C5AR1_RABIT
ID C5AR1_RABIT Reviewed; 350 AA.
AC Q9TUE1;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 105.
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;
DE Flags: Fragment;
GN Name=C5AR1; Synonyms=C5R1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=New Zealand white;
RX PubMed=10510441; DOI=10.1038/sj.bjp.0702812;
RA Bachvarov D.R., Houle S., Bachvarova M., Bouthillier J., St Pierre S.A.,
RA Fukuoka Y., Ember J.A., Marceau F.;
RT "Cloning and preliminary pharmacological characterization of the
RT anaphylatoxin C5a receptor in the rabbit.";
RL Br. J. Pharmacol. 128:321-326(1999).
CC -!- FUNCTION: Receptor for the chemotactic and inflammatory peptide
CC anaphylatoxin C5a (PubMed:10510441). 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:10510441}.
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:10510441};
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; AF068680; AAF13030.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9TUE1; -.
DR SMR; Q9TUE1; -.
DR STRING; 9986.ENSOCUP00000023879; -.
DR eggNOG; ENOG502R35Z; Eukaryota.
DR InParanoid; Q9TUE1; -.
DR Proteomes; UP000001811; 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: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; 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; Glycoprotein; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Sulfation; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN <1..350
FT /note="C5a anaphylatoxin chemotactic receptor 1"
FT /id="PRO_0000069214"
FT TOPO_DOM <1..36
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 37..63
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 64..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 69..92
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 93..109
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 110..131
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 132..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 153..173
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 174..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 MOD_RES 10
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT MOD_RES 13
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 CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 108..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT NON_TER 1
SQ SEQUENCE 350 AA; 38586 MW; C69871B3E20897C2 CRC64;
APMENSTYDY TNYDSLGTLD PSTPVDNTVR RLRPTTIVAL VIYMAVFLVG VPGNALVVWV
TALEAKRTVN AIWFLNLAVA DLLSCLALPI LFVSIIQEGH WPFGRAACSV LPSLILLNMY
ASILLLATIS ADRFLLVFNP IWCQNTRGAG LAWLACCVAW GLALLLTIPS FLYRKVLQDD
YPPKTTCGVD YGHEGVRAER AVAIVRLVVG FLLPLFTLSV CYTFLLLRTW SRNGTRSTKT
LKVVVAVVVS FFIFWLPYQV MGMILALLHP SSATFRWAIR LDPLCIALAY VNCCINPIIY
VVAGKGFQGQ LRKSLPSLLR NVLAEESVIQ GSKSFSRSTV DTVADKCQAV
