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Fractalkine (C-X3-C motif chemokine 1) (CX3C membrane-anchored chemokine) (Neurotactin) (Small-inducible cytokine D1) [Cleaved into: Processed fractalkine]

 X3CL1_RAT               Reviewed;         393 AA.
O55145;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
14-AUG-2001, sequence version 3.
22-NOV-2017, entry version 121.
RecName: Full=Fractalkine;
AltName: Full=C-X3-C motif chemokine 1;
AltName: Full=CX3C membrane-anchored chemokine;
AltName: Full=Neurotactin;
AltName: Full=Small-inducible cytokine D1;
Contains:
RecName: Full=Processed fractalkine;
Flags: Precursor;
Name=Cx3cl1; Synonyms=Acc1, Fkn, Scyd1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=9724801; DOI=10.1073/pnas.95.18.10896;
Harrison J.K., Jiang Y., Chen S., Xia Y., Maciejewski D.,
McNamara R.K., Streit W.J., Salafranca M.N., Adhikari S.,
Thompson D.A., Botti P., Bacon K.B., Feng L.;
"Role for neuronally derived fractalkine in mediating interactions
between neurons and CX3CR1-expressing microglia.";
Proc. Natl. Acad. Sci. U.S.A. 95:10896-10901(1998).
[2]
SEQUENCE REVISION TO 127-151.
Feng L., Harrison J.K.;
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 204-335, AND TISSUE SPECIFICITY.
PubMed=9845323; DOI=10.1016/S0014-5793(98)01384-2;
Schwaeble W.J., Stover C.M., Schall T.J., Dairaghi D.J.,
Trinder P.K.E., Linington C., Iglesias A., Schubart A., Lynch N.J.,
Weihe E., Schaefer M.K.-H.;
"Neuronal expression of fractalkine in the presence and absence of
inflammation.";
FEBS Lett. 439:203-207(1998).
-!- FUNCTION: Acts as a ligand for both CX3CR1 and integrins. Binds to
CX3CR1 and to integrins ITGAV:ITGB3 and ITGA4:ITGB1. Can activate
integrins in both a CX3CR1-dependent and CX3CR1-independent
manner. In the presence of CX3CR1, activates integrins by binding
to the classical ligand-binding site (site 1) in integrins. 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. The soluble form is chemotactic for T-
cells and monocytes, but not for neutrophils. The membrane-bound
form promotes adhesion of those leukocytes to endothelial cells.
May play a role in regulating leukocyte adhesion and migration
processes at the endothelium. {ECO:0000250|UniProtKB:P78423}.
-!- SUBUNIT: Monomer. Forms a ternary complex with CX3CR1 and
ITGAV:ITGB3 or ITGA4:ITGB1. {ECO:0000250|UniProtKB:P78423}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P78423}; Single-pass type I membrane
protein {ECO:0000255}.
-!- SUBCELLULAR LOCATION: Processed fractalkine: Secreted
{ECO:0000250|UniProtKB:P78423}.
-!- TISSUE SPECIFICITY: Highest levels in brain (neurons). Significant
levels in kidney, heart, lung and adrenal gland.
{ECO:0000269|PubMed:9724801, ECO:0000269|PubMed:9845323}.
-!- PTM: A soluble short form may be released by proteolytic cleavage
from the long membrane-anchored form.
{ECO:0000250|UniProtKB:P78423}.
-!- SIMILARITY: Belongs to the intercrine delta family. {ECO:0000305}.
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EMBL; AF030358; AAC33834.2; -; mRNA.
EMBL; Y16813; CAA76404.1; -; mRNA.
RefSeq; NP_604450.1; NM_134455.1.
UniGene; Rn.107266; -.
ProteinModelPortal; O55145; -.
SMR; O55145; -.
BioGrid; 250131; 1.
STRING; 10116.ENSRNOP00000022128; -.
PaxDb; O55145; -.
PRIDE; O55145; -.
GeneID; 89808; -.
KEGG; rno:89808; -.
UCSC; RGD:620458; rat.
CTD; 6376; -.
RGD; 620458; Cx3cl1.
eggNOG; ENOG410IJQZ; Eukaryota.
eggNOG; ENOG41116BY; LUCA.
HOGENOM; HOG000036946; -.
HOVERGEN; HBG057269; -.
InParanoid; O55145; -.
KO; K05508; -.
PhylomeDB; O55145; -.
PRO; PR:O55145; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0042995; C:cell projection; IDA:RGD.
GO; GO:0009986; C:cell surface; ISO:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005576; C:extracellular region; ISO:RGD.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; ISO:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0098794; C:postsynapse; IEA:GOC.
GO; GO:0048020; F:CCR chemokine receptor binding; IBA:GO_Central.
GO; GO:0008009; F:chemokine activity; IDA:RGD.
GO; GO:0031737; F:CX3C chemokine receptor binding; ISS:UniProtKB.
GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0060055; P:angiogenesis involved in wound healing; ISO:RGD.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0071346; P:cellular response to interferon-gamma; IBA:GO_Central.
GO; GO:0071347; P:cellular response to interleukin-1; IBA:GO_Central.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IBA:GO_Central.
GO; GO:0070098; P:chemokine-mediated signaling pathway; IBA:GO_Central.
GO; GO:0006935; P:chemotaxis; IDA:RGD.
GO; GO:0019221; P:cytokine-mediated signaling pathway; ISO:RGD.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IBA:GO_Central.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0060080; P:inhibitory postsynaptic potential; IMP:RGD.
GO; GO:0033622; P:integrin activation; ISS:UniProtKB.
GO; GO:0050902; P:leukocyte adhesive activation; IEA:InterPro.
GO; GO:0002523; P:leukocyte migration involved in inflammatory response; ISS:UniProtKB.
GO; GO:0048247; P:lymphocyte chemotaxis; ISO:RGD.
GO; GO:0048246; P:macrophage chemotaxis; ISO:RGD.
GO; GO:0001774; P:microglial cell activation; IDA:RGD.
GO; GO:0002548; P:monocyte chemotaxis; IBA:GO_Central.
GO; GO:0030336; P:negative regulation of cell migration; ISO:RGD.
GO; GO:0050710; P:negative regulation of cytokine secretion; IMP:RGD.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:RGD.
GO; GO:0045906; P:negative regulation of vasoconstriction; IDA:RGD.
GO; GO:0030593; P:neutrophil chemotaxis; ISO:RGD.
GO; GO:0030168; P:platelet activation; IMP:RGD.
GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD.
GO; GO:0051041; P:positive regulation of calcium-independent cell-cell adhesion; ISO:RGD.
GO; GO:0045785; P:positive regulation of cell adhesion; IDA:RGD.
GO; GO:0030335; P:positive regulation of cell migration; IDA:RGD.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
GO; GO:0050729; P:positive regulation of inflammatory response; ISO:RGD.
GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IMP:RGD.
GO; GO:0002052; P:positive regulation of neuroblast proliferation; IDA:RGD.
GO; GO:0010976; P:positive regulation of neuron projection development; IDA:ParkinsonsUK-UCL.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IDA:RGD.
GO; GO:0032914; P:positive regulation of transforming growth factor beta1 production; ISO:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0042060; P:wound healing; ISO:RGD.
CDD; cd00274; Chemokine_CX3C; 1.
InterPro; IPR034127; Chemokine_CX3C.
InterPro; IPR001811; Chemokine_IL8-like_dom.
InterPro; IPR008097; CX3CL1.
InterPro; IPR036048; Interleukin_8-like_sf.
PANTHER; PTHR12015:SF92; PTHR12015:SF92; 1.
Pfam; PF00048; IL8; 1.
SMART; SM00199; SCY; 1.
SUPFAM; SSF54117; SSF54117; 1.
2: Evidence at transcript level;
Cell adhesion; Cell membrane; Chemotaxis; Complete proteome; Cytokine;
Disulfide bond; Glycoprotein; Membrane; Reference proteome; Secreted;
Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 393 Fractalkine.
/FTId=PRO_0000005254.
CHAIN 25 ?335 Processed fractalkine.
/FTId=PRO_0000296226.
TOPO_DOM 25 337 Extracellular. {ECO:0000255}.
TRANSMEM 338 358 Helical. {ECO:0000255}.
TOPO_DOM 359 393 Cytoplasmic. {ECO:0000255}.
REGION 25 100 Chemokine and involved in interaction
with ITGAV:ITGB3 and ITGA4:ITGB1.
{ECO:0000250|UniProtKB:P78423}.
REGION 101 337 Mucin-like stalk.
SITE 335 336 Cleavage; to produce soluble form.
{ECO:0000255}.
CARBOHYD 33 33 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 32 58 {ECO:0000250|UniProtKB:P78423}.
DISULFID 36 74 {ECO:0000250|UniProtKB:P78423}.
SEQUENCE 393 AA; 41977 MW; F06BB027CBD8CE14 CRC64;
MAPSQLAWLL RLAAFFHLCT LLAGQHLGMT KCNITCHKMT SPIPVTLLIH YQLNQESCGK
RAIILETRQH RHFCADPKEK WVQDAMKHLD HQTAALTRNG GKFEKRVDNV TPRITSATRG
LSPTALAKPE SATVEDLTLE PTAISQEARR PMGTSQEPPA AVTGSSPSTS KAQDAGLAAK
PQSTGISEVA AVSTTIWPSS AVYQSGSSLW AEEKATESPP TIALSTQAST TSSPKQNVGS
EGQPPWVQEQ DSTPEKSPGP EETNPVHTDI FQDRGPGSTV HPSVAPTSSE KTPSPELVAS
GSQAPKVEEP IHATADPQKL SVFITPVPDS QAATRRQAVG LLAFLGLLFC LGVAMFAYQS
LQGCPRKMAG EMVEGLRYVP RSCGSNSYVL VPV


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