CCR2 is a member of the beta chemokine receptor family. CCR2 is a seven transmembrane protein similar to G protein-coupled receptors. This gene encodes two isoforms of a receptor for monocyte chemoattractant protein-1, a chemokine which specifically mediates monocyte chemotaxis. Monocyte chemoattractant protein-1 is involved in monocyte infiltration in inflammatory diseases such as rheumatoid arthritis as well as in the inflammatory response against tumors. The receptors encoded by this gene mediate agonist-dependent calcium mobilization and inhibition of adenylyl cyclase. This gene is located in the chemokine receptor gene cluster region including CCR1, CCRL2, CCR3, CCR5 and CCXCR1 on chromosome 3p.

Size: 7195 bases.
2 isoforms:
- C-C chemokine receptor type 2 isoform A. CCDS43078.1
- C-C chemokine receptor type 2 isoform B. CCDS46813.1

Homo sapiens chemokine (C-C motif) receptor 2 (CCR2), transcript variant A, mRNA: 2689 bp.
Homo sapiens chemokine (C-C motif) receptor 2 (CCR2), transcript variant B, mRNA: 2335 bp.

No pseudogenes have been reported for CCR2.

Chemokine receptors are cytokine receptors found on the surface of cells, which interact with a type of cytokine called a chemokine. They have a 7 transmembrane structure and couple to G-protein for signal transduction within a cell, making them members of a large protein family of G protein-coupled receptors. Following interaction with their specific chemokine ligands, chemokine receptors trigger a flux in intracellular calcium (Ca²⁺) ions (calcium signaling). This causes cell responses, including the onset of a process known as chemotaxis that traffics the cell to a desired location within the organism. Chemokine receptors share many common structural features; they are composed of about 350 amino acids that are divided into a short and acidic N-terminal end, seven helical transmembrane domains with three intracellular and three extracellular hydrophilic loops, and an intracellular C-terminus containing serine and threonine residues that act as phosphorylation sites during receptor regulation. The first two extracellular loops of chemokine receptors are linked together by disulfide bonding between two conserved cysteine residues. The N-terminal end of a chemokine receptor binds to chemokine(s) and is important for ligand specificity. G-proteins couple to the C-terminal end, which is important for receptor signaling following ligand binding.

374 amino acids; 41915 Da.

Peripheral blood monocytes, activated T cells, B cells and immature dendritic cells.

Cell membrane; multi-pass membrane protein.

Receptor for the MCP-1/CCL2, MCP-3/CCL7 and MCP-4/CCL13 chemokines. Transduces a signal by increasing the intracellular calcium ions level. Alternative coreceptor with CD4 for HIV-1 infection.

CCR2 proteins contains amino acid sequence homology to other C-C chemokines. CCR1 (56%), CCR5 (71%), CCR3 (78%), CCR4 (75%).