C5AR1_CANLF
ID C5AR1_CANLF Reviewed; 352 AA.
AC P30992;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 136.
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;
GN Name=C5AR1; Synonyms=C5R1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1472004; DOI=10.1042/bj2880911;
RA Perret J.J., Raspe E., Vassart G., Parmentier M.;
RT "Cloning and functional expression of the canine anaphylatoxin C5a
RT receptor. Evidence for high interspecies variability.";
RL Biochem. J. 288:911-917(1992).
CC -!- FUNCTION: Receptor for the chemotactic and inflammatory peptide
CC anaphylatoxin C5a (PubMed:1472004). The ligand interacts with at least
CC two sites on the receptor: a high-affinity site on the extracellular N-
CC terminus, and a second site in the transmembrane region which activates
CC downstream signaling events. Receptor activation stimulates chemotaxis,
CC granule enzyme release, intracellular calcium release and superoxide
CC anion production (By similarity). {ECO:0000250|UniProtKB:P21730,
CC ECO:0000269|PubMed:1472004}.
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.
CC {ECO:0000250|UniProtKB:P21730}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1472004};
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. {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; X65860; CAA46690.1; -; mRNA.
DR PIR; S27357; S27357.
DR RefSeq; NP_001003373.1; NM_001003373.1.
DR AlphaFoldDB; P30992; -.
DR SMR; P30992; -.
DR STRING; 9612.ENSCAFP00000039091; -.
DR ChEMBL; CHEMBL5745; -.
DR PaxDb; P30992; -.
DR GeneID; 442974; -.
DR KEGG; cfa:442974; -.
DR CTD; 728; -.
DR eggNOG; ENOG502R35Z; Eukaryota.
DR InParanoid; P30992; -.
DR PRO; PR:P30992; -.
DR Proteomes; UP000002254; 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 2: Evidence at transcript level;
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..352
FT /note="C5a anaphylatoxin chemotactic receptor 1"
FT /id="PRO_0000069206"
FT TOPO_DOM 1..38
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 39..65
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 66..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 71..94
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 95..111
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 112..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 134..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 155..175
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 176..202
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 203..228
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 229..244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 245..267
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 268..284
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 285..305
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 306..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOD_RES 11
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT MOD_RES 14
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT DISULFID 110..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 352 AA; 39213 MW; A31F8F1F8D02F135 CRC64;
MASMNFSPPE YPDYGTATLD PNIFVDESLN TPKLSVPDMI ALVIFVMVFL VGVPGNFLVV
WVTGFEVRRT INAIWFLNLA VADLLSCLAL PILFSSIVQQ GYWPFGNAAC RILPSLILLN
MYASILLLTT ISADRFVLVF NPIWCQNYRG PQLAWAACSV AWAVALLLTV PSFIFRGVHT
EYFPFWMTCG VDYSGVGVLV ERGVAILRLL MGFLGPLVIL SICYTFLLIR TWSRKATRST
KTLKVVVAVV VSFFVLWLPY QVTGMMMALF YKHSESFRRV SRLDSLCVAV AYINCCINPI
IYVLAAQGFH SRFLKSLPAR LRQVLAEESV GRDSKSITLS TVDTPAQKSQ GV
