CLEC1B
entrez
51266
canonical
uniprot
Q9P126
canonical
ensembl
ENSG00000165682
resolver
ensp
ENSP00000298527
resolver
ensp
ENSP00000327169
resolver
genesymbol
CLEC1B
resolver
genesymbol_syn
CLEC2
resolver
hgnc
HGNC:24356
resolver
uniprot
Q6UWX7
resolver
uniprot
Q8NHR6
resolver
uniprot_entry
CLC1B_HUMAN
resolver
uniprot_sec
Q6UWX7
resolver
uniprot_sec
Q8NHR6
resolver
amino_acid_sequence
MQDEDGYITLNIKTRKPALISVGSASSSWWRVMALILLILCVGMVVGLVALGIWSVMQRNYLQGENENRTGTLQQLAKRFCQYVVKQSELKGTFKGHKCSPCDTNWRYYGDSCYGFFRHNLTWEESKQYCTDMNATLLKIDNRNIVEYIKARTHLIRWVGLSRQKSNEVWKWEDGSVISENMFEFLEDGKGNMNCAYFHNGKMHPTFCENKHYLMCERKAGMTKVDQLP
uniprot
proteins
function
FUNCTION: C-type lectin-like receptor that serves as a platelet receptor for the lymphatic endothelial marker PDPN (PubMed:18215137). Plays an essential role in blood/lymphatic vessel separation and thrombus formation through homophilic association (PubMed:22556408). Acts as a negative regulator of lymphatic endothelial cell behavior by inhibiting proliferation, migration, and tube formation (PubMed:22556408). Upon ligand binding, triggers a signaling cascade via sequential activation of SRC and SYK tyrosine kinases, leading to activation of PLCG2 (PubMed:18955485). Through this pathway, mediates platelet adhesion, aggregation, and secretion in response to PDPN-expressing cells. During embryonic development, plays a central role in cerebrovascular formation and blood/lymphatic vessel separation. Interacts with PDPN on neuroepithelial cells to promote platelet activation, thereby ensuring maturation and integrity of cerebrovascular structures and preventing hemorrhage. {ECO:0000269|PubMed:18215137, ECO:0000269|PubMed:18955485, ECO:0000269|PubMed:22556408}.; FUNCTION: (Microbial infection) Acts as a receptor for the platelet-aggregating snake venom protein rhodocytin. Rhodocytin binding leads to tyrosine phosphorylation and this promotes the binding of spleen tyrosine kinase (SYK) and initiation of downstream tyrosine phosphorylation events and activation of PLCG2 (PubMed:16174766, PubMed:18955485). {ECO:0000269|PubMed:18955485, ECO:0000305|PubMed:16174766}.; FUNCTION: (Microbial infection) Acts as an attachment factor for Human immunodeficiency virus type 1 (HIV-1) and facilitates its capture by platelets (PubMed:16940507). {ECO:0000305|PubMed:16940507}.
uniprot
proteins
mass_dalton
26596
uniprot
proteins
mutagenesis
MUTAGEN 7; /note="Y->F: Loss of activation upon podoplanin or rhodocytin stimulation."; /evidence="ECO:0000269|PubMed:18955485"; MUTAGEN 150; /note="K->A: Substantial reduction in rhodocytin binding."; /evidence="ECO:0000269|PubMed:17132623"; MUTAGEN 171; /note="K->A: Significant reduction in rhodocytin binding."; /evidence="ECO:0000269|PubMed:17132623"; MUTAGEN 184; /note="E->A: Significant reduction in rhodocytin binding."; /evidence="ECO:0000269|PubMed:17132623"; MUTAGEN 187; /note="E->A: Significant reduction in rhodocytin binding."; /evidence="ECO:0000269|PubMed:17132623"; MUTAGEN 188; /note="D->A: Significant reduction in rhodocytin binding."; /evidence="ECO:0000269|PubMed:17132623"; MUTAGEN 190; /note="K->A: Significant reduction in rhodocytin binding."; /evidence="ECO:0000269|PubMed:17132623"; MUTAGEN 192; /note="N->A: Significant reduction in rhodocytin binding."; /evidence="ECO:0000269|PubMed:17132623
uniprot
proteins
post_translational_modification
PTM: Glycosylated. {ECO:0000269|PubMed:16174766, ECO:0000269|PubMed:18215137}.; PTM: Phosphorylated on tyrosine residue in response to rhodocytin binding. {ECO:0000269|PubMed:16174766, ECO:0000269|PubMed:20154219}.
uniprot
proteins
pubmed
10671229
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16174766
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
16940507
uniprot
proteins
pubmed
17132623
uniprot
proteins
pubmed
18215137
uniprot
proteins
pubmed
18955485
uniprot
proteins
pubmed
19785988
uniprot
proteins
pubmed
19824697
uniprot
proteins
pubmed
20154219
uniprot
proteins
pubmed
22556408
uniprot
proteins
pubmed
25694214
uniprot
proteins
sequence_length
229
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
uniprot
proteins
transmembrane_region
TRANSMEM 34..54; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins