ID C5AR1_GORGO Reviewed; 350 AA. AC P79175; G3QZV7; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 07-JAN-2015, sequence version 2. DT 26-FEB-2020, entry version 119. 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=C5AR, C5R1; OS Gorilla gorilla gorilla (Western lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Gorilla. OX NCBI_TaxID=9595; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Scally A.; RT "Insights into the evolution of the great apes provided by the gorilla RT genome."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-347. 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-14 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X97733; CAA66317.1; -; Genomic_DNA. DR RefSeq; XP_004061097.1; XM_004061049.2. DR SMR; P79175; -. DR STRING; 9593.ENSGGOP00000008426; -. DR Ensembl; ENSGGOT00000008658; ENSGGOP00000008426; ENSGGOG00000008622. DR GeneTree; ENSGT00980000198522; -. DR InParanoid; P79175; -. DR OMA; ACTLVKG; -. DR OrthoDB; 978188at2759; -. DR TreeFam; TF330976; -. DR Proteomes; UP000001519; Chromosome 19. DR Bgee; ENSGGOG00000008622; Expressed in liver and 5 other tissues. DR GO; GO:0045177; C:apical part of cell; ISS:UniProtKB. DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB. DR GO; GO:0005623; C:cell; IEA:GOC. 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: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..350 FT /note="C5a anaphylatoxin chemotactic receptor 1" FT /evidence="ECO:0000305" FT /id="PRO_0000069208" FT TOPO_DOM 1..37 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 38..64 FT /note="Helical; Name=1" FT /evidence="ECO:0000250|UniProtKB:P21730" FT TOPO_DOM 65..69 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 70..93 FT /note="Helical; Name=2" FT /evidence="ECO:0000250|UniProtKB:P21730" FT TOPO_DOM 94..110 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 111..132 FT /note="Helical; Name=3" FT /evidence="ECO:0000250|UniProtKB:P21730" FT TOPO_DOM 133..153 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 154..174 FT /note="Helical; Name=4" FT /evidence="ECO:0000250|UniProtKB:P21730" FT TOPO_DOM 175..200 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 201..226 FT /note="Helical; Name=5" FT /evidence="ECO:0000250|UniProtKB:P21730" FT TOPO_DOM 227..242 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 243..265 FT /note="Helical; Name=6" FT /evidence="ECO:0000250|UniProtKB:P21730" FT TOPO_DOM 266..282 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 283..303 FT /note="Helical; Name=7" FT /evidence="ECO:0000250|UniProtKB:P21730" FT TOPO_DOM 304..350 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT REGION 10..18 FT /note="Required for CHIPS binding" FT /evidence="ECO:0000250|UniProtKB:P21730" FT REGION 21..30 FT /note="Involved in C5a binding" FT /evidence="ECO:0000250|UniProtKB:P21730" 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 314 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P21730" FT MOD_RES 317 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 332 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 338 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P21730" FT DISULFID 109..188 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" FT CONFLICT 57 FT /note="L -> M (in Ref. 2; CAA66317)" FT /evidence="ECO:0000305" FT CONFLICT 66 FT /note="V -> A (in Ref. 2; CAA66317)" FT /evidence="ECO:0000305" FT CONFLICT 197 FT /note="Q -> R (in Ref. 2; CAA66317)" FT /evidence="ECO:0000305" FT CONFLICT 204 FT /note="V -> I (in Ref. 2; CAA66317)" FT /evidence="ECO:0000305" FT CONFLICT 279 FT /note="K -> N (in Ref. 2; CAA66317)" FT /evidence="ECO:0000305" FT CONFLICT 345 FT /note="E -> Q (in Ref. 2; CAA66317)" FT /evidence="ECO:0000305" SQ SEQUENCE 350 AA; 39376 MW; 5229D43B0D900CFC CRC64; MDSFNYTTPD YGHYDDKDTL DPNTPVDKTS NTLRVPDILA LVIFAVVFLV GVLGNALVVW VTAFEVKRTI NAIWFLNLAV ADFLSCLALP ILFTSIVQHH HWPFGGAACR ILPSLILLNM YASILLLATI SADRFLLVFK PIWCQNFRGA GLAWIACAVA WGLALLLTIP SFLYRVVREE YFPPKVLCGV DYSHDKQRER AVAVVRLVLG FLWPLLTLTI CYTFILLRTW SRRATRSTKT LKVVVAVVAS FFIFWLPYQV TGIMMSFLEP SSPTFLLLKK LDSLCVSFAY INCCINPIIY VVAGQGFQGR LRKSLPSLLR NVLTEESVVR ESKSFTRSTV DTMAEKTQAV //