-induced NF-kappa-B activation."; /evidence="ECO:0000269|PubMed:24101491"; MUTAGEN 198..199; /note="FL->AA: Reduces trehalose-6,6'-dimycolate (TDM)-induced NF-kappa-B activation."; /evidence="ECO:0000269|PubMed:24101491
uniprot
proteins
pubmed
10528209
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
18490740
uniprot
proteins
pubmed
18509109
uniprot
proteins
pubmed
18776906
uniprot
proteins
pubmed
23602766
uniprot
proteins
pubmed
24101491
uniprot
proteins
sequence_length
219
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18490740, ECO:0000305|PubMed:24101491}; Single-pass type II membrane protein {ECO:0000305}. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:Q9R0Q8}.
uniprot
proteins
transmembrane_region
TRANSMEM 20..40; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins