CX3C1_RAT
ID CX3C1_RAT Reviewed; 354 AA.
AC P35411;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=CX3C chemokine receptor 1 {ECO:0000250|UniProtKB:P49238};
DE Short=C-X3-C CKR-1 {ECO:0000250|UniProtKB:P49238};
DE Short=CX3CR1 {ECO:0000250|UniProtKB:P49238};
DE AltName: Full=Fractalkine receptor {ECO:0000250|UniProtKB:P49238};
GN Name=Cx3cr1 {ECO:0000250|UniProtKB:P49238};
GN Synonyms=Rbs11 {ECO:0000303|PubMed:8047298};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND ABSENCE OF
RP GLYCOSYLATION.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RX PubMed=8047298; DOI=10.1016/0304-3940(94)90362-x;
RA Harrison J.K., Barber C.M., Lynch K.R.;
RT "cDNA cloning of a G-protein-coupled receptor expressed in rat spinal cord
RT and brain related to chemokine receptors.";
RL Neurosci. Lett. 169:85-89(1994).
CC -!- FUNCTION: Receptor for the C-X3-C chemokine fractalkine (CX3CL1)
CC present on many early leukocyte cells; CX3CR1-CX3CL1 signaling exerts
CC distinct functions in different tissue compartments, such as immune
CC response, inflammation, cell adhesion and chemotaxis. CX3CR1-CX3CL1
CC signaling mediates cell migratory functions. Responsible for the
CC recruitment of natural killer (NK) cells to inflamed tissues. Acts as a
CC regulator of inflammation process leading to atherogenesis by mediating
CC macrophage and monocyte recruitment to inflamed atherosclerotic
CC plaques, promoting cell survival. Involved in airway inflammation by
CC promoting interleukin 2-producing T helper (Th2) cell survival in
CC inflamed lung. Involved in the migration of circulating monocytes to
CC non-inflamed tissues, where they differentiate into macrophages and
CC dendritic cells. Acts as a negative regulator of angiogenesis, probably
CC by promoting macrophage chemotaxis. Plays a key role in brain microglia
CC by regulating inflammatory response in the central nervous system (CNS)
CC and regulating synapse maturation. Required to restrain the microglial
CC inflammatory response in the CNS and the resulting parenchymal damage
CC in response to pathological stimuli. Involved in brain development by
CC participating in synaptic pruning, a natural process during which brain
CC microglia eliminates extra synapses during postnatal development.
CC Synaptic pruning by microglia is required to promote the maturation of
CC circuit connectivity during brain development. Acts as an important
CC regulator of the gut microbiota by controlling immunity to intestinal
CC bacteria and fungi. Expressed in lamina propria dendritic cells in the
CC small intestine, which form transepithelial dendrites capable of taking
CC up bacteria in order to provide defense against pathogenic bacteria.
CC Required to initiate innate and adaptive immune responses against
CC dissemination of commensal fungi (mycobiota) component of the gut:
CC expressed in mononuclear phagocytes (MNPs) and acts by promoting
CC induction of antifungal IgG antibodies response to confer protection
CC against disseminated C.albicans or C.auris infection (By similarity).
CC Also acts as a receptor for C-C motif chemokine CCL26, inducing cell
CC chemotaxis (By similarity). {ECO:0000250|UniProtKB:P49238,
CC ECO:0000250|UniProtKB:Q9Z0D9}.
CC -!- SUBUNIT: Found in a ternary complex with CX3CL1 and ITGAV:ITGB3 or
CC ITGA4:ITGB1. {ECO:0000250|UniProtKB:P49238}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P49238};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Most abundant in adult spinal cord, brain, kidney,
CC gut, uterus and testes. {ECO:0000269|PubMed:8047298}.
CC -!- PTM: This protein is not N-glycosylated which is unusual for G-protein-
CC coupled receptors. {ECO:0000269|PubMed:8047298}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U04808; AAB87093.1; -; mRNA.
DR PIR; I58186; I58186.
DR RefSeq; NP_598218.1; NM_133534.1.
DR AlphaFoldDB; P35411; -.
DR SMR; P35411; -.
DR STRING; 10116.ENSRNOP00000025019; -.
DR ChEMBL; CHEMBL2346491; -.
DR PhosphoSitePlus; P35411; -.
DR PaxDb; P35411; -.
DR Ensembl; ENSRNOT00000025019; ENSRNOP00000025019; ENSRNOG00000018509.
DR Ensembl; ENSRNOT00000093935; ENSRNOP00000097085; ENSRNOG00000018509.
DR GeneID; 171056; -.
DR KEGG; rno:171056; -.
DR UCSC; RGD:620137; rat.
DR CTD; 1524; -.
DR RGD; 620137; Cx3cr1.
DR eggNOG; ENOG502QVQK; Eukaryota.
DR GeneTree; ENSGT01020000230359; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; P35411; -.
DR OMA; FRKYLYH; -.
DR OrthoDB; 900867at2759; -.
DR PhylomeDB; P35411; -.
DR TreeFam; TF330966; -.
DR Reactome; R-RNO-380108; Chemokine receptors bind chemokines.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:P35411; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000018509; Expressed in frontal cortex and 16 other tissues.
DR Genevisible; P35411; RN.
DR GO; GO:0009986; C:cell surface; IDA:ARUK-UCL.
DR GO; GO:0097447; C:dendritic tree; IDA:ARUK-UCL.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0032809; C:neuronal cell body membrane; IDA:ARUK-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0019957; F:C-C chemokine binding; IBA:GO_Central.
DR GO; GO:0016493; F:C-C chemokine receptor activity; IBA:GO_Central.
DR GO; GO:0019960; F:C-X3-C chemokine binding; ISS:UniProtKB.
DR GO; GO:0016495; F:C-X3-C chemokine receptor activity; IDA:RGD.
DR GO; GO:0004950; F:chemokine receptor activity; IMP:ARUK-UCL.
DR GO; GO:0031737; F:CX3C chemokine receptor binding; ISO:RGD.
DR GO; GO:0004896; F:cytokine receptor activity; ISO:RGD.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISO:RGD.
DR GO; GO:0002250; P:adaptive immune response; ISS:UniProtKB.
DR GO; GO:0061760; P:antifungal innate immune response; ISS:UniProtKB.
DR GO; GO:0035425; P:autocrine signaling; IGI:ARUK-UCL.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0060326; P:cell chemotaxis; IMP:ARUK-UCL.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:RGD.
DR GO; GO:0021626; P:central nervous system maturation; ISO:RGD.
DR GO; GO:0070098; P:chemokine-mediated signaling pathway; IMP:ARUK-UCL.
DR GO; GO:0006935; P:chemotaxis; ISO:RGD.
DR GO; GO:0048874; P:host-mediated regulation of intestinal microbiota composition; ISS:UniProtKB.
DR GO; GO:0006955; P:immune response; ISS:UniProtKB.
DR GO; GO:0030595; P:leukocyte chemotaxis; ISS:UniProtKB.
DR GO; GO:0050901; P:leukocyte tethering or rolling; ISO:RGD.
DR GO; GO:0007613; P:memory; IMP:RGD.
DR GO; GO:0002282; P:microglial cell activation involved in immune response; ISS:UniProtKB.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0150090; P:multiple spine synapse organization, single dendrite; ISO:RGD.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IGI:ARUK-UCL.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:RGD.
DR GO; GO:0110091; P:negative regulation of hippocampal neuron apoptotic process; IGI:ARUK-UCL.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IMP:ARUK-UCL.
DR GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; IMP:RGD.
DR GO; GO:1904150; P:negative regulation of microglial cell mediated cytotoxicity; ISS:UniProtKB.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:1903721; P:positive regulation of I-kappaB phosphorylation; IGI:ARUK-UCL.
DR GO; GO:1904141; P:positive regulation of microglial cell migration; IMP:ARUK-UCL.
DR GO; GO:0090026; P:positive regulation of monocyte chemotaxis; ISO:RGD.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IMP:RGD.
DR GO; GO:0050769; P:positive regulation of neurogenesis; ISO:RGD.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IGI:ARUK-UCL.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IGI:ARUK-UCL.
DR GO; GO:0045428; P:regulation of nitric oxide biosynthetic process; ISO:RGD.
DR GO; GO:0032680; P:regulation of tumor necrosis factor production; ISO:RGD.
DR GO; GO:0002931; P:response to ischemia; IGI:ARUK-UCL.
DR GO; GO:0035176; P:social behavior; ISO:RGD.
DR GO; GO:0060074; P:synapse maturation; ISO:RGD.
DR GO; GO:0098883; P:synapse pruning; ISS:UniProtKB.
DR InterPro; IPR005387; Chemokine_CX3CR1.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01562; FRACTALKINER.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Immunity; Inflammatory response;
KW Innate immunity; Membrane; Phosphoprotein; Receptor; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..354
FT /note="CX3C chemokine receptor 1"
FT /id="PRO_0000069328"
FT TOPO_DOM 1..32
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..60
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..104
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..126
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..168
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..196
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..216
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..257
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..274
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..298
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..354
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 345
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0D9"
FT DISULFID 103..176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 354 AA; 40327 MW; CFC4578095E77376 CRC64;
MPTSFPELDL ENFEYDDSAE ACYLGDIVAF GTIFLSIFYS LVFTFGLVGN LLVVLALTNS
RKSKSITDIY LLNLALSDLL FVATLPFWTH YLISHEGLHN AMCKLTTAFF FIGFFGGIFF
ITVISIDRYL AIVLAANSMN NRTVQHGVTI SLGVWAAAIL VASPQFMFTK RKDNECLGDY
PEVLQEIWPV LRNSEVNILG FVLPLLIMSF CYFRIVRTLF SCKNRKKARA IRLILLVVVV
FFLFWTPYNI VIFLETLKFY NFFPSCGMKR DLRWALSVTE TVAFSHCCLN PFIYAFAGEK
FRRYLRHLYN KCLAVLCGRP VHAGFSTESQ RSRQDSILSS LTHYTSEGEG SLLL
