C5AR1_MACMU
ID C5AR1_MACMU Reviewed; 340 AA.
AC P79188;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=C5a anaphylatoxin chemotactic receptor 1;
DE AltName: Full=C5a anaphylatoxin chemotactic receptor;
DE Short=C5a-R;
DE Short=C5aR;
DE AltName: CD_antigen=CD88;
DE Flags: Fragment;
GN Name=C5AR1; Synonyms=C5AR, C5R1;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8824156; DOI=10.1007/bf02602806;
RA Alvarez V., Coto E., Sehen F., Gouzalek-Koces S., Lopez-Larrea C.;
RT "Molecular evolution of the N-formyl peptide and C5a receptors in non-human
RT primates.";
RL Immunogenetics 44:446-452(1996).
CC -!- FUNCTION: Receptor for the chemotactic and inflammatory peptide
CC anaphylatoxin C5a. The ligand interacts with at least two sites on the
CC receptor: a high-affinity site on the extracellular N-terminus, and a
CC second site in the transmembrane region which activates downstream
CC signaling events. Receptor activation stimulates chemotaxis, granule
CC enzyme release, intracellular calcium release and superoxide anion
CC production. {ECO:0000250|UniProtKB:P21730}.
CC -!- SUBUNIT: Homodimer. May also form higher-order oligomers. Interacts
CC (when phosphorylated) with ARRB1 and ARRB2; the interaction is
CC associated with internalization of C5aR. Interacts (via N-terminal
CC domain) with S.aureus chemotaxis inhibitory protein (CHIPS); the
CC interaction blocks the receptor and may thus inhibit the immune
CC response. {ECO:0000250|UniProtKB:P21730}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P21730};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P21730}. Cytoplasmic
CC vesicle {ECO:0000250|UniProtKB:P21730}. Note=Phosphorylated C5aR
CC colocalizes with ARRB1 and ARRB2 in cytoplasmic vesicles.
CC {ECO:0000250|UniProtKB:P21730}.
CC -!- PTM: Sulfation plays a critical role in the association of C5aR with
CC C5a, but no significant role in the ability of the receptor to
CC transduce a signal and mobilize calcium in response to a small peptide
CC agonist. Sulfation at Tyr-7 is important for CHIPS binding.
CC {ECO:0000250|UniProtKB:P21730}.
CC -!- PTM: Phosphorylated on serine residues in response to C5a binding,
CC resulting in internalization of the receptor and short-term
CC desensitization to C5a. {ECO:0000250|UniProtKB:P21730}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; X97731; CAA66315.1; -; Genomic_DNA.
DR AlphaFoldDB; P79188; -.
DR SMR; P79188; -.
DR STRING; 9544.ENSMMUP00000012156; -.
DR eggNOG; ENOG502R35Z; Eukaryota.
DR InParanoid; P79188; -.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0045177; C:apical part of cell; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004878; F:complement component C5a receptor activity; ISS:UniProtKB.
DR GO; GO:0004875; F:complement receptor activity; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0002430; P:complement receptor mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR InterPro; IPR001274; Anaphtx_C5AR1/C5AR2.
DR InterPro; IPR002234; Anphylx_rcpt.
DR InterPro; IPR000826; Formyl_rcpt-rel.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24225; PTHR24225; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01104; ANPHYLATOXNR.
DR PRINTS; PR00426; C5ANPHYLTXNR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Chemotaxis; Cytoplasmic vesicle; Disulfide bond;
KW G-protein coupled receptor; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Sulfation; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN <1..>340
FT /note="C5a anaphylatoxin chemotactic receptor 1"
FT /id="PRO_0000069210"
FT TOPO_DOM <1..30
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 31..57
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 58..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 63..86
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 87..103
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 104..125
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 126..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 147..167
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 168..193
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 194..219
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 220..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 236..258
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 259..275
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 276..296
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 297..>340
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 3..11
FT /note="Required for CHIPS binding"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT REGION 14..23
FT /note="Involved in C5a binding"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT MOD_RES 4
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT MOD_RES 7
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT DISULFID 102..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT NON_TER 1
FT NON_TER 340
SQ SEQUENCE 340 AA; 38274 MW; E11F7C73AB97FFBB CRC64;
TPDYGHYDDK DTLDANTPVD KTSNTLRVPD ILALVIFAVV FLVGVLRNAL VVWVTAFEAK
RTINAIWFLN LAVADFLSCL ALPILFTSIV QHHHWPFGGA ACRILPSLIL LNMYASILLL
ATISADRFLL VFNPIWCQNF RGAGLAWIAC AVAWGLALLL TIPSFLYRVV REEYFPPKVL
CGVDHGHDKR RERAVAIARL VLGFVWPLLT LTMCYTFLLL RTWSRRATRS TKTLKVVVAV
VASFFIFWLP YQVTGMMMSF LEPSSPTFLL LKKLDSLCIS FAYINCCINP IIYVVAGQGF
QGRLRKSLPS LLRNVLTEES MVRESKSFTR STVDTMAQKT
