Recombinant Human C5a anaphylatoxin chemotactic receptor (C5AR1), partial, Biotinylated

Function

Receptor for the chemotactic and inflammatory peptide anaphylatoxin C5a, stimulating chemotaxis, granule enzyme release, intracellular calcium release and superoxide anion production (PubMed:10636859, PubMed:15153520, PubMed:1847994, PubMed:29300009, PubMed:36806352, PubMed:7622471, PubMed:8182049, PubMed:9553099). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as adenylate cyclase (PubMed:36806352, PubMed:37852260). C5AR1 is coupled to G(i)/G(o) (GNAI1 or GNAO1) G alpha proteins and mediates inhibition of adenylate cyclase (PubMed:36806352, PubMed:37852260). The ligand interacts with at least two sites on the receptor: a high-affinity site on the extracellular N-terminus, and a second site in the transmembrane region which activates downstream signaling events (PubMed:7622471, PubMed:8182049, PubMed:9553099)

Subcellular Location

Cell membrane (Multi-pass membrane protein); Cytoplasmic vesicle

Subunit

(Microbial infection) Interacts (via N-terminal domain) with S.aureus chemotaxis inhibitory protein (CHIPS); the interaction blocks the receptor and may thus inhibit the immune response

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• Gerard N.P. et al. The chemotactic receptor for human C5a anaphylatoxin. — Nature (1991)
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• The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). — Genome Res. (2004)
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• DeMartino J.A. et al. The amino terminus of the human C5a receptor is required for high affinity C5a binding and for receptor activation by C5a but not C5a analogs. — J. Biol. Chem. (1994)