| Post Translational Modifications | Sulfated on at least 2 of the N-terminal tyrosines. Sulfation contributes to the efficiency of HIV-1 entry and is required for efficient binding of the chemokines, CCL3 and CCL4. O-glycosylated, but not N-glycosylated. Ser-6 appears to be the major site even if Ser-7 may be also O-glycosylated. Also sialylated glycans present which contribute to chemokine binding. Thr-16 and Ser-17 may also be glycosylated and, if so, with small moieties such as a T-antigen. Palmitoylation in the C-terminal is important for cell surface expression, and to a lesser extent, for HIV entry. Phosphorylation on serine residues in the C-terminal is stimulated by binding CC chemokines especially by APO-RANTES. |
| Function | Receptor for a number of inflammatory CC-chemokines including CCL3/MIP-1-alpha, CCL4/MIP-1-beta and RANTES and subsequently transduces a signal by increasing the intracellular calcium ion level. May play a role in the control of granulocytic lineage proliferation or differentiation. Participates in T-lymphocyte migration to the infection site by acting as a chemotactic receptor. (Microbial infection) Acts as a coreceptor (CD4 being the primary receptor) of human immunodeficiency virus-1/HIV-1. |
| Protein Name | C-C Chemokine Receptor Type 5C-C Ckr-5Cc-Ckr-5Ccr-5Ccr5Chemr13Hiv-1 Fusion CoreceptorCd Antigen Cd195 |
| Database Links | Reactome: R-HSA-173107Reactome: R-HSA-380108Reactome: R-HSA-418594Reactome: R-HSA-6783783 |
| Cellular Localisation | Cell MembraneMulti-Pass Membrane Protein |
| Alternative Protein Names | C-C Chemokine Receptor Type 5 proteinC-C Ckr-5 proteinCc-Ckr-5 proteinCcr-5 proteinCcr5 proteinChemr13 proteinHiv-1 Fusion Coreceptor proteinCd Antigen Cd195 proteinCCR5 proteinCMKBR5 protein |
Information sourced from Uniprot.org
