C5AR1_GORGO
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 25-MAY-2022, entry version 123.
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}.
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DR EMBL; X97733; CAA66317.1; -; Genomic_DNA.
DR RefSeq; XP_004061097.1; XM_004061049.2.
DR AlphaFoldDB; P79175; -.
DR SMR; P79175; -.
DR STRING; 9593.ENSGGOP00000008426; -.
DR Ensembl; ENSGGOT00000008658; ENSGGOP00000008426; ENSGGOG00000008622.
DR eggNOG; ENOG502R35Z; Eukaryota.
DR GeneTree; ENSGT01020000230336; -.
DR InParanoid; P79175; -.
DR OMA; YTFLLIR; -.
DR OrthoDB; 978188at2759; -.
DR TreeFam; TF330976; -.
DR Proteomes; UP000001519; Chromosome 19.
DR Bgee; ENSGGOG00000008622; Expressed in liver and 6 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: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..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
