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CX3C chemokine receptor 1 (C-X3-C CKR-1) (CX3CR1) (Beta chemokine receptor-like 1) (CMK-BRL-1) (CMK-BRL1) (Fractalkine receptor) (G-protein coupled receptor 13) (V28)

 CX3C1_HUMAN             Reviewed;         355 AA.
P49238; A0N0N6; B2R5Z4; J3KP17;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
12-SEP-2018, entry version 173.
RecName: Full=CX3C chemokine receptor 1;
Short=C-X3-C CKR-1;
Short=CX3CR1;
AltName: Full=Beta chemokine receptor-like 1;
AltName: Full=CMK-BRL-1;
Short=CMK-BRL1;
AltName: Full=Fractalkine receptor;
AltName: Full=G-protein coupled receptor 13;
AltName: Full=V28;
Name=CX3CR1; Synonyms=CMKBRL1, GPR13;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=7590284; DOI=10.1016/0378-1119(95)00336-5;
Raport C.J., Schweickart V.L., Eddy R.L. Jr., Shows T.B., Gray P.W.;
"The orphan G-protein-coupled receptor-encoding gene V28 is closely
related to genes for chemokine receptors and is expressed in lymphoid
and neural tissues.";
Gene 163:295-299(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=7646814; DOI=10.1089/dna.1995.14.673;
Combadiere C., Ahuja S.K., Murphy P.M.;
"Cloning, chromosomal localization, and RNA expression of a human beta
chemokine receptor-like gene.";
DNA Cell Biol. 14:673-680(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=12551893; DOI=10.1074/jbc.M211422200;
DeVries M.E., Cao H., Wang J., Xu L., Kelvin A.A., Ran L., Chau L.A.,
Madrenas J., Hegele R.A., Kelvin D.J.;
"Genomic organization and evolution of the CX3CR1/CCR8 chemokine
receptor locus.";
J. Biol. Chem. 278:11985-11994(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 8-185 (ISOFORM 4), AND VARIANTS ILE-249
AND MET-280.
TISSUE=Amygdala, and Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B.,
Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O.,
Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I.,
Nickerson D.A.;
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASP-13; ILE-249 AND
MET-280.
NIEHS SNPs program;
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Blood;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
INTERACTION WITH HRSV PROTEIN G (MICROBIAL INFECTION).
PubMed=11477410; DOI=10.1038/90675;
Tripp R.A., Jones L.P., Haynes L.M., Zheng H., Murphy P.M.,
Anderson L.J.;
"CX3C chemokine mimicry by respiratory syncytial virus G
glycoprotein.";
Nat. Immunol. 2:732-738(2001).
[11]
ALTERNATIVE SPLICING, CHARACTERIZATION (ISOFORMS 2 AND 3), AND
FUNCTION (ISOFORMS 2 AND 3).
PubMed=14607932; DOI=10.4049/jimmunol.171.10.5305;
Garin A., Tarantino N., Faure S., Daoudi M., Lecureuil C.,
Bourdais A., Debre P., Deterre P., Combadiere C.;
"Two novel fully functional isoforms of CX3CR1 are potent HIV
coreceptors.";
J. Immunol. 171:5305-5312(2003).
[12]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=9390561; DOI=10.1016/S0092-8674(00)80438-9;
Imai T., Hieshima K., Haskell C., Baba M., Nagira M., Nishimura M.,
Kakizaki M., Takagi S., Nomiyama H., Schall T.J., Yoshie O.;
"Identification and molecular characterization of fractalkine receptor
CX3CR1, which mediates both leukocyte migration and adhesion.";
Cell 91:521-530(1997).
[13]
FUNCTION, AND INTERACTION WITH HIV-1 PROTEIN GP160 (MICROBIAL
INFECTION).
PubMed=9726990; DOI=10.1074/jbc.273.37.23799;
Combadiere C., Salzwedel K., Smith E.D., Tiffany H.L., Berger E.A.,
Murphy P.M.;
"Identification of CX3CR1. A chemotactic receptor for the human CX3C
chemokine fractalkine and a fusion coreceptor for HIV-1.";
J. Biol. Chem. 273:23799-23804(1998).
[14]
FUNCTION, BINDING TO CX3CL1, AND IDENTIFICATION IN A COMPLEX WITH
INTEGRINS AND CX3CL1.
PubMed=23125415; DOI=10.4049/jimmunol.1200889;
Fujita M., Takada Y.K., Takada Y.;
"Integrins alphavbeta3 and alpha4beta1 act as coreceptors for
fractalkine, and the integrin-binding defective mutant of fractalkine
is an antagonist of CX3CR1.";
J. Immunol. 189:5809-5819(2012).
[15]
VARIANTS ALA-57; ILE-122; ILE-249 AND MET-280.
PubMed=10731151; DOI=10.1126/science.287.5461.2274;
Faure S., Meyer L., Costagliola D., Vaneensberghe C., Genin E.,
Autran B., Delfraissy J.-F., McDermott D.H., Murphy P.M., Debre P.,
Theodorou I., Combadiere C.;
"Rapid progression to AIDS in HIV+ individuals with a structural
variant of the chemokine receptor CX3CR1.";
Science 287:2274-2277(2000).
[16]
VARIANT ILE-249.
PubMed=11264153; DOI=10.1182/blood.V97.7.1925;
Moatti D., Faure S., Fumeron F., Amara M.E.-W., Seknadji P.,
McDermott D.H., Debre P., Aumont M.C., Murphy P.M., de Prost D.,
Combadiere C.;
"Polymorphism in the fractalkine receptor CX3CR1 as a genetic risk
factor for coronary artery disease.";
Blood 97:1925-1928(2001).
[17]
VARIANTS ILE-249 AND MET-280, AND ASSOCIATION WITH ARMD12.
PubMed=15208270; DOI=10.1096/fj.04-1862fje;
Tuo J., Smith B.C., Bojanowski C.M., Meleth A.D., Gery I., Csaky K.G.,
Chew E.Y., Chan C.C.;
"The involvement of sequence variation and expression of CX3CR1 in the
pathogenesis of age-related macular degeneration.";
FASEB J. 18:1297-1299(2004).
[18]
CHARACTERIZATION OF VARIANTS ILE-249 AND MET-280, AND EFFECT ON
CHEMOTAXIS OF MONOCYTES OF ARMD12 PATIENTS.
PubMed=17909628; DOI=10.1172/JCI31692;
Combadiere C., Feumi C., Raoul W., Keller N., Rodero M., Pezard A.,
Lavalette S., Houssier M., Jonet L., Picard E., Debre P., Sirinyan M.,
Deterre P., Ferroukhi T., Cohen S.Y., Chauvaud D., Jeanny J.C.,
Chemtob S., Behar-Cohen F., Sennlaub F.;
"CX3CR1-dependent subretinal microglia cell accumulation is associated
with cardinal features of age-related macular degeneration.";
J. Clin. Invest. 117:2920-2928(2007).
-!- FUNCTION: Receptor for the CX3C chemokine fractalkine (CX3CL1);
binds to CX3CL1 and mediates both its adhesive and migratory
functions (PubMed:9390561, PubMed:23125415). Acts as coreceptor
with CD4 for HIV-1 virus envelope protein (in vitro)
(PubMed:9726990). Isoform 2 and isoform 3 seem to be more potent
HIV-1 coreceptors than isoform 1 (PubMed:14607932).
{ECO:0000269|PubMed:14607932, ECO:0000269|PubMed:23125415,
ECO:0000269|PubMed:9390561, ECO:0000269|PubMed:9726990}.
-!- SUBUNIT: Found in a ternary complex with CX3CL1 and ITGAV:ITGB3 or
ITGA4:ITGB1. {ECO:0000269|PubMed:23125415}.
-!- SUBUNIT: (Microbial infection) Interacts with human respiratory
syncytial virus (HRSV) protein G; this interaction modulates host
immune response. {ECO:0000269|PubMed:11477410}.
-!- SUBUNIT: (Microbial infection) Interacts with HIV-1 envelope
polyprotein gp160. {ECO:0000269|PubMed:9726990}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9390561};
Multi-pass membrane protein {ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=P49238-1; Sequence=Displayed;
Name=2;
IsoId=P49238-2; Sequence=VSP_009681;
Name=3;
IsoId=P49238-3; Sequence=VSP_009682;
Name=4;
IsoId=P49238-4; Sequence=VSP_044595;
Note=Ref.4 (DA413545) sequence is in conflict in position:
8:F->L. No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed in lymphoid and neural tissues.
-!- PTM: This protein is not N-glycosylated which is unusual for G-
protein-coupled receptors. {ECO:0000250|UniProtKB:P35411}.
-!- POLYMORPHISM: Variations in CX3CR1 are associated with rapid
progression to AIDS [MIM:609423]. Increased susceptibility to HIV
infection and rapid progression to AIDS are associated with the
Ile-249/Met-280 haplotype. {ECO:0000269|PubMed:10731151}.
-!- DISEASE: Macular degeneration, age-related, 12 (ARMD12)
[MIM:613784]: 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. {ECO:0000269|PubMed:15208270}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/cx3cr1/";
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EMBL; U20350; AAA91783.1; -; mRNA.
EMBL; U28934; AAA87032.1; -; mRNA.
EMBL; AY016370; AAK08627.1; -; Genomic_DNA.
EMBL; AK312373; BAG35291.1; -; mRNA.
EMBL; DA413545; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; EF064744; ABK41927.1; -; Genomic_DNA.
EMBL; EU006531; ABS29268.1; -; Genomic_DNA.
EMBL; AC092053; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471055; EAW64576.1; -; Genomic_DNA.
EMBL; BC028078; AAH28078.1; -; mRNA.
CCDS; CCDS43069.1; -. [P49238-1]
CCDS; CCDS54571.1; -. [P49238-4]
PIR; JC4304; JC4304.
RefSeq; NP_001164642.1; NM_001171171.1. [P49238-1]
RefSeq; NP_001164643.1; NM_001171172.1. [P49238-1]
RefSeq; NP_001164645.1; NM_001171174.1. [P49238-4]
RefSeq; NP_001328.1; NM_001337.3. [P49238-1]
UniGene; Hs.78913; -.
ProteinModelPortal; P49238; -.
BioGrid; 107904; 1.
DIP; DIP-5879N; -.
IntAct; P49238; 4.
STRING; 9606.ENSP00000351059; -.
BindingDB; P49238; -.
ChEMBL; CHEMBL4843; -.
GuidetoPHARMACOLOGY; 74; -.
iPTMnet; P49238; -.
PhosphoSitePlus; P49238; -.
BioMuta; CX3CR1; -.
DMDM; 1351394; -.
PaxDb; P49238; -.
PeptideAtlas; P49238; -.
PRIDE; P49238; -.
ProteomicsDB; 55973; -.
ProteomicsDB; 55974; -. [P49238-2]
ProteomicsDB; 55975; -. [P49238-3]
DNASU; 1524; -.
Ensembl; ENST00000358309; ENSP00000351059; ENSG00000168329. [P49238-4]
Ensembl; ENST00000399220; ENSP00000382166; ENSG00000168329. [P49238-1]
Ensembl; ENST00000541347; ENSP00000439140; ENSG00000168329. [P49238-1]
Ensembl; ENST00000542107; ENSP00000444928; ENSG00000168329. [P49238-1]
GeneID; 1524; -.
KEGG; hsa:1524; -.
UCSC; uc003cjl.4; human. [P49238-1]
CTD; 1524; -.
DisGeNET; 1524; -.
EuPathDB; HostDB:ENSG00000168329.13; -.
GeneCards; CX3CR1; -.
HGNC; HGNC:2558; CX3CR1.
HPA; CAB032478; -.
HPA; HPA030311; -.
HPA; HPA046587; -.
HPA; HPA077743; -.
MalaCards; CX3CR1; -.
MIM; 601470; gene.
MIM; 609423; phenotype.
MIM; 613784; phenotype.
neXtProt; NX_P49238; -.
OpenTargets; ENSG00000168329; -.
Orphanet; 279; Age-related macular degeneration.
PharmGKB; PA27054; -.
eggNOG; ENOG410IGZ8; Eukaryota.
eggNOG; ENOG41118PP; LUCA.
GeneTree; ENSGT00760000118785; -.
HOGENOM; HOG000234122; -.
HOVERGEN; HBG106917; -.
InParanoid; P49238; -.
KO; K04192; -.
OMA; PQFMFTK; -.
OrthoDB; EOG091G0D5U; -.
PhylomeDB; P49238; -.
TreeFam; TF330966; -.
Reactome; R-HSA-380108; Chemokine receptors bind chemokines.
Reactome; R-HSA-418594; G alpha (i) signalling events.
SIGNOR; P49238; -.
GeneWiki; CX3CR1; -.
GenomeRNAi; 1524; -.
PRO; PR:P49238; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000168329; Expressed in 208 organ(s), highest expression level in mononuclear cell.
CleanEx; HS_CX3CR1; -.
ExpressionAtlas; P49238; baseline and differential.
Genevisible; P49238; HS.
GO; GO:0009986; C:cell surface; ISS:ARUK-UCL.
GO; GO:0097447; C:dendritic tree; ISS:ARUK-UCL.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005622; C:intracellular; ISS:ARUK-UCL.
GO; GO:0043005; C:neuron projection; ISS:ARUK-UCL.
GO; GO:0032809; C:neuronal cell body membrane; ISS:ARUK-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0019960; F:C-X3-C chemokine binding; IDA:UniProtKB.
GO; GO:0016495; F:C-X3-C chemokine receptor activity; IEA:Ensembl.
GO; GO:0004950; F:chemokine receptor activity; TAS:ProtInc.
GO; GO:0008528; F:G-protein coupled peptide receptor activity; TAS:ARUK-UCL.
GO; GO:0004930; F:G-protein coupled receptor activity; ISS:ARUK-UCL.
GO; GO:0035425; P:autocrine signaling; ISS:ARUK-UCL.
GO; GO:0007155; P:cell adhesion; ISS:ARUK-UCL.
GO; GO:0007267; P:cell-cell signaling; TAS:ARUK-UCL.
GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:ARUK-UCL.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
GO; GO:0021795; P:cerebral cortex cell migration; IEA:Ensembl.
GO; GO:0006935; P:chemotaxis; IGI:ARUK-UCL.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0045087; P:innate immune response; IC:ARUK-UCL.
GO; GO:0050901; P:leukocyte tethering or rolling; ISS:ARUK-UCL.
GO; GO:0048246; P:macrophage chemotaxis; IEA:Ensembl.
GO; GO:0007613; P:memory; IEA:Ensembl.
GO; GO:0002282; P:microglial cell activation involved in immune response; IEA:Ensembl.
GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; ISS:ARUK-UCL.
GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
GO; GO:0110091; P:negative regulation of hippocampal neuron apoptotic process; ISS:ARUK-UCL.
GO; GO:0032691; P:negative regulation of interleukin-1 beta production; ISS:ARUK-UCL.
GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; IEA:Ensembl.
GO; GO:0007200; P:phospholipase C-activating G-protein coupled receptor signaling pathway; ISS:ARUK-UCL.
GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
GO; GO:1903721; P:positive regulation of I-kappaB phosphorylation; ISS:ARUK-UCL.
GO; GO:0002052; P:positive regulation of neuroblast proliferation; ISS:ARUK-UCL.
GO; GO:0050769; P:positive regulation of neurogenesis; ISS:ARUK-UCL.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:ARUK-UCL.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:ARUK-UCL.
GO; GO:1904139; P:regulation of microglial cell migration; TAS:ARUK-UCL.
GO; GO:0050767; P:regulation of neurogenesis; TAS:ARUK-UCL.
GO; GO:0045428; P:regulation of nitric oxide biosynthetic process; ISS:ARUK-UCL.
GO; GO:0048167; P:regulation of synaptic plasticity; TAS:ARUK-UCL.
GO; GO:0042534; P:regulation of tumor necrosis factor biosynthetic process; ISS:ARUK-UCL.
GO; GO:0002931; P:response to ischemia; ISS:ARUK-UCL.
GO; GO:0009611; P:response to wounding; TAS:ProtInc.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd15186; 7tmA_CX3CR1; 1.
InterPro; IPR005387; Chemokine_CX3CR1.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR01562; FRACTALKINER.
PRINTS; PR00237; GPCRRHODOPSN.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
Age-related macular degeneration; Alternative splicing; Cell membrane;
Complete proteome; Disulfide bond; G-protein coupled receptor;
Host-virus interaction; Membrane; Phosphoprotein; Polymorphism;
Receptor; Reference proteome; Transducer; Transmembrane;
Transmembrane helix.
CHAIN 1 355 CX3C chemokine receptor 1.
/FTId=PRO_0000069326.
TOPO_DOM 1 31 Extracellular. {ECO:0000255}.
TRANSMEM 32 59 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 60 69 Cytoplasmic. {ECO:0000255}.
TRANSMEM 70 90 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 91 103 Extracellular. {ECO:0000255}.
TRANSMEM 104 125 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 126 142 Cytoplasmic. {ECO:0000255}.
TRANSMEM 143 167 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 168 195 Extracellular. {ECO:0000255}.
TRANSMEM 196 215 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 216 231 Cytoplasmic. {ECO:0000255}.
TRANSMEM 232 256 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 257 273 Extracellular. {ECO:0000255}.
TRANSMEM 274 297 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 298 355 Cytoplasmic. {ECO:0000255}.
MOD_RES 346 346 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9Z0D9}.
DISULFID 102 175 {ECO:0000255|PROSITE-ProRule:PRU00521}.
VAR_SEQ 1 1 M -> MREPLEALKLADLDFRKSSLASGWRMASGAFTM
(in isoform 2). {ECO:0000305}.
/FTId=VSP_009681.
VAR_SEQ 1 1 M -> MASGAFTM (in isoform 3).
{ECO:0000305}.
/FTId=VSP_009682.
VAR_SEQ 1 1 M -> MREPLEAFKLADLDFRKSSLASGWRMASGAFTM
(in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044595.
VARIANT 13 13 E -> D (in dbSNP:rs41535248).
{ECO:0000269|Ref.6}.
/FTId=VAR_049386.
VARIANT 57 57 T -> A (in dbSNP:rs199811198).
{ECO:0000269|PubMed:10731151}.
/FTId=VAR_010041.
VARIANT 122 122 V -> I (in dbSNP:rs143001773).
{ECO:0000269|PubMed:10731151}.
/FTId=VAR_010042.
VARIANT 147 147 V -> I (in dbSNP:rs3732380).
/FTId=VAR_022062.
VARIANT 249 249 V -> I (common polymorphism in Caucasian
population; associated with a markedly
reduced risk of acute coronary artery
disease; associated with higher risk of
developing ARMD12; chemotaxis of
monocytes of individuals with homozygous
Ile-249 and Met-280 genotypes is impaired
in the presence of bound CX3CR1 protein;
dbSNP:rs3732379).
{ECO:0000269|PubMed:10731151,
ECO:0000269|PubMed:11264153,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15208270,
ECO:0000269|PubMed:17909628,
ECO:0000269|Ref.6}.
/FTId=VAR_010043.
VARIANT 280 280 T -> M (common polymorphism in Caucasian
population; associated with higher risk
of developing ARMD12; chemotaxis of
monocytes of individuals with homozygous
Met-280 and Ile-249 genotypes is impaired
in the presence of bound CX3CR1 protein;
dbSNP:rs3732378).
{ECO:0000269|PubMed:10731151,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15208270,
ECO:0000269|PubMed:17909628,
ECO:0000269|Ref.6}.
/FTId=VAR_010044.
SEQUENCE 355 AA; 40396 MW; C59DC5F4C4312F22 CRC64;
MDQFPESVTE NFEYDDLAEA CYIGDIVVFG TVFLSIFYSV IFAIGLVGNL LVVFALTNSK
KPKSVTDIYL LNLALSDLLF VATLPFWTHY LINEKGLHNA MCKFTTAFFF IGFFGSIFFI
TVISIDRYLA IVLAANSMNN RTVQHGVTIS LGVWAAAILV AAPQFMFTKQ KENECLGDYP
EVLQEIWPVL RNVETNFLGF LLPLLIMSYC YFRIIQTLFS CKNHKKAKAI KLILLVVIVF
FLFWTPYNVM IFLETLKLYD FFPSCDMRKD LRLALSVTET VAFSHCCLNP LIYAFAGEKF
RRYLYHLYGK CLAVLCGRSV HVDFSSSESQ RSRHGSVLSS NFTYHTSDGD ALLLL


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