CX3CR1

CX3CR1 (C-X3-C Motif Chemokine Receptor 1) is a Protein Coding gene. Diseases associated with CX3CR1 include Macular Degeneration, Age-Related, 12 and Human Immunodeficiency Virus Type 1. Among its related pathways are Akt Signaling and Hematopoietic Stem Cell Differentiation Pathways and Lineage-specific Markers. Gene Ontology (GO) annotations related to this gene include G-protein coupled receptor activity and chemokine receptor activity. An important paralog of this gene is CCR4.

C-X3-C Motif Chemokine Receptor 1

Receptor for the C-X3-C chemokine fractalkine (CX3CL1) present on many early leukocyte cells; CX3CR1-CX3CL1 signaling exerts distinct functions in different tissue compartments, such as immune response, inflammation, cell adhesion and chemotaxis (PubMed:9390561, PubMed:9782118, PubMed:12055230, PubMed:23125415).

CX3CR1-CX3CL1 signaling mediates cell migratory functions (By similarity).

Responsible for the recruitment of natural killer (NK) cells to inflamed tissues (By similarity).

Acts as a regulator of inflammation process leading to atherogenesis by mediating macrophage and monocyte recruitment to inflamed atherosclerotic plaques, promoting cell survival (By similarity).

Involved in airway inflammation by promoting interleukin 2-producing T helper (Th2) cell survival in inflamed lung (By similarity).

Involved in the migration of circulating monocytes to non-inflamed tissues, where they differentiate into macrophages and dendritic cells (By similarity).

Acts as a negative regulator of angiogenesis, probably by promoting macrophage chemotaxis (PubMed:14581400, PubMed:18971423).

Plays a key role in brain microglia by regulating inflammatory response in the central nervous system (CNS) and regulating synapse maturation (By similarity).

Required to restrain the microglial inflammatory response in the CNS and the resulting parenchymal damage in response to pathological stimuli (By similarity).

Involved in brain development by participating to synaptic pruning, a natural process during which brain microglia eliminates extra synapses during postnatal development (By similarity).

Synaptic pruning by microglia is required to promote the maturation of circuit connectivity during brain development (By similarity).

Acts as an important regulator of the gut microbiota by controlling immunity to intestinal bacteria and fungi (By similarity).

Expressed in lamina propria dendritic cells in the small intestine, which form transepithelial dendrites capable of taking up bacteria in order to provide defense against pathogenic bacteria (By similarity).

Required to initiate innate and adaptive immune responses against dissemination of commensal fungi (mycobiota) component of the gut: expressed in mononuclear phagocytes (MNPs) and acts by promoting induction of antifungal IgG antibodies response to confer protection against disseminated C.albicans or C.auris infection (PubMed:29326275).

Also acts as a receptor for C-C motif chemokine CCL26, inducing cell chemotaxis (PubMed:20974991).

Isoform 1:
(Microbial infection) Acts as coreceptor with CD4 for HIV-1 virus envelope protein.

Isoform 2:
(Microbial infection) Acts as coreceptor with CD4 for HIV-1 virus envelope protein (PubMed:14607932).

May have more potent HIV-1 coreceptothr activity than isoform 1 (PubMed:14607932).

Isoform 3:
(Microbial infection) Acts as coreceptor with CD4 for HIV-1 virus envelope protein (PubMed:14607932).

May have more potent HIV-1 coreceptor activity than isoform 1 (PubMed:14607932).

Autocrine signaling Source: ARUK-UCL
Calcium-mediated signaling Source: GO_Central
Cell adhesion Source: ARUK-UCL
Cell-cell signaling Source: ARUK-UCL
Cell chemotaxis Source: GO_Central
Cellular defense response Source: ProtInc
Cellular response to lipopolysaccharide Source: ARUK-UCL
Cellular response to transforming growth factor beta stimulus Source: Ensembl
Central nervous system maturation Source: ARUK-UCL
Chemotaxis Source: ARUK-UCL
G protein-coupled receptor signaling pathway Source: Reactome
Immune response Source: GO_Central
Innate immune response Source: ARUK-UCL
Leukocyte tethering or rolling Source: ARUK-UCL
Memory Source: Ensembl
Modulation of chemical synaptic transmission Source: ARUK-UCL
Multiple spine synapse organization, single dendrite Source: ARUK-UCL
Negative regulation of apoptotic signaling pathway Source: ARUK-UCL
Negative regulation of cell migration Source: Ensembl
Negative regulation of hippocampal neuron apoptotic process Source: ARUK-UCL
Negative regulation of interleukin-1 beta production Source: ARUK-UCL
Negative regulation of long-term synaptic potentiation Source: Ensembl
Phospholipase C-activating G protein-coupled receptor signaling pathway Source: ARUK-UCL
Positive regulation of angiogenesis Source: Ensembl
Positive regulation of cytosolic calcium ion concentration Source: GO_Central
Positive regulation of I-kappaB phosphorylation Source: ARUK-UCL
Positive regulation of microglial cell migration Source: Ensembl
Positive regulation of neuroblast proliferation Source: ARUK-UCL
Positive regulation of neurogenesis Source: ARUK-UCL
Positive regulation of NF-kappaB transcription factor activity Source: ARUK-UCL
Positive regulation of protein kinase B signaling Source: ARUK-UCL
Regulation of microglial cell migration Source: ARUK-UCL
Regulation of neurogenesis Source: ARUK-UCL
Regulation of nitric oxide biosynthetic process Source: ARUK-UCL
Regulation of synaptic plasticity Source: ARUK-UCL
Regulation of tumor necrosis factor production Source: ARUK-UCL
Response to ischemia Source: ARUK-UCL
Response to wounding Source: ProtInc
Social behavior Source: ARUK-UCL
Synapse maturation Source: ARUK-UCL
Synapse pruning Source: ARUK-UCL
Viral process Source: UniProtKB-KW

Cell membrane

Macular degeneration, age-related, 12 (ARMD12):
A form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.

Extracellular: 1-31
Helical: 32-59
Cytoplasmic: 60-69
Helical: 70-90
Extracellular: 91-103
Helical: 104-125
Cytoplasmic: 126-142
Helical: 143-167
Extracellular: 168-195
Helical: 196-215
Cytoplasmic: 216-231
Helical: 232-256
Extracellular: 257-273
Helical: 274-297
Cytoplasmic: 298-355

This protein is not N-glycosylated which is unusual for G-protein-coupled receptors.