Probable pathogen-recognition receptor involved in peripheral immune surveillance in liver. May mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. Is a receptor for ICAM3, probably by binding to mannose-like carbohydrates. (Microbial infection) Acts as an attachment receptor for Ebolavirus. (Microbial infection) Acts as an attachment receptor for Hepatitis C virus. (Microbial infection) Acts as an attachment receptor for HIV-1. (Microbial infection) Acts as an attachment receptor for Human coronavirus 229E. (Microbial infection) Acts as an attachment receptor for Human cytomegalovirus/HHV-5. (Microbial infection) Acts as an attachment receptor for Influenzavirus. (Microbial infection) Acts as an attachment receptor for SARS-CoV. (Microbial infection) Acts as an attachment receptor for West-nile virus. (Microbial infection) Acts as an attachment receptor for Japanese encephalitis virus. (Microbial infection) Acts as an attachment receptor for Marburg virus glycoprotein. (Microbial infection) Recognition of M.bovis by dendritic cells may occur partially via this molecule. Homotetramer. (Microbial infection) Interacts with ebola virus glycoprotein (PubMed:12050398, PubMed:12502850). (Microbial infection) Interacts with hepatitis C virus E1 and E2 protein (PubMed:15371595, PubMed:16816373). (Microbial infection) Interacts with HIV-1 gp120 (PubMed:21277928, PubMed:12502850). (Microbial infection) Interacts with human coronavirus 229E spike glycoprotein. (Microbial infection) Interacts with human cytomegalovirus/HHV-5 gB protein. (Microbial infection) Interacts with influenzavirus hemagglutinin. (Microbial infection) Interacts with SARS-CoV spike glycoprotein. (Microbial infection) Interacts with west-nile virus envelope protein E. (Microbial infection) Interacts with Japanese encephalitis virus E protein. (Microbial infection) Interacts with Marburg virus glycoprotein. (Microbial infection) Interacts with M.bovis LprG. Additional isoforms seem to exist. Several splicing events may occur independently in a modular way. Deletion of the transmembrane domain encoding exon through alternative splicing produces soluble isoforms. Predominantly highly expressed in liver sinusoidal endothelial cells and in lymph node. Found in placental endothelium but not in macrophages. Expressed in type II alveolar cells and lung endothelial cells. The tandem repeat domain, also called neck domain, mediates oligomerization. The number of repeats in the tandem repeat domain is shown to vary between 3 and 9 per allele thus contributing to a further variability in addition to alternative splicing. The shown 7 repeat-containing form has been shown to be the most frequent one (53.9%) in a study with 350 Caucasian individuals. In vitro, is a receptor for HIV-1 and transmits HIV-1 to permissive T-cells. May be due to intron retention. May be due to intron retention. Non-canonical intron-exon splice junction. May be due to intron retention. Aberrant splicing. DC-SIGNR