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 27-MAY-2015, entry version 87. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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- RT human 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 CC the receptor: a high-affinity site on the extracellular N- CC terminus, and a second site in the transmembrane region which CC activates downstream signaling events. Receptor activation CC stimulates chemotaxis, granule enzyme release, intracellular CC calcium release and superoxide anion production. CC {ECO:0000250|UniProtKB:P21730}. CC -!- SUBUNIT: Homodimer. May also form higher-order oligmers. 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 CC {ECO:0000250|UniProtKB:P21730}; Multi-pass membrane protein CC {ECO:0000255}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P21730}. CC Note=Phosphorylated C5aR colocalizes with ARRB1 and ARRB2 in CC cytoplasmic vesicles. {ECO:0000250|UniProtKB:P21730}. CC -!- PTM: Sulfation plays a critical role in the association of C5aR CC with C5a, but no significant role in the ability of the receptor CC to transduce a signal and mobilize calcium in response to a small CC peptide agonist. Sulfation at Tyr-14 is important for CHIPS CC binding. {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_004061049.1. DR ProteinModelPortal; P79175; -. DR Ensembl; ENSGGOT00000008658; ENSGGOP00000008426; ENSGGOG00000008622. DR GeneID; 101126529; -. DR KEGG; ggo:101126529; -. DR CTD; 728; -. DR GeneTree; ENSGT00760000118990; -. DR HOVERGEN; HBG107927; -. DR InParanoid; P79175; -. DR KO; K04010; -. DR OMA; YINCCIN; -. DR OrthoDB; EOG71P2BC; -. DR Proteomes; UP000001519; Chromosome 19. DR GO; GO:0045177; C:apical part of cell; ISS:UniProtKB. DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB. DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004944; F:C5a anaphylatoxin receptor activity; ISS:UniProtKB. DR GO; GO:0004878; F:complement component C5a receptor activity; ISS:UniProtKB. DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW. DR GO; GO:0038178; P:complement component C5a signaling pathway; ISS:GOC. DR GO; GO:0042789; P:mRNA transcription from RNA polymerase II promoter; 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 PANTHER; PTHR24225:SF28; PTHR24225:SF28; 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; Complete proteome; Cytoplasmic vesicle; KW Disulfide bond; G-protein coupled receptor; Membrane; Phosphoprotein; KW Receptor; Reference proteome; Sulfation; Transducer; Transmembrane; KW Transmembrane helix. FT CHAIN 1 350 C5a anaphylatoxin chemotactic receptor 1. FT {ECO:0000305}. FT /FTId=PRO_0000069208. FT TOPO_DOM 1 37 Extracellular. {ECO:0000255}. FT TRANSMEM 38 60 Helical; Name=1. {ECO:0000255}. FT TOPO_DOM 61 71 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 72 94 Helical; Name=2. {ECO:0000255}. FT TOPO_DOM 95 110 Extracellular. {ECO:0000255}. FT TRANSMEM 111 132 Helical; Name=3. {ECO:0000255}. FT TOPO_DOM 133 153 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 154 174 Helical; Name=4. {ECO:0000255}. FT TOPO_DOM 175 200 Extracellular. {ECO:0000255}. FT TRANSMEM 201 226 Helical; Name=5. {ECO:0000255}. FT TOPO_DOM 227 242 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 243 265 Helical; Name=6. {ECO:0000255}. FT TOPO_DOM 266 282 Extracellular. {ECO:0000255}. FT TRANSMEM 283 303 Helical; Name=7. {ECO:0000255}. FT TOPO_DOM 304 350 Cytoplasmic. {ECO:0000255}. FT REGION 10 18 Required for CHIPS binding. FT {ECO:0000250|UniProtKB:P21730}. FT REGION 21 30 Involved in C5a binding. FT {ECO:0000250|UniProtKB:P21730}. FT MOD_RES 11 11 Sulfotyrosine. FT {ECO:0000250|UniProtKB:P21730}. FT MOD_RES 14 14 Sulfotyrosine. FT {ECO:0000250|UniProtKB:P21730}. FT MOD_RES 314 314 Phosphoserine. FT {ECO:0000250|UniProtKB:P21730}. FT MOD_RES 317 317 Phosphoserine. FT {ECO:0000250|UniProtKB:P21730}. FT MOD_RES 327 327 Phosphoserine. FT {ECO:0000250|UniProtKB:P21730}. FT MOD_RES 332 332 Phosphoserine. FT {ECO:0000250|UniProtKB:P21730}. FT MOD_RES 334 334 Phosphoserine. FT {ECO:0000250|UniProtKB:P21730}. FT MOD_RES 338 338 Phosphoserine. FT {ECO:0000250|UniProtKB:P21730}. FT DISULFID 109 188 {ECO:0000255|PROSITE-ProRule:PRU00521}. FT CONFLICT 57 57 L -> M (in Ref. 2; CAA66317). FT {ECO:0000305}. FT CONFLICT 66 66 V -> A (in Ref. 2; CAA66317). FT {ECO:0000305}. FT CONFLICT 197 197 Q -> R (in Ref. 2; CAA66317). FT {ECO:0000305}. FT CONFLICT 204 204 V -> I (in Ref. 2; CAA66317). FT {ECO:0000305}. FT CONFLICT 279 279 K -> N (in Ref. 2; CAA66317). FT {ECO:0000305}. FT CONFLICT 345 345 E -> Q (in Ref. 2; CAA66317). FT {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 //