CX3C1_RABIT
ID CX3C1_RABIT Reviewed; 356 AA.
AC Q2KTE1;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=CX3C chemokine receptor 1 {ECO:0000303|Ref.1};
DE Short=C-X3-C CKR-1 {ECO:0000303|Ref.1};
DE Short=CX3CR1 {ECO:0000303|Ref.1};
DE AltName: Full=Fractalkine receptor {ECO:0000250|UniProtKB:P49238};
GN Name=CX3CR1 {ECO:0000303|Ref.1};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Karlsson-Svalstedt B., Drmota T.;
RT "Rabbit CX3C chemokine receptor 1 (CX3CR1_RABBIT), complete cDNA.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- PTM: This protein is not N-glycosylated which is unusual for G-protein-
CC coupled receptors. {ECO:0000250|UniProtKB:P35411}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AM183335; CAJ66583.1; -; mRNA.
DR RefSeq; NP_001075603.1; NM_001082134.1.
DR RefSeq; XP_008258422.1; XM_008260200.1.
DR AlphaFoldDB; Q2KTE1; -.
DR SMR; Q2KTE1; -.
DR STRING; 9986.ENSOCUP00000024608; -.
DR Ensembl; ENSOCUT00000028713; ENSOCUP00000024608; ENSOCUG00000027509.
DR GeneID; 100008874; -.
DR KEGG; ocu:100008874; -.
DR CTD; 1524; -.
DR eggNOG; ENOG502QVQK; Eukaryota.
DR GeneTree; ENSGT01020000230359; -.
DR InParanoid; Q2KTE1; -.
DR OrthoDB; 900867at2759; -.
DR Proteomes; UP000001811; Chromosome 9.
DR Bgee; ENSOCUG00000027509; Expressed in brain and 17 other tissues.
DR ExpressionAtlas; Q2KTE1; baseline.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
DR GO; GO:0019960; F:C-X3-C chemokine binding; ISS:UniProtKB.
DR GO; GO:0016495; F:C-X3-C chemokine receptor activity; IEA:Ensembl.
DR GO; GO:0031737; F:CX3C chemokine receptor binding; IEA:Ensembl.
DR GO; GO:0002250; P:adaptive immune response; ISS:UniProtKB.
DR GO; GO:0061760; P:antifungal innate immune response; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:Ensembl.
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:0002282; P:microglial cell activation involved in immune response; ISS:UniProtKB.
DR GO; GO:1904150; P:negative regulation of microglial cell mediated cytotoxicity; ISS:UniProtKB.
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 2: Evidence at transcript 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..356
FT /note="CX3C chemokine receptor 1"
FT /id="PRO_0000375806"
FT TOPO_DOM 1..26
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..47
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..105
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..195
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..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..253
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..277
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..356
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 347
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0D9"
FT DISULFID 103..176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 356 AA; 40234 MW; E5D2CCE4A0D0DEE2 CRC64;
MTTLYSDWAT ESFEYDESSE ACFIGDIVAF GTIFLSIFYS LVFAFGLVGN LLVVCALTSS
RKPKSITDIY LLNLALSDLL FVATLPFWTH YVISEQGFHN AVCKLTTALF FIGFFGGIFF
ITVISIDRYM AIVLAANSIN NRTVQHGVTT SLGVWAAAIL VAAPQFMFTK QKGNECLGDY
PEVLQDIWPV LRNTEANFLG FLLPVLIMSY CYFRIIQTLF SCKNHKKAKA IKLILLVVIV
FFLFWTPYNV MIFLETLKLY GFFPNCDMKR DLRLALSVTE TVAFSHCCLN PLIYAFAGQK
FRRYLRHLSR KCQAVLCGRP VHVSFSPSES QRSRQESIVS SNFTHYTSDG DASLLL
