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atypical chemokine receptor 3; C-X-C chemokine receptor type 7; CXC-R7; CXCR-7; chemokine orphan receptor 1; G-protein coupled receptor 159; G-protein coupled receptor RDC1 homolog; RDC-1 (ACKR3, CMKOR1, CXCR7, GPR159, RDC1)

Function: - atypical chemokine receptor - controls chemokine levels & localization via high-affinity chemokine binding uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis - also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor - acts as a receptor for chemokines CXCL11 & CXCL12/SDF1 - chemokine binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalization & activation of MAPK signaling pathway - required for regulation of CXCR4 protein levels in migrating interneurons, thereby adapting their chemokine responsiveness - in glioma cells, transduces signals via MEK/ERK pathway, mediating resistance to apoptosis - promotes cell growth & survival - plays a regulatory role in CXCR4-mediated activation of cell surface integrins by CXCL12 - required for heart valve development - the Ser/Thr residues in the C-terminal cytoplasmic tail may be phosphorylated - ubiquitinated on Lys in its C-terminal cytoplasmic tail & is essential for correct trafficking from & to the cell membrane - deubiquitinated by CXCL12-stimulation (reversible) - homodimer - can form heterodimers with CXCR4 - heterodimerization may regulate CXCR4 signaling activity - interacts with ARRB1 & ARRB2 Structure: - the C-terminal cytoplasmic tail, plays a key role in: - correct trafficking to the cell membrane - recruitment of beta-arrestin - ubiquitination, - chemokine scavenging & signaling functions - the Ser/Thr residues & the Lys residues in the C-terminal cytoplasmic tail are essential for beta-arrestin recruitment & ubiquitination respectively - belongs to the G-protein coupled receptor 1 family atypical chemokine receptor subfamily Compartment: - cell membrane; multi-pass membrane protein - cytoplasm, perinuclear region. early endosome, recycling endosome - predominantly localizes to endocytic vesicles, & upon stimulation by the ligand is internalized via clathrin-coated pits in a beta-arrestin-dependent manner - once internalized, the ligand dissociates from the receptor, & is targeted to degradation while the receptor is recycled back to the cell membrane Expression: - expressed in monocytes, basophils, B-cells, umbilical vein endothelial cells & B-lymphoblastoid cells - lower expression detected in CD4+ T-cell & NK cells - in brain, detected in endothelial cells & capillaries, & in mature neurons of the frontal cortex & hippocampus - expressed in tubular formation in the kidney - highly expressed in astroglial tumor endothelial, microglial & glioma cells - expressed at low levels in normal CD34+ progenitor cells, but at very high levels in several myeloid malignant cell lines - expressed in breast carcinomas but not in normal breast tissue (at protein level) - up-regulated during cell differentiation in glioma cells Pathology: - acts as coreceptor with CXCR4 for a restricted number of HIV1 isolates - not involved in cell migration, adhesion or proliferation of normal hematopoietic progenitors but activated by CXCL11 in malignant hemapoietic cells, leading to phosphorylation of ERK1/2 (MAPK3/MAPK1) & enhanced cell adhesion & migration Note: originally thought to be receptor for VIP [4]

General

atypical chemokine receptor; chemokine-scavenging receptor; chemokine decoy receptor CXC chemokine receptor glycoprotein

Properties

SIZE: entity length = 362 aa MW = 41 kD COMPARTMENT: cytoplasm cell nucleus MOTIF: exoplasmic domain {1-40} MOTIF: N-glycosylation site {N13} N-glycosylation site {N22} N-glycosylation site {N39} transmembrane domain {41-61} cytoplasmic loop {62-81} transmembrane domain {82-102} exoplasmic loop {103-118} MOTIF: cysteine residue {C117} MODIFICATION: cysteine residue {C196} transmembrane domain {119-139} cytoplasmic loop {140-162} transmembrane domain {163-183} exoplasmic loop {184-213} MOTIF: cysteine residue {C196} MODIFICATION: cysteine residue {C117} transmembrane domain {214-234} cytoplasmic loop {235-252} transmembrane domain {253-273} exoplasmic loop {274-296} transmembrane domain {297-319} cytoplasmic domain {320-362} MOTIF: C-terminal cytoplasmic tail {324-362}

Database Correlations

OMIM 610376 UniProt P25106 Pfam PF00001 Entrez Gene 57007 Kegg hsa:57007

References

  1. UniProt :accession P25106
  2. Atlas of genetics & cytogenetics in oncology & haematology http://atlasgeneticsoncology.org/genes/CMKOR1ID40108ch2q37.html
  3. Wikipedia; CXC chemokine receptors entry http://en.wikipedia.org/wiki/CXC_chemokine_receptors
  4. Sreedharan SP, Robichon A, Peterson KE, Goetzl EJ. Cloning and expression of the human vasoactive intestinal peptide receptor. Proc Natl Acad Sci U S A. 1991 Jun 1;88(11):4986-90 PMID: 1675791