C5AR1_CAVPO
ID C5AR1_CAVPO Reviewed; 345 AA.
AC O70129;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 112.
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 Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Hartley;
RX PubMed=9576615; DOI=10.1093/intimm/10.3.275;
RA Fukuoka Y., Ember J.A., Yasui A., Hugli T.E.;
RT "Cloning and characterization of the guinea pig C5a anaphylatoxin receptor:
RT interspecies diversity among the C5a receptors.";
RL Int. Immunol. 10:275-283(1998).
CC -!- FUNCTION: Receptor for the chemotactic and inflammatory peptide
CC anaphylatoxin C5a (PubMed:9576615). 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:9576615}.
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:9576615};
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 -!- TISSUE SPECIFICITY: Expressed strongly in macrophages and spleen. Weak
CC expression detected in lung, liver, brain, heart and kidney.
CC {ECO:0000269|PubMed:9576615}.
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; U86103; AAC40074.1; -; mRNA.
DR RefSeq; NP_001166393.1; NM_001172922.1.
DR AlphaFoldDB; O70129; -.
DR SMR; O70129; -.
DR STRING; 10141.ENSCPOP00000020216; -.
DR ChEMBL; CHEMBL2861; -.
DR GeneID; 100135489; -.
DR KEGG; cpoc:100135489; -.
DR CTD; 728; -.
DR eggNOG; ENOG502R35Z; Eukaryota.
DR InParanoid; O70129; -.
DR OrthoDB; 978188at2759; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
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:0004878; F:complement component C5a receptor activity; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISS:UniProtKB.
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; 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; Glycoprotein; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Sulfation; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..345
FT /note="C5a anaphylatoxin chemotactic receptor 1"
FT /id="PRO_0000069207"
FT TOPO_DOM 1..32
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 33..59
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 60..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 65..88
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 89..105
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 106..127
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 128..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 149..169
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 170..195
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 196..221
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 222..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 238..260
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 261..277
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 278..298
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 299..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOD_RES 9
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT MOD_RES 11
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT MOD_RES 322
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 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 104..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 345 AA; 38592 MW; BE40459F1450404A CRC64;
MMVTVSYDYD YNSTFLPDGF VDNYVERLSF GDLVAVVIMV VVFLVGVPGN ALVVWVTACE
ARRHINAIWF LNLAAADLLS CLALPILLVS TVHLNHWYFG DTACKVLPSL ILLNMYTSIL
LLATISADRL LLVLSPIWCQ RFRGGCLAWT ACGLAWVLAL LLSSPSFLYR RTHNEHFSFK
VYCVTDYGRD ISKERAVALV RLLVGFIVPL ITLTACYTFL LLRTWSRKAT RSAKTVKVVV
AVVSSFFVFW LPYQVTGILL AWHSPNSATY RNTKALDAVC VAFAYINCCI NPIIYVVAGH
GFQGRLLKSL PSVLRNVLTE ESLDKRHQSF ARSTVDTMPQ KSESV
