X3CL1_MOUSE
ID X3CL1_MOUSE Reviewed; 395 AA.
AC O35188; O35933; Q91V44;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Fractalkine {ECO:0000303|PubMed:10382755};
DE Short=FK {ECO:0000303|PubMed:12569158};
DE AltName: Full=C-X3-C motif chemokine 1 {ECO:0000303|PubMed:9479488};
DE AltName: Full=CX3C membrane-anchored chemokine {ECO:0000303|PubMed:9479488};
DE AltName: Full=Neurotactin {ECO:0000303|PubMed:9177350};
DE AltName: Full=Small-inducible cytokine D1;
DE Contains:
DE RecName: Full=Processed fractalkine;
DE Flags: Precursor;
GN Name=Cx3cl1 {ECO:0000303|PubMed:9479488, ECO:0000312|MGI:MGI:1097153};
GN Synonyms=Cx3c {ECO:0000303|PubMed:9479488},
GN Fkn {ECO:0000303|PubMed:10382755}, Scyd1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND INDUCTION.
RX PubMed=9177350; DOI=10.1038/42491;
RA Pan Y., Lloyd C., Zhou H., Dolich S., Deeds J., Gonzalo J.-A., Vath J.,
RA Gosselin M., Ma J., Dussault B., Woolf E., Alperin G., Culpepper J.,
RA Gutierrez-Ramos J.-C., Gearing D.P.;
RT "Neurotactin, a membrane-anchored chemokine upregulated in brain
RT inflammation.";
RL Nature 387:611-617(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=9479488; DOI=10.1006/geno.1997.5058;
RA Rossi D.L., Hardiman G., Copeland N.G., Gilbert D.J., Jenkins N.,
RA Zlotnik A., Bazan J.F.;
RT "Cloning and characterization of a new type of mouse chemokine.";
RL Genomics 47:163-170(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PROTEOLYTIC CLEAVAGE, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=BALB/cJ;
RX PubMed=10382755;
RX DOI=10.1002/(sici)1521-4141(199906)29:06<1925::aid-immu1925>3.0.co;2-u;
RA Kanazawa N., Nakamura T., Tashiro K., Muramatsu M., Morita K., Yoneda K.,
RA Inaba K., Imamura S., Honjo T.;
RT "Fractalkine and macrophage-derived chemokine: T cell-attracting chemokines
RT expressed in T cell area dendritic cells.";
RL Eur. J. Immunol. 29:1925-1932(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Hypothalamus, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Eye, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=9845323; DOI=10.1016/s0014-5793(98)01384-2;
RA Schwaeble W.J., Stover C.M., Schall T.J., Dairaghi D.J., Trinder P.K.E.,
RA Linington C., Iglesias A., Schubart A., Lynch N.J., Weihe E.,
RA Schaefer M.K.-H.;
RT "Neuronal expression of fractalkine in the presence and absence of
RT inflammation.";
RL FEBS Lett. 439:203-207(1998).
RN [8]
RP FUNCTION.
RX PubMed=10187784; DOI=10.1074/jbc.274.15.10053;
RA Haskell C.A., Cleary M.D., Charo I.F.;
RT "Molecular uncoupling of fractalkine-mediated cell adhesion and signal
RT transduction. Rapid flow arrest of CX3CR1-expressing cells is independent
RT of G-protein activation.";
RL J. Biol. Chem. 274:10053-10058(1999).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=11287620; DOI=10.1128/mcb.21.9.3159-3165.2001;
RA Cook D.N., Chen S.C., Sullivan L.M., Manfra D.J., Wiekowski M.T.,
RA Prosser D.M., Vassileva G., Lira S.A.;
RT "Generation and analysis of mice lacking the chemokine fractalkine.";
RL Mol. Cell. Biol. 21:3159-3165(2001).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=12569158; DOI=10.1172/jci200315555;
RA Lesnik P., Haskell C.A., Charo I.F.;
RT "Decreased atherosclerosis in CX3CR1-/- mice reveals a role for fractalkine
RT in atherogenesis.";
RL J. Clin. Invest. 111:333-340(2003).
RN [11]
RP FUNCTION.
RX PubMed=18971423; DOI=10.1182/blood-2008-07-170787;
RA Landsman L., Bar-On L., Zernecke A., Kim K.W., Krauthgamer R.,
RA Shagdarsuren E., Lira S.A., Weissman I.L., Weber C., Jung S.;
RT "CX3CR1 is required for monocyte homeostasis and atherogenesis by promoting
RT cell survival.";
RL Blood 113:963-972(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Chemokine that acts as a ligand for both CX3CR1 and integrins
CC ITGAV:ITGB3 and ITGA4:ITGB1 (PubMed:10187784, PubMed:18971423). The
CC CX3CR1-CX3CL1 signaling exerts distinct functions in different tissue
CC compartments, such as immune response, inflammation, cell adhesion and
CC chemotaxis (PubMed:10382755, PubMed:9177350, PubMed:10187784,
CC PubMed:18971423). Regulates leukocyte adhesion and migration processes
CC at the endothelium (PubMed:10382755, PubMed:9177350). Can activate
CC integrins in both a CX3CR1-dependent and CX3CR1-independent manner (By
CC similarity). In the presence of CX3CR1, activates integrins by binding
CC to the classical ligand-binding site (site 1) in integrins (By
CC similarity). In the absence of CX3CR1, binds to a second site (site 2)
CC in integrins which is distinct from site 1 and enhances the binding of
CC other integrin ligands to site 1 (By similarity).
CC {ECO:0000250|UniProtKB:P78423, ECO:0000269|PubMed:10187784,
CC ECO:0000269|PubMed:10382755, ECO:0000269|PubMed:18971423,
CC ECO:0000269|PubMed:9177350}.
CC -!- FUNCTION: [Processed fractalkine]: The soluble form is chemotactic for
CC T-cells and monocytes, but not for neutrophils.
CC {ECO:0000250|UniProtKB:P78423}.
CC -!- FUNCTION: [Fractalkine]: The membrane-bound form promotes adhesion of
CC those leukocytes to endothelial cells. {ECO:0000250|UniProtKB:P78423}.
CC -!- SUBUNIT: Monomer (By similarity). Forms a ternary complex with CX3CR1
CC and ITGAV:ITGB3 or ITGA4:ITGB1 (By similarity).
CC {ECO:0000250|UniProtKB:P78423}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9177350};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Processed fractalkine]: Secreted
CC {ECO:0000269|PubMed:10382755}.
CC -!- TISSUE SPECIFICITY: Highest levels in brain (PubMed:9177350,
CC PubMed:9479488, PubMed:9845323). Lower levels in kidney, heart and lung
CC (PubMed:9177350, PubMed:9479488). Also found in skeletal muscle and
CC testis (PubMed:9177350, PubMed:9479488). Highly expressed in lesional
CC smooth muscle cells, but not macrophages (PubMed:12569158).
CC {ECO:0000269|PubMed:12569158, ECO:0000269|PubMed:9177350,
CC ECO:0000269|PubMed:9479488, ECO:0000269|PubMed:9845323}.
CC -!- INDUCTION: By 12-O-tetradecanoylphorbol-13-acetate (TPA) and
CC lipopolysaccharides (LPS) in bone marrow stroma cells.
CC {ECO:0000269|PubMed:9177350}.
CC -!- PTM: A soluble short 80 kDa form may be released by proteolytic
CC cleavage from the long membrane-anchored form.
CC {ECO:0000269|PubMed:10382755}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:11287620). Mice
CC develop normally and have normal migration of leukocytes to lymphoid
CC tissue and peripheral sites in several models of inflammation
CC (PubMed:11287620). {ECO:0000269|PubMed:11287620}.
CC -!- SIMILARITY: Belongs to the intercrine delta family. {ECO:0000305}.
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DR EMBL; AF010586; AAB66331.1; -; mRNA.
DR EMBL; U92565; AAB71763.1; -; mRNA.
DR EMBL; AF071549; AAD41620.1; -; mRNA.
DR EMBL; AK138214; BAE23585.1; -; mRNA.
DR EMBL; AK138472; BAE23673.1; -; mRNA.
DR EMBL; AK138574; BAE23702.1; -; mRNA.
DR EMBL; AK154646; BAE32737.1; -; mRNA.
DR EMBL; CH466525; EDL11144.1; -; Genomic_DNA.
DR EMBL; BC006650; AAH06650.1; -; mRNA.
DR EMBL; BC054838; AAH54838.1; -; mRNA.
DR CCDS; CCDS22548.1; -.
DR RefSeq; NP_033168.2; NM_009142.3.
DR AlphaFoldDB; O35188; -.
DR SMR; O35188; -.
DR STRING; 10090.ENSMUSP00000034230; -.
DR iPTMnet; O35188; -.
DR PhosphoSitePlus; O35188; -.
DR CPTAC; non-CPTAC-3612; -.
DR jPOST; O35188; -.
DR MaxQB; O35188; -.
DR PaxDb; O35188; -.
DR PeptideAtlas; O35188; -.
DR PRIDE; O35188; -.
DR ProteomicsDB; 299795; -.
DR Antibodypedia; 15022; 771 antibodies from 43 providers.
DR DNASU; 20312; -.
DR Ensembl; ENSMUST00000034230; ENSMUSP00000034230; ENSMUSG00000031778.
DR GeneID; 20312; -.
DR KEGG; mmu:20312; -.
DR UCSC; uc009mwx.1; mouse.
DR CTD; 6376; -.
DR MGI; MGI:1097153; Cx3cl1.
DR VEuPathDB; HostDB:ENSMUSG00000031778; -.
DR eggNOG; ENOG502SNIE; Eukaryota.
DR GeneTree; ENSGT01050000244920; -.
DR HOGENOM; CLU_738793_0_0_1; -.
DR InParanoid; O35188; -.
DR OMA; QNQESCG; -.
DR OrthoDB; 1060256at2759; -.
DR TreeFam; TF337534; -.
DR Reactome; R-MMU-380108; Chemokine receptors bind chemokines.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 20312; 2 hits in 74 CRISPR screens.
DR PRO; PR:O35188; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; O35188; protein.
DR Bgee; ENSMUSG00000031778; Expressed in perirhinal cortex and 208 other tissues.
DR ExpressionAtlas; O35188; baseline and differential.
DR Genevisible; O35188; MM.
DR GO; GO:0044297; C:cell body; IDA:ARUK-UCL.
DR GO; GO:0042995; C:cell projection; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:ARUK-UCL.
DR GO; GO:0043025; C:neuronal cell body; IDA:ARUK-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0048020; F:CCR chemokine receptor binding; IBA:GO_Central.
DR GO; GO:0042056; F:chemoattractant activity; ISO:MGI.
DR GO; GO:0008009; F:chemokine activity; ISO:MGI.
DR GO; GO:0031737; F:CX3C chemokine receptor binding; IDA:UniProtKB.
DR GO; GO:0045237; F:CXCR1 chemokine receptor binding; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR GO; GO:0060055; P:angiogenesis involved in wound healing; IMP:MGI.
DR GO; GO:0035425; P:autocrine signaling; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR GO; GO:0060326; P:cell chemotaxis; ISO:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:MGI.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IBA:GO_Central.
DR GO; GO:0071347; P:cellular response to interleukin-1; IBA:GO_Central.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IBA:GO_Central.
DR GO; GO:0070098; P:chemokine-mediated signaling pathway; ISO:MGI.
DR GO; GO:0006935; P:chemotaxis; ISS:UniProtKB.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IMP:MGI.
DR GO; GO:0048245; P:eosinophil chemotaxis; IBA:GO_Central.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IDA:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0060080; P:inhibitory postsynaptic potential; ISO:MGI.
DR GO; GO:0033622; P:integrin activation; ISS:UniProtKB.
DR GO; GO:0050902; P:leukocyte adhesive activation; IEA:InterPro.
DR GO; GO:0002523; P:leukocyte migration involved in inflammatory response; ISS:UniProtKB.
DR GO; GO:0048247; P:lymphocyte chemotaxis; IDA:MGI.
DR GO; GO:0001774; P:microglial cell activation; ISO:MGI.
DR GO; GO:0061518; P:microglial cell proliferation; ISO:MGI.
DR GO; GO:0002548; P:monocyte chemotaxis; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IDA:MGI.
DR GO; GO:1900450; P:negative regulation of glutamate receptor signaling pathway; ISO:MGI.
DR GO; GO:0110091; P:negative regulation of hippocampal neuron apoptotic process; ISO:MGI.
DR GO; GO:0032690; P:negative regulation of interleukin-1 alpha production; ISO:MGI.
DR GO; GO:1903979; P:negative regulation of microglial cell activation; ISO:MGI.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:MGI.
DR GO; GO:0045906; P:negative regulation of vasoconstriction; ISO:MGI.
DR GO; GO:0070050; P:neuron cellular homeostasis; ISO:MGI.
DR GO; GO:0030593; P:neutrophil chemotaxis; IDA:MGI.
DR GO; GO:0030168; P:platelet activation; ISO:MGI.
DR GO; GO:0050918; P:positive chemotaxis; ISO:MGI.
DR GO; GO:0032233; P:positive regulation of actin filament bundle assembly; ISO:MGI.
DR GO; GO:0051041; P:positive regulation of calcium-independent cell-cell adhesion; ISO:MGI.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
DR GO; GO:1903721; P:positive regulation of I-kappaB phosphorylation; ISO:MGI.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0010759; P:positive regulation of macrophage chemotaxis; ISO:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
DR GO; GO:1904141; P:positive regulation of microglial cell migration; ISO:MGI.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; ISO:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISO:MGI.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0032914; P:positive regulation of transforming growth factor beta1 production; IMP:MGI.
DR GO; GO:0031664; P:regulation of lipopolysaccharide-mediated signaling pathway; ISO:MGI.
DR GO; GO:0002931; P:response to ischemia; ISO:MGI.
DR GO; GO:0042060; P:wound healing; IMP:MGI.
DR CDD; cd00274; Chemokine_CX3C; 1.
DR InterPro; IPR039809; Chemokine_b/g/d.
DR InterPro; IPR034127; Chemokine_CX3C.
DR InterPro; IPR001811; Chemokine_IL8-like_dom.
DR InterPro; IPR008097; CX3CL1.
DR InterPro; IPR036048; Interleukin_8-like_sf.
DR PANTHER; PTHR12015; PTHR12015; 1.
DR PANTHER; PTHR12015:SF92; PTHR12015:SF92; 1.
DR Pfam; PF00048; IL8; 1.
DR SMART; SM00199; SCY; 1.
DR SUPFAM; SSF54117; SSF54117; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Chemotaxis; Cytokine; Disulfide bond;
KW Inflammatory response; Membrane; Reference proteome; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..395
FT /note="Fractalkine"
FT /id="PRO_0000005253"
FT CHAIN 25..?337
FT /note="Processed fractalkine"
FT /id="PRO_0000296225"
FT TOPO_DOM 25..336
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 358..395
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 25..100
FT /note="Chemokine and involved in interaction with
FT ITGAV:ITGB3 and ITGA4:ITGB1"
FT /evidence="ECO:0000250|UniProtKB:P78423"
FT REGION 101..336
FT /note="Mucin-like stalk"
FT REGION 148..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 337..338
FT /note="Cleavage; to produce soluble form"
FT /evidence="ECO:0000255"
FT DISULFID 32..58
FT /evidence="ECO:0000250|UniProtKB:P78423"
FT DISULFID 36..74
FT /evidence="ECO:0000250|UniProtKB:P78423"
FT CONFLICT 37
FT /note="D -> G (in Ref. 2; AAB71763)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 395 AA; 42099 MW; B5A16F8BD4B80340 CRC64;
MAPSPLAWLL RLAAFFHLCT LLPGQHLGMT KCEIMCDKMT SRIPVALLIR YQLNQESCGK
RAIVLETTQH RRFCADPKEK WVQDAMKHLD HQAAALTKNG GKFEKRVDNV TPGITLATRG
LSPSALTKPE SATLEDLALE LTTISQEARG TMGTSQEPPA AVTGSSLSTS EAQDAGLTAK
PQSIGSFEAA DISTTVWPSP AVYQSGSSSW AEEKATESPS TTAPSPQVST TSPSTPEENV
GSEGQPPWVQ GQDLSPEKSL GSEEINPVHT DNFQERGPGN TVHPSVAPIS SEETPSPELV
ASGSQAPKIE EPIHATADPQ KLSVLITPVP DTQAATRRQA VGLLAFLGLL FCLGVAMFAY
QSLQGCPRKM AGEMVEGLRY VPRSCGSNSY VLVPV
