CLEC12A
entrez
160364
canonical
uniprot
Q5QGZ9
canonical
ensembl
ENSG00000172322
resolver
ensp
ENSP00000302804
resolver
ensp
ENSP00000345448
resolver
ensp
ENSP00000347916
resolver
ensp
ENSP00000405244
resolver
ensp
ENSP00000763246
resolver
ensp
ENSP00000798064
resolver
ensp
ENSP00000800921
resolver
genesymbol
CLEC12A
resolver
genesymbol_syn
CLL1
resolver
genesymbol_syn
DCAL2
resolver
genesymbol_syn
KLRL1
resolver
genesymbol_syn
MICL
resolver
hgnc
HGNC:31713
resolver
uniprot
B2RA16
resolver
uniprot
Q6P4H1
resolver
uniprot
Q6RH77
resolver
uniprot
Q6RH78
resolver
uniprot
Q8TDQ6
resolver
uniprot_entry
CL12A_HUMAN
resolver
uniprot_sec
B2RA16
resolver
uniprot_sec
Q6P4H1
resolver
uniprot_sec
Q6RH77
resolver
uniprot_sec
Q6RH78
resolver
uniprot_sec
Q8TDQ6
resolver
amino_acid_sequence
MSEEVTYADLQFQNSSEMEKIPEIGKFGEKAPPAPSHVWRPAALFLTLLCLLLLIGLGVLASMFHVTLKIEMKKMNKLQNISEELQRNISLQLMSNMNISNKIRNLSTTLQTIATKLCRELYSKEQEHKCKPCPRRWIWHKDSCYFLSDDVQTWQESKMACAAQNASLLKINNKNALEFIKSQSRSYDYWLGLSPEEDSTRGMRVDNIINSSAWVIRNAPDLNNMYCGYINRLYVQYYHCTYKKRMICEKMANPVQLGSTYFREA
uniprot
proteins
function
FUNCTION: Myeloid inhibitory C-type lectin receptor that acts as a negative regulator of myeloid cell activation (PubMed:14739280, PubMed:15238421, PubMed:16239426, PubMed:34234773, PubMed:38367667, PubMed:38386511, PubMed:39143217). Myeloid cell inhibition is required to limit proinflammatory pathways and protect against excessive inflammation (By similarity). Specifically recognizes and binds various structures, such as neutrophil extracellular traps (NETs) or monosodium urate crystals (PubMed:38367667, PubMed:38386511, PubMed:39143217). Also acts as a pattern-recognition receptor for pathogen-associated molecules, such as plasmodium hemozoin or mycobacterial micolic acid (PubMed:31269448, PubMed:36542980). Ligand-binding induces phosphorylation of its ITIM motif, followed by recruitment of tyrosine-protein phosphatases PTPN6 and PTPN11, which counteract tyrosine-protein kinase SYK, thereby preventing myeloid cell activation (PubMed:14739280, PubMed:16239426, PubMed:34234773). Acts as a pattern-recognition receptor for NETs in neutrophils: specifically recognizes DNA in NETs, leading to inhibit neutrophil activation and limit further NET formation (PubMed:39143217). This regulation is essential for controlling key neutrophil responses and limit NET-mediated inflammatory conditions (By similarity). Also recognizes dead cells by acting as a receptor for monosodium urate crystals, leading to down-regulate neutrophil activation (PubMed:38367667, PubMed:38386511). Binding to monosodium urate crystals also promotes the type I interferon response (By similarity). Acts as an inhibitor of natural killer (NK) cell cytotoxicity (PubMed:15238421). Also acts as an inhibitor of dendritic cell maturation in an IL10-dependent manner (PubMed:16239426). {ECO:0000250|UniProtKB:Q504P2, ECO:0000269|PubMed:14739280, ECO:0000269|PubMed:15238421, ECO:0000269|PubMed:16239426, ECO:0000269|PubMed:31269448, ECO:0000269|PubMed:34234773, ECO:0000269|PubMed:36542980, ECO:0000269|PubMed:38367667, ECO:0000269|PubMed:38386511, ECO:0000269|PubMed:39143217}.
uniprot
proteins
mass_dalton
30762
uniprot
proteins
mutagenesis
MUTAGEN 7; /note="Y->F: Abolished phosphorylation."; /evidence="ECO:0000269|PubMed:34234773"; MUTAGEN 185; /note="R->A: Strongly decreased ligand-binding."; /evidence="ECO:0000269|PubMed:38386511"; MUTAGEN 232; /note="R->A: Decreased ligand-binding."; /evidence="ECO:0000269|PubMed:38386511"; MUTAGEN 234; /note="Y->A: Decreased ligand-binding."; /evidence="ECO:0000269|PubMed:38386511
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Tyr-7 by SRC in the ITIM motif following ligand-binding, promoting recruitment of tyrosine-protein phosphatases PTPN6 and PTPN11. {ECO:0000269|PubMed:14739280, ECO:0000269|PubMed:15238421, ECO:0000269|PubMed:16239426, ECO:0000269|PubMed:34234773}.; PTM: Highly N-glycosylated; glycosylation varies between cell types. {ECO:0000269|PubMed:14739280, ECO:0000269|PubMed:15238421, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16838277}.
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14739280
uniprot
proteins
pubmed
15238421
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15548716
uniprot
proteins
pubmed
16239426
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
16838277
uniprot
proteins
pubmed
31269448
uniprot
proteins
pubmed
34234773
uniprot
proteins
pubmed
36542980
uniprot
proteins
pubmed
38367667
uniprot
proteins
pubmed
38386511
uniprot
proteins
pubmed
39143217
uniprot
proteins
sequence_length
265
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14739280, ECO:0000269|PubMed:15238421, ECO:0000269|PubMed:15548716, ECO:0000269|PubMed:16239426, ECO:0000269|PubMed:16838277, ECO:0000269|PubMed:34234773, ECO:0000269|PubMed:38367667}; Single-pass type II membrane protein {ECO:0000255}. Note=Ligand binding leads to internalization (PubMed:16239426). Clusters at phagocytic vesicles upon monosodium urate crystal-binding (PubMed:38367667). {ECO:0000269|PubMed:16239426, ECO:0000269|PubMed:38367667}.
uniprot
proteins
transmembrane_region
TRANSMEM 44..64; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins