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C-X-C chemokine receptor type 4 (CXC-R4) (CXCR-4) (Fusin) (Leukocyte-derived seven transmembrane domain receptor) (LESTR) (Pre-B-cell-derived chemokine receptor) (PB-CKR) (Stromal cell-derived factor 1 receptor) (SDF-1 receptor) (CD antigen CD184)

 CXCR4_MOUSE             Reviewed;         359 AA.
P70658; O09059; O09062; P70233; P70346; Q4KMW1;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
10-OCT-2018, entry version 168.
RecName: Full=C-X-C chemokine receptor type 4;
Short=CXC-R4;
Short=CXCR-4;
AltName: Full=Fusin {ECO:0000303|PubMed:8955194};
AltName: Full=Leukocyte-derived seven transmembrane domain receptor;
Short=LESTR {ECO:0000303|PubMed:9295051};
AltName: Full=Pre-B-cell-derived chemokine receptor;
Short=PB-CKR;
AltName: Full=Stromal cell-derived factor 1 receptor;
Short=SDF-1 receptor;
AltName: CD_antigen=CD184;
Name=Cxcr4; Synonyms=Cmkar4, Lestr, Sdf1r;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM CXCR4-B).
STRAIN=129/Sv, and C57BL/6J; TISSUE=Peritoneal exudate;
PubMed=8955194;
Heesen M., Berman M.A., Benson J.D., Gerard C., Dorf M.E.;
"Cloning of the mouse fusin gene, homologue to a human HIV-1 co-
factor.";
J. Immunol. 157:5455-5460(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CXCR4-B), FUNCTION, AND
SUBCELLULAR LOCATION.
TISSUE=Pre-B cell;
PubMed=8962122; DOI=10.1073/pnas.93.25.14726;
Nagasawa T., Nakajima T., Tachibana K., Iizasa H., Bleul C.C.,
Yoshie O., Matsushima K., Yoshida N., Springer T.A., Kishimoto T.;
"Molecular cloning and characterization of a murine pre-B-cell growth-
stimulating factor/stromal cell-derived factor 1 receptor, a murine
homolog of the human immunodeficiency virus 1 entry coreceptor
fusin.";
Proc. Natl. Acad. Sci. U.S.A. 93:14726-14729(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CXCR4-B).
STRAIN=129/Sv; TISSUE=Thymus;
Schubel A., Burgstahler R., Lipp M.;
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS CXCR4-A AND
CXCR4-B), AND FUNCTION.
STRAIN=C57BL/6J X CBA/J; TISSUE=Thymus;
PubMed=9295051; DOI=10.1002/eji.1830270839;
Moepps B., Frodl R., Rodewald H.-R., Baggiolini M., Gierschik P.;
"Two murine homologues of the human chemokine receptor CXCR4 mediating
stromal cell-derived factor 1alpha activation of Gi2 are
differentially expressed in vivo.";
Eur. J. Immunol. 27:2102-2112(1997).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS CXCR4-A AND CXCR4-B), AND
FUNCTION.
PubMed=9103415;
Heesen M., Berman M.A., Hoepken U.E., Gerard N.P., Dorf M.E.;
"Alternate splicing of mouse fusin/CXC chemokine receptor-4: stromal
cell-derived factor-1alpha is a ligand for both CXC chemokine
receptor-4 isoforms.";
J. Immunol. 158:3561-3564(1997).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CXCR4-B).
STRAIN=C57BL/6J; TISSUE=Thymus;
Suzuki G., Nakata Y., Uzawa A., Shirasawa T., Saito T., Mita K.;
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CXCR4-B).
STRAIN=FVB/N; TISSUE=Mammary gland;
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).
[8]
ALTERNATIVE SPLICING.
PubMed=9879064; DOI=10.3109/10799899809047750;
Frodl R., Gierschik P., Moepps B.;
"Genomic organization and expression of the CXCR4 gene in mouse and
man: absence of a splice variant corresponding to mouse CXCR4-B in
human tissues.";
J. Recept. Signal Transduct. 18:321-344(1998).
[9]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=9634237; DOI=10.1038/31261;
Tachibana K., Hirota S., Iizasa H., Yoshida H., Kawabata K.,
Kataoka Y., Kitamura Y., Matsushima K., Yoshida N., Nishikawa S.,
Kishimoto T., Nagasawa T.;
"The chemokine receptor CXCR4 is essential for vascularization of the
gastrointestinal tract.";
Nature 393:591-594(1998).
[10]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=9634238; DOI=10.1038/31269;
Zou Y.-R., Kottmann A.H., Kuroda M., Taniuchi I., Littman D.R.;
"Function of the chemokine receptor CXCR4 in haematopoiesis and in
cerebellar development.";
Nature 393:595-599(1998).
[11]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=9689100; DOI=10.1073/pnas.95.16.9448;
Ma Q., Jones D., Borghesani P.R., Segal R.A., Nagasawa T.,
Kishimoto T., Bronson R.T., Springer T.A.;
"Impaired B-lymphopoiesis, myelopoiesis, and derailed cerebellar
neuron migration in CXCR4- and SDF-1-deficient mice.";
Proc. Natl. Acad. Sci. U.S.A. 95:9448-9453(1998).
[12]
DEVELOPMENTAL STAGE.
STRAIN=ICR;
PubMed=10479460; DOI=10.1006/dbio.1999.9405;
McGrath K.E., Koniski A.D., Maltby K.M., McGann J.K., Palis J.;
"Embryonic expression and function of the chemokine SDF-1 and its
receptor, CXCR4.";
Dev. Biol. 213:442-456(1999).
[13]
INTERACTION WITH CD164.
PubMed=18227060; DOI=10.1074/jbc.M706730200;
Bae G.-U., Gaio U., Yang Y.-J., Lee H.-J., Kang J.-S., Krauss R.S.;
"Regulation of myoblast motility and fusion by the CXCR4-associated
sialomucin, CD164.";
J. Biol. Chem. 283:8301-8309(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Receptor for the C-X-C chemokine CXCL12/SDF-1 that
transduces a signal by increasing intracellular calcium ion levels
and enhancing MAPK1/MAPK3 activation (PubMed:8962122,
PubMed:9295051, PubMed:9103415). Plays a role in regulation of
cell migration, e.g. during wound healing. Acts as a receptor for
extracellular ubiquitin; leading to enhanced intracellular calcium
ions and reduced cellular cAMP levels. Binds bacterial
lipopolysaccharide (LPS) et mediates LPS-induced inflammatory
response, including TNF secretion by monocytes (By similarity).
Involved in hematopoiesis and in cardiac ventricular septum
formation (PubMed:9634237, PubMed:9634238, PubMed:9689100). Also
plays an essential role in vascularization of the gastrointestinal
tract, probably by regulating vascular branching and/or remodeling
processes in endothelial cells (PubMed:9634237). Involved in
cerebellar development. In the CNS, could mediate hippocampal-
neuron survival (PubMed:9634238, PubMed:9689100).
{ECO:0000250|UniProtKB:P61073, ECO:0000269|PubMed:8962122,
ECO:0000269|PubMed:9103415, ECO:0000269|PubMed:9295051,
ECO:0000269|PubMed:9634237, ECO:0000269|PubMed:9634238,
ECO:0000269|PubMed:9689100}.
-!- SUBUNIT: Monomer. Can form homodimers. Interacts with CD164.
Interacts with ARRB2; the interaction is dependent on the C-
terminal phosphorylation of CXCR4 and allows activation of MAPK1
and MAPK3. Interacts with ARRC; the interaction is dependent on
the C-terminal phosphorylation of CXCR4 and modulates calcium
mobilization. Interacts with RNF113A; the interaction, enhanced by
CXCL12, promotes CXCR4 ubiquitination and subsequent degradation.
Interacts (via the cytoplasmic C-terminal) with ITCH (via the WW
domains I and II); the interaction, enhanced by CXCL12, promotes
CXCR4 ubiquitination and leads to its degradation. Interacts with
extracellular ubiquitin. Interacts with DBN1; this interaction is
enhanced by antigenic stimulation. Following LPS binding, may form
a complex with GDF5, HSP90AA1 and HSPA8.
{ECO:0000250|UniProtKB:P61073}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8962122,
ECO:0000269|PubMed:9295051}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P61073}. Cell junction {ECO:0000250}. Early
endosome {ECO:0000250}. Late endosome {ECO:0000250}. Lysosome
{ECO:0000250}. Note=In unstimulated cells, diffuse pattern on
plasma membrane. On agonist stimulation, colocalizes with ITCH at
the plasma membrane where it becomes ubiquitinated (By
similarity). In the presence of antigen, distributes to the
immunological synapse forming at the T-cell-APC contact area,
where it localizes at the peripheral and distal supramolecular
activation cluster (SMAC) (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=CXCR4-B; Synonyms=LESTR-B;
IsoId=P70658-1; Sequence=Displayed;
Name=CXCR4-A; Synonyms=LESTR-A;
IsoId=P70658-2; Sequence=VSP_001891;
-!- TISSUE SPECIFICITY: Lymphocytes, macrophages, neutrophils,
microglial cells and astrocytes. Found in spleen, thymus, bone
marrow, lymph nodes and, at lower levels in brain, small
intestine, stomach and kidney. CXCR4-A is predominant in all
tissues tested. During embryonic development, high levels are
detected in the endothelium of developing blood vessels and in
many regions of the developing brain including the olfactory
epithelium, olfactory bulb, hippocampus, cerebellum and spinal
cord. {ECO:0000269|PubMed:9634237, ECO:0000269|PubMed:9634238}.
-!- DEVELOPMENTAL STAGE: High expression during embryonic development
does not seem to be associated with the differentiation of any
particular cell type, but is widely utilized when there is a
requirement for cell movement. Frequently associated with less
differentiated cell types and down-regulated with subsequent
differentiation. Detected in sites with hemopoietic potential: the
yolk sac (7.5, 8.5 and 12.5 dpc) and fetal liver (12.5 dpc).
During gastrulation, at 7.2 to 7.8 dpc, expressed in the mesoderm
and the definitive endoderm. As gastrulation pattern fades (8.5
dpc), expression in the mesoderm is down-regulated, while it
becomes predominant in neural ectoderm. Endodermal expression is
retained in the foregut and later in a subset of foregut
derivatives, including the stomach (10.5 dpc), the cystic ducts of
the gall bladder and the lung epithelium (12.5 dpc). In neuronal
tissue: at 10.5 and 12.5 dpc, expressed in the dorsal root
ganglia, in the ventral mantle layer of the spinal cord (or basal
plates), in the hindbrain. At 14.5 dpc, expression more tightly
confined to the neural epithelium lining the ventricular space and
to the external granular layer of the ventral rhombic lip (the
developing cerebellum). Expressed in the outpocketing of the
diencephalic floor at 10.5 dpc and in the developing thalamus and,
to a lesser extent, the developing hypothalamus. At 14.5 dpc,
restricted to the region where thalamus and hypothalamus meet.
Detected in a discrete band of cells at the edge of the olfactory
bulb. In the vascular system: expressed in the endothelium of
numerous blood vessels, but not all, at 10.5, 11.5 and 12.5 dpc,
such as vitelline/umbilical vessels, cardiac ventricular wall
capillaries, facial vessels and, at 14.5 dpc, in the vasculature
of the herniated gut. Expression seems to be associated with
expanding vascular networks. In the heart development, expressed
at 10.5 dpc in the precursor to the aortopulmonary (AP) septum. At
12.5 dpc, detected in the AP septum at the base of the outflow
tract and in the atrioventricular valves. Detected in cranofacial
ectoderm from 10.5 to 14.5 dpc. At 10.5 and 11.5 dpc, expressed in
the Rathke pouch. {ECO:0000269|PubMed:10479460}.
-!- PTM: Phosphorylated on agonist stimulation. Rapidly phosphorylated
on serine and threonine residues in the C-terminal.
Phosphorylation at Ser-331 and Ser-332 leads to recruitment of
ITCH, ubiquitination and protein degradation.
{ECO:0000250|UniProtKB:P61073}.
-!- PTM: Ubiquitinated after ligand binding, leading to its
degradation. Ubiquitinated by ITCH at the cell membrane on agonist
stimulation. The ubiquitin-dependent mechanism, endosomal sorting
complex required for transport (ESCRT), then targets CXCR4 for
lysosomal degradation. This process is dependent also on prior
Ser-/Thr-phosphorylation in the C-terminal of CXCR4. Also binding
of ARRB1 to STAM negatively regulates CXCR4 sorting to lysosomes
though modulating ubiquitination of SFR5S.
{ECO:0000250|UniProtKB:P61073}.
-!- PTM: Sulfation is required for efficient binding of CXCL12/SDF-
1alpha and promotes its dimerization.
{ECO:0000250|UniProtKB:P61073}.
-!- PTM: O- and N-glycosylated. N-glycosylation can mask coreceptor
function. The O-glycosylation chondroitin sulfate attachment does
not affect interaction with CXCL12/SDF-1alpha nor its coreceptor
activity. {ECO:0000250|UniProtKB:P61073}.
-!- DISRUPTION PHENOTYPE: Half of the embryos die by E17.5-E18.5 and
neonates die within a few hours. Mutants display defective
vascular development, cerebellar development, B-lymphopoiesis,
myelopoiesis, and cardiogenesis with defective formation of the
large vessels supplying the gastrointestinal tract.
{ECO:0000269|PubMed:9634237, ECO:0000269|PubMed:9634238,
ECO:0000269|PubMed:9689100}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
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EMBL; U59760; AAB07725.1; -; mRNA.
EMBL; U65580; AAC52953.1; -; Genomic_DNA.
EMBL; D87747; BAA13451.1; -; mRNA.
EMBL; Z80111; CAB02201.1; -; mRNA.
EMBL; Z80112; CAB02202.1; -; mRNA.
EMBL; X99581; CAA67893.1; -; Genomic_DNA.
EMBL; X99582; CAA67894.1; -; mRNA.
EMBL; AB000803; BAA19187.1; -; mRNA.
EMBL; BC031665; AAH31665.1; -; mRNA.
EMBL; BC098322; AAH98322.1; -; mRNA.
CCDS; CCDS15254.1; -. [P70658-1]
RefSeq; NP_034041.2; NM_009911.3.
UniGene; Mm.1401; -.
ProteinModelPortal; P70658; -.
SMR; P70658; -.
BioGrid; 198767; 2.
IntAct; P70658; 1.
STRING; 10090.ENSMUSP00000053489; -.
BindingDB; P70658; -.
ChEMBL; CHEMBL1250365; -.
GuidetoPHARMACOLOGY; 71; -.
iPTMnet; P70658; -.
PhosphoSitePlus; P70658; -.
MaxQB; P70658; -.
PaxDb; P70658; -.
PeptideAtlas; P70658; -.
PRIDE; P70658; -.
GeneID; 12767; -.
KEGG; mmu:12767; -.
UCSC; uc007cls.1; mouse. [P70658-2]
UCSC; uc007clt.1; mouse. [P70658-1]
CTD; 7852; -.
MGI; MGI:109563; Cxcr4.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
HOGENOM; HOG000234122; -.
HOVERGEN; HBG106917; -.
InParanoid; P70658; -.
KO; K04189; -.
PhylomeDB; P70658; -.
TreeFam; TF330966; -.
ChiTaRS; Cxcr4; mouse.
PRO; PR:P70658; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_CXCR4; -.
GO; GO:0031252; C:cell leading edge; ISO:MGI.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
GO; GO:0005769; C:early endosome; ISS:UniProtKB.
GO; GO:0005768; C:endosome; ISO:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0030426; C:growth cone; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005770; C:late endosome; ISS:UniProtKB.
GO; GO:0005764; C:lysosome; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0003779; F:actin binding; ISO:MGI.
GO; GO:0019957; F:C-C chemokine binding; ISO:MGI.
GO; GO:0016494; F:C-X-C chemokine receptor activity; ISO:MGI.
GO; GO:0038147; F:C-X-C motif chemokine 12 receptor activity; ISS:UniProtKB.
GO; GO:0008144; F:drug binding; ISO:MGI.
GO; GO:0032027; F:myosin light chain binding; ISO:MGI.
GO; GO:0043130; F:ubiquitin binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0001667; P:ameboidal-type cell migration; IMP:MGI.
GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc.
GO; GO:0035904; P:aorta development; IMP:MGI.
GO; GO:0007420; P:brain development; IMP:MGI.
GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IMP:MGI.
GO; GO:0019722; P:calcium-mediated signaling; ISO:MGI.
GO; GO:0060048; P:cardiac muscle contraction; ISO:MGI.
GO; GO:0016477; P:cell migration; ISO:MGI.
GO; GO:0071345; P:cellular response to cytokine stimulus; IDA:MGI.
GO; GO:0038160; P:CXCL12-activated CXCR4 signaling pathway; ISS:UniProtKB.
GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; ISO:MGI.
GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; ISO:MGI.
GO; GO:0045446; P:endothelial cell differentiation; ISO:MGI.
GO; GO:0061154; P:endothelial tube morphogenesis; ISO:MGI.
GO; GO:0002064; P:epithelial cell development; ISO:MGI.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; ISO:MGI.
GO; GO:0048699; P:generation of neurons; IEP:DFLAT.
GO; GO:0007281; P:germ cell development; IMP:MGI.
GO; GO:0008354; P:germ cell migration; IMP:MGI.
GO; GO:0035701; P:hematopoietic stem cell migration; IMP:MGI.
GO; GO:0008045; P:motor neuron axon guidance; IMP:MGI.
GO; GO:0043217; P:myelin maintenance; IMP:BHF-UCL.
GO; GO:0007399; P:nervous system development; TAS:ProtInc.
GO; GO:0061351; P:neural precursor cell proliferation; IEP:DFLAT.
GO; GO:0022008; P:neurogenesis; ISO:MGI.
GO; GO:0001764; P:neuron migration; IDA:MGI.
GO; GO:0090280; P:positive regulation of calcium ion import; IDA:MGI.
GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
GO; GO:1903861; P:positive regulation of dendrite extension; ISO:MGI.
GO; GO:1905322; P:positive regulation of mesenchymal stem cell migration; ISO:MGI.
GO; GO:0050769; P:positive regulation of neurogenesis; ISO:MGI.
GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IMP:BHF-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:MGI.
GO; GO:0035470; P:positive regulation of vascular wound healing; ISO:MGI.
GO; GO:0051924; P:regulation of calcium ion transport; ISO:MGI.
GO; GO:0030334; P:regulation of cell migration; IMP:MGI.
GO; GO:0050920; P:regulation of chemotaxis; ISO:MGI.
GO; GO:0043067; P:regulation of programmed cell death; ISO:MGI.
GO; GO:0050792; P:regulation of viral process; ISO:MGI.
GO; GO:0042098; P:T cell proliferation; IMP:MGI.
GO; GO:0022029; P:telencephalon cell migration; ISO:MGI.
GO; GO:0003281; P:ventricular septum development; IMP:MGI.
InterPro; IPR022726; Chemokine_CXCR4_N_dom.
InterPro; IPR000355; Chemokine_rcpt.
InterPro; IPR001277; CXCR4/ACKR2.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
Pfam; PF00001; 7tm_1; 1.
Pfam; PF12109; CXCR4_N; 1.
PRINTS; PR00657; CCCHEMOKINER.
PRINTS; PR00645; CXCCHMKINER4.
PRINTS; PR00237; GPCRRHODOPSN.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
Alternative splicing; Cell junction; Cell membrane; Complete proteome;
Disulfide bond; Endosome; G-protein coupled receptor; Glycoprotein;
Isopeptide bond; Lysosome; Membrane; Phosphoprotein; Proteoglycan;
Receptor; Reference proteome; Sulfation; Transducer; Transmembrane;
Transmembrane helix; Ubl conjugation.
CHAIN 1 359 C-X-C chemokine receptor type 4.
/FTId=PRO_0000069355.
TOPO_DOM 1 40 Extracellular. {ECO:0000305}.
TRANSMEM 41 65 Helical; Name=1.
{ECO:0000250|UniProtKB:P61073}.
TOPO_DOM 66 79 Cytoplasmic. {ECO:0000305}.
TRANSMEM 80 101 Helical; Name=2.
{ECO:0000250|UniProtKB:P61073}.
TOPO_DOM 102 112 Extracellular. {ECO:0000305}.
TRANSMEM 113 132 Helical; Name=3.
{ECO:0000250|UniProtKB:P61073}.
TOPO_DOM 133 156 Cytoplasmic. {ECO:0000305}.
TRANSMEM 157 176 Helical; Name=4.
{ECO:0000250|UniProtKB:P61073}.
TOPO_DOM 177 202 Extracellular. {ECO:0000305}.
TRANSMEM 203 223 Helical; Name=5.
{ECO:0000250|UniProtKB:P61073}.
TOPO_DOM 224 248 Cytoplasmic. {ECO:0000305}.
TRANSMEM 249 268 Helical; Name=6.
{ECO:0000250|UniProtKB:P61073}.
TOPO_DOM 269 289 Extracellular. {ECO:0000305}.
TRANSMEM 290 309 Helical; Name=7.
{ECO:0000250|UniProtKB:P61073}.
TOPO_DOM 310 359 Cytoplasmic. {ECO:0000305}.
REGION 1 23 Important for chemokine binding and
signaling. {ECO:0000250}.
REGION 96 99 Chemokine binding. {ECO:0000250}.
REGION 115 119 Chemokine binding. {ECO:0000250}.
REGION 137 149 Involved in dimerization; when bound to
chemokine. {ECO:0000250}.
REGION 193 197 Chemokine binding, important for
signaling. {ECO:0000250}.
REGION 198 217 Involved in dimerization. {ECO:0000250}.
REGION 273 275 Involved in dimerization. {ECO:0000250}.
MOTIF 135 137 Important for signaling. {ECO:0000250}.
BINDING 173 173 Chemokine. {ECO:0000250}.
BINDING 295 295 Chemokine. {ECO:0000250}.
MOD_RES 9 9 Sulfotyrosine.
{ECO:0000250|UniProtKB:P61073}.
MOD_RES 14 14 Sulfotyrosine.
{ECO:0000250|UniProtKB:P61073}.
MOD_RES 23 23 Sulfotyrosine.
{ECO:0000250|UniProtKB:P61073}.
MOD_RES 326 326 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 328 328 Phosphoserine.
{ECO:0000250|UniProtKB:P61073}.
MOD_RES 331 331 Phosphoserine; by PKC and GRK6.
{ECO:0000250|UniProtKB:P61073}.
MOD_RES 332 332 Phosphoserine; by PKC and GRK6.
{ECO:0000250|UniProtKB:P61073}.
MOD_RES 337 337 Phosphoserine; by GRK6.
{ECO:0000250|UniProtKB:P61073}.
MOD_RES 346 346 Phosphoserine; by GRK6.
{ECO:0000250|UniProtKB:P61073}.
MOD_RES 355 355 Phosphoserine.
{ECO:0000250|UniProtKB:P61073}.
MOD_RES 358 358 Phosphoserine.
{ECO:0000250|UniProtKB:P61073}.
CARBOHYD 13 13 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CARBOHYD 20 20 O-linked (Xyl...) (chondroitin sulfate)
serine. {ECO:0000250|UniProtKB:P61073}.
DISULFID 30 281 {ECO:0000255|PROSITE-ProRule:PRU00521}.
DISULFID 111 193 {ECO:0000255|PROSITE-ProRule:PRU00521}.
CROSSLNK 338 338 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P61073}.
VAR_SEQ 6 7 Missing (in isoform CXCR4-A).
{ECO:0000303|PubMed:9295051}.
/FTId=VSP_001891.
CONFLICT 216 216 I -> V (in Ref. 4; CAA67893 and 6;
BAA19187). {ECO:0000305}.
SEQUENCE 359 AA; 40426 MW; 33D1B5552A31595B CRC64;
MEPISVSIYT SDNYSEEVGS GDYDSNKEPC FRDENVHFNR IFLPTIYFII FLTGIVGNGL
VILVMGYQKK LRSMTDKYRL HLSVADLLFV ITLPFWAVDA MADWYFGKFL CKAVHIIYTV
NLYSSVLILA FISLDRYLAI VHATNSQRPR KLLAEKAVYV GVWIPALLLT IPDFIFADVS
QGDISQGDDR YICDRLYPDS LWMVVFQFQH IMVGLILPGI VILSCYCIII SKLSHSKGHQ
KRKALKTTVI LILAFFACWL PYYVGISIDS FILLGVIKQG CDFESIVHKW ISITEALAFF
HCCLNPILYA FLGAKFKSSA QHALNSMSRG SSLKILSKGK RGGHSSVSTE SESSSFHSS


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