C5AR1
entrez
728
canonical
uniprot
P21730
canonical
ensembl
ENSG00000197405
resolver
ensp
ENSP00000347197
resolver
enst
ENST00000355085
resolver
genesymbol
C5AR1
resolver
genesymbol_syn
C5AR
resolver
genesymbol_syn
C5R1
resolver
hgnc
HGNC:1338
resolver
uniprot_entry
C5AR1_HUMAN
resolver
activity_regulation
ACTIVITY REGULATION: Activated by peptide agonist PMX53 (PubMed:29867214). Specifically inhibited by small-molecule antagonist NDT9513727 (PubMed:29300009, PubMed:29867214). {ECO:0000269|PubMed:29300009, ECO:0000269|PubMed:29867214}.
uniprot
proteins
amino_acid_sequence
MDSFNYTTPDYGHYDDKDTLDLNTPVDKTSNTLRVPDILALVIFAVVFLVGVLGNALVVWVTAFEAKRTINAIWFLNLAVADFLSCLALPILFTSIVQHHHWPFGGAACSILPSLILLNMYASILLLATISADRFLLVFKPIWCQNFRGAGLAWIACAVAWGLALLLTIPSFLYRVVREEYFPPKVLCGVDYSHDKRRERAVAIVRLVLGFLWPLLTLTICYTFILLRTWSRRATRSTKTLKVVVAVVASFFIFWLPYQVTGIMMSFLEPSSPTFLLLKKLDSLCVSFAYINCCINPIIYVVAGQGFQGRLRKSLPSLLRNVLTEESVVRESKSFTRSTVDTMAQKTQAV
uniprot
proteins
function
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). {ECO:0000269|PubMed:10636859, ECO:0000269|PubMed:15153520, ECO:0000269|PubMed:1847994, ECO:0000269|PubMed:29300009, ECO:0000269|PubMed:36806352, ECO:0000269|PubMed:37852260, ECO:0000269|PubMed:7622471, ECO:0000269|PubMed:8182049, ECO:0000269|PubMed:9553099}.
uniprot
proteins
mass_dalton
39336
uniprot
proteins
mutagenesis
MUTAGEN 2..30; /note="Missing: Strongly impairs C5a binding (45,000-fold)."; /evidence="ECO:0000269|PubMed:8182049"; MUTAGEN 2..22; /note="Missing: Impairs C5a binding. Strongly impairs C5a binding; when associated with A-27."; /evidence="ECO:0000269|PubMed:8182049"; MUTAGEN 10; /note="D->A: Strongly impairs C5a binding; when associated with A-15; A-16; A-18 and A-21 (PubMed:8182049). Moderately impairs CHIPS binding (PubMed:15542591). Strongly impairs CHIPS binding; when associated with A-15 (PubMed:15542591). Strongly impairs CHIPS binding; when associated with A-18 (PubMed:15542591)."; /evidence="ECO:0000269|PubMed:15542591, ECO:0000269|PubMed:8182049"; MUTAGEN 11; /note="Y->F: Weakly impairs CHIPS binding. Loss of CHIPS binding; when associated with F-14."; /evidence="ECO:0000269|PubMed:21706042"; MUTAGEN 12; /note="G->A: Moderately impairs CHIPS binding."; /evidence="ECO:0000269|PubMed:15542591"; MUTAGEN 14; /note="Y->F: Weakly impairs CHIPS binding (PubMed:15542591). Strongly impairs CHIPS binding (PubMed:21706042). Loss of CHIPS binding; when associated with F-11 (PubMed:21706042)."; /evidence="ECO:0000269|PubMed:15542591, ECO:0000269|PubMed:21706042"; MUTAGEN 15; /note="D->A: Strongly impairs C5a binding; when associated with A-10; A-16; A-18 and A-21 (PubMed:8182049). Moderately impairs CHIPS binding (PubMed:15542591). Strongly impairs CHIPS binding; when associated with A-10 (PubMed:15542591). Strongly impairs CHIPS binding; when associated with A-18 (PubMed:15542591)."; /evidence="ECO:0000269|PubMed:15542591, ECO:0000269|PubMed:8182049"; MUTAGEN 16; /note="D->A: Strongly impairs C5a binding; when associated with A-10; A-15; A-18 and A-21."; /evidence="ECO:0000269|PubMed:8182049"; MUTAGEN 18; /note="D->A: Strongly impairs C5a binding; when associated with A-10; A-15; A-16 and A-21 (PubMed:8182049). Impairs CHIPS binding (PubMed:15542591). Strongly impairs CHIPS binding; when associated with A-10 (PubMed:15542591). Strongly impairs CHIPS binding; when associated with A-15 (PubMed:15542591)."; /evidence="ECO:0000269|PubMed:15542591, ECO:0000269|PubMed:8182049"; MUTAGEN 21; /note="D->A: Strongly impairs C5a binding; when associated with A-10; A-15; A-16 and A-18."; /evidence="ECO:0000269|PubMed:8182049"; MUTAGEN 27; /note="D->A: Strongly impairs C5a binding; when associated with 2-D--L-22 Del. Decreased ability to activate G(i)/GNAI1."; /evidence="ECO:0000269|PubMed:37169960, ECO:0000269|PubMed:8182049"; MUTAGEN 33; /note="Missing: Decreased ability to activate G(i)/GNAI1."; /evidence="ECO:0000269|PubMed:37169960"; MUTAGEN 34; /note="Missing: Decreased ability to activate G(i)/GNAI1."; /evidence="ECO:0000269|PubMed:37169960"; MUTAGEN 144; /note="C->S: Fails to homodimerize."; /evidence="ECO:0000269|PubMed:12835319"; MUTAGEN 157; /note="C->S: No effect on homodimer formation."; /evidence="ECO:0000269|PubMed:12835319"; MUTAGEN 175; /note="R->A: Reduced activation by anaphylatoxin C5a."; /evidence="ECO:0000269|PubMed:36806352"; MUTAGEN 180; /note="E->A: Decreased ability to activate G(i)/GNAI1."; /evidence="ECO:0000269|PubMed:36806352"; MUTAGEN 181; /note="Y->A: Decreased ability to activate G(i)/GNAI1."; /evidence="ECO:0000269|PubMed:36806352"; MUTAGEN 182; /note="F->A: Decreased ability to activate G(i)/GNAI1."; /evidence="ECO:0000269|PubMed:36806352"; MUTAGEN 183; /note="P->A: Decreased ability to activate G(i)/GNAI1."; /evidence="ECO:0000269|PubMed:36806352"; MUTAGEN 191; /note="D->A: Reduced activation by anaphylatoxin C5a."; /evidence="ECO:0000269|PubMed:36806352"; MUTAGEN 199; /note="E->A: Reduced activation by anaphylatoxin C5a."; /evidence="ECO:0000269|PubMed:36806352"; MUTAGEN 199; /note="E->Q: Impairs C5a binding (10-fold reduction) and C5a-induced 5-HT secretion."; /evidence="ECO:0000269|PubMed:7622471"; MUTAGEN 221; /note="C->S: No effect on homodimer formation."; /evidence="ECO:0000269|PubMed:12835319"; MUTAGEN 258; /note="Y->A: Decreased ability to activate G(i)/GNAI1. Reduced activation by anaphylatoxin C5a."; /evidence="ECO:0000269|PubMed:36806352, ECO:0000269|PubMed:37169960"; MUTAGEN 282; /note="D->A: Decreased ability to activate G(i)/GNAI1. Reduced activation by anaphylatoxin C5a."; /evidence="ECO:0000269|PubMed:36806352, ECO:0000269|PubMed:37169960"; MUTAGEN 336; /note="T->TR: Impaired interaction with ARRB1 and ARRB2."; /evidence="ECO:0000269|PubMed:37209686
uniprot
proteins
post_translational_modification
PTM: Phosphorylation of the P-X-P-P motif by GRK2 or GRK3 in response to C5a binding promotes association with beta-arrestin (ARRB1 and/or ARRB2), resulting in internalization of the receptor and short-term desensitization to the ligand. {ECO:0000269|PubMed:10636859, ECO:0000269|PubMed:12464600, ECO:0000269|PubMed:37209686}.; PTM: Sulfation plays a critical role in the association of C5aR with C5a, but no significant role in the ability of the receptor to transduce a signal and mobilize calcium in response to a small a small peptide agonist (PubMed:11342590). Sulfation at Tyr-14 is important for CHIPS binding (PubMed:21706042). {ECO:0000269|PubMed:11342590, ECO:0000303|PubMed:21706042}.
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
pubmed
10508278
uniprot
proteins
pubmed
10636859
uniprot
proteins
pubmed
11342590
uniprot
proteins
pubmed
12464600
uniprot
proteins
pubmed
12835319
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15153520
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15542591
uniprot
proteins
pubmed
1847994
uniprot
proteins
pubmed
19251703
uniprot
proteins
pubmed
2007135
uniprot
proteins
pubmed
21706042
uniprot
proteins
pubmed
29300009
uniprot
proteins
pubmed
29867214
uniprot
proteins
pubmed
36806352
uniprot
proteins
pubmed
37169960
uniprot
proteins
pubmed
37209686
uniprot
proteins
pubmed
37852260
uniprot
proteins
pubmed
7622471
uniprot
proteins
pubmed
7642584
uniprot
proteins
pubmed
8182049
uniprot
proteins
pubmed
8383526
uniprot
proteins
pubmed
9553099
uniprot
proteins
sequence_length
350
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12464600, ECO:0000269|PubMed:29300009}; Multi-pass membrane protein {ECO:0000269|PubMed:29300009}. Cytoplasmic vesicle {ECO:0000269|PubMed:12464600}. Note=Phosphorylated C5aR colocalizes with ARRB1 and ARRB2 in cytoplasmic vesicles. {ECO:0000269|PubMed:12464600}.
uniprot
proteins
transmembrane_region
TRANSMEM 38..64; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:29300009, ECO:0000269|PubMed:37169960, ECO:0000269|PubMed:37852260, ECO:0007744|PDB:8HK5, ECO:0007744|PDB:8IA2, ECO:0007744|PDB:8JZZ"; TRANSMEM 70..93; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:29300009, ECO:0000269|PubMed:37169960, ECO:0000269|PubMed:37852260, ECO:0007744|PDB:8HK5, ECO:0007744|PDB:8IA2, ECO:0007744|PDB:8JZZ"; TRANSMEM 111..132; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:29300009, ECO:0000269|PubMed:37169960, ECO:0000269|PubMed:37852260, ECO:0007744|PDB:8HK5, ECO:0007744|PDB:8IA2, ECO:0007744|PDB:8JZZ"; TRANSMEM 154..174; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:29300009, ECO:0000269|PubMed:37169960, ECO:0000269|PubMed:37852260, ECO:0007744|PDB:8HK5, ECO:0007744|PDB:8IA2, ECO:0007744|PDB:8JZZ"; TRANSMEM 201..226; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:29300009, ECO:0000269|PubMed:37169960, ECO:0000269|PubMed:37852260, ECO:0007744|PDB:8HK5, ECO:0007744|PDB:8IA2, ECO:0007744|PDB:8JZZ"; TRANSMEM 243..265; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:29300009, ECO:0000269|PubMed:37169960, ECO:0000269|PubMed:37852260, ECO:0007744|PDB:8HK5, ECO:0007744|PDB:8IA2, ECO:0007744|PDB:8JZZ"; TRANSMEM 283..303; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:29300009, ECO:0000269|PubMed:37169960, ECO:0000269|PubMed:37852260, ECO:0007744|PDB:8HK5, ECO:0007744|PDB:8IA2, ECO:0007744|PDB:8JZZ
uniprot
proteins