CX3CL1
entrez
6376
canonical
uniprot
P78423
canonical
ensembl
ENSG00000006210
resolver
ensp
ENSP00000006053
resolver
enst
ENST00000006053
resolver
genesymbol
CX3CL1
resolver
genesymbol_syn
FKN
resolver
genesymbol_syn
NTT
resolver
genesymbol_syn
SCYD1
resolver
hgnc
HGNC:10647
resolver
uniprot
A0N0N7
resolver
uniprot
O00672
resolver
uniprot_entry
A0N0N7_HUMAN
resolver
uniprot_entry
X3CL1_HUMAN
resolver
uniprot_sec
O00672
resolver
amino_acid_sequence
MAPISLSWLLRLATFCHLTVLLAGQHHGVTKCNITCSKMTSKIPVALLIHYQQNQASCGKRAIILETRQHRLFCADPKEQWVKDAMQHLDRQAAALTRNGGTFEKQIGEVKPRTTPAAGGMDESVVLEPEATGESSSLEPTPSSQEAQRALGTSPELPTGVTGSSGTRLPPTPKAQDGGPVGTELFRVPPVSTAATWQSSAPHQPGPSLWAEAKTSEAPSTQDPSTQASTASSPAPEENAPSEGQRVWGQGQSPRPENSLEREEMGPVPAHTDAFQDWGPGSMAHVSVVPVSSEGTPSREPVASGSWTPKAEEPIHATMDPQRLGVLITPVPDAQAATRRQAVGLLAFLGLLFCLGVAMFTYQSLQGCPRKMAGEMAEGLRYIPRSCGSNSYVLVPV
uniprot
proteins
function
FUNCTION: Chemokine that acts as a ligand for both CX3CR1 and integrins ITGAV:ITGB3 and ITGA4:ITGB1 (PubMed:12055230, PubMed:21829356, PubMed:23125415, PubMed:9782118, PubMed:9931005). The CX3CR1-CX3CL1 signaling exerts distinct functions in different tissue compartments, such as immune response, inflammation, cell adhesion and chemotaxis (PubMed:12055230, PubMed:9024663, PubMed:9177350, PubMed:9782118). Regulates leukocyte adhesion and migration processes at the endothelium (PubMed:9024663, PubMed:9177350). Can activate integrins in both a CX3CR1-dependent and CX3CR1-independent manner (PubMed:23125415, PubMed:24789099). In the presence of CX3CR1, activates integrins by binding to the classical ligand-binding site (site 1) in integrins (PubMed:23125415, PubMed:24789099). In the absence of CX3CR1, binds to a second site (site 2) in integrins which is distinct from site 1 and enhances the binding of other integrin ligands to site 1 (PubMed:23125415, PubMed:24789099). {ECO:0000269|PubMed:12055230, ECO:0000269|PubMed:21829356, ECO:0000269|PubMed:23125415, ECO:0000269|PubMed:24789099, ECO:0000269|PubMed:9024663, ECO:0000269|PubMed:9177350, ECO:0000269|PubMed:9782118, ECO:0000269|PubMed:9931005}.; FUNCTION: [Processed fractalkine]: The soluble form is chemotactic for T-cells and monocytes, but not for neutrophils. {ECO:0000269|PubMed:9024663}.; FUNCTION: [Fractalkine]: The membrane-bound form promotes adhesion of those leukocytes to endothelial cells. {ECO:0000269|PubMed:9024663}.; FUNCTION: (Microbial infection) Mediates the cytoadherence of erythrocytes infected with parasite P.falciparum (strain 3D7) with endothelial cells by interacting with P.falciparum CBP1 and CBP2 expressed at the surface of erythrocytes (PubMed:27653778). The adhesion prevents the elimination of infected erythrocytes by the spleen (Probable). {ECO:0000269|PubMed:27653778, ECO:0000305|PubMed:27653778}.
uniprot
proteins
mass_dalton
42203
uniprot
proteins
mutagenesis
MUTAGEN 60; /note="K->A: Reduced binding to integrin ITGAV:ITGB3, but no effect on binding to CX3CR1; when associated with A-61."; /evidence="ECO:0000269|PubMed:23125415"; MUTAGEN 60; /note="K->E: Dominant-negative mutant, reduced binding to integrins ITGAV:ITGB3 and ITGA4:ITGB1, no effect on binding to CX3CR1, defective in ternary complex formation, integrin activation and fractalkine signaling and suppression of leukocyte recruitment in the peritonitis model in vivo; when associated with E-61."; /evidence="ECO:0000269|PubMed:23125415, ECO:0000269|PubMed:24789099"; MUTAGEN 61; /note="R->A: Reduced binding to integrin ITGAV:ITGB3, but no effect on binding to CX3CR1; when associated with A-60."; /evidence="ECO:0000269|PubMed:23125415"; MUTAGEN 61; /note="R->E: Dominant-negative mutant, reduced binding to integrins ITGAV:ITGB3 and ITGA4:ITGB1, no effect on binding to CX3CR1, defective in ternary complex formation, integrin activation and fractalkine signaling and suppression of leukocyte recruitment in the peritonitis model in vivo; when associated with E-60."; /evidence="ECO:0000269|PubMed:23125415, ECO:0000269|PubMed:24789099"; MUTAGEN 71; /note="R->A: Loss of binding to CX3CR1 and ability to induce chemotaxis but no effect on binding to integrins."; /evidence="ECO:0000269|PubMed:23125415"; MUTAGEN 78; /note="K->A: Little or no effect on binding to integrin ITGAV:ITGB3."; /evidence="ECO:0000269|PubMed:23125415"; MUTAGEN 78; /note="K->A: Little or no effect on binding to integrin ITGAV:ITGB3; when associated with A-83."; /evidence="ECO:0000269|PubMed:23125415"; MUTAGEN 83; /note="K->A: Little or no effect on binding to integrin ITGAV:ITGB3; when associated with A-78."; /evidence="ECO:0000269|PubMed:23125415
uniprot
proteins
post_translational_modification
PTM: A soluble short 95 kDa form may be released by proteolytic cleavage from the long membrane-anchored form. {ECO:0000269|PubMed:9024663}.; PTM: O-glycosylated with core 1 or possibly core 8 glycans. {ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320}.
uniprot
proteins
protein_family
Intercrine delta family
uniprot
proteins
pubmed
10493829
uniprot
proteins
pubmed
10770945
uniprot
proteins
pubmed
12055230
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19838169
uniprot
proteins
pubmed
21829356
uniprot
proteins
pubmed
22171320
uniprot
proteins
pubmed
23125415
uniprot
proteins
pubmed
23765988
uniprot
proteins
pubmed
24789099
uniprot
proteins
pubmed
25745166
uniprot
proteins
pubmed
27653778
uniprot
proteins
pubmed
29882741
uniprot
proteins
pubmed
9024663
uniprot
proteins
pubmed
9177350
uniprot
proteins
pubmed
9782118
uniprot
proteins
pubmed
9931005
uniprot
proteins
sequence_length
397
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9024663}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Processed fractalkine]: Secreted {ECO:0000269|PubMed:9024663}.
uniprot
proteins
transmembrane_region
TRANSMEM 342..362; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins