C5AR1_RAT
ID C5AR1_RAT Reviewed; 352 AA.
AC P97520; O09088;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 154.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=Sprague-Dawley;
RX PubMed=9464523; DOI=10.1016/s0161-5890(97)00104-1;
RA Rothermel E., Zwirner J., Vogt T., Rabini S., Goetze O.;
RT "Molecular cloning and expression of the functional rat C5a receptor.";
RL Mol. Immunol. 34:877-886(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Lung;
RX PubMed=9272704; DOI=10.1111/j.1348-0421.1997.tb01894.x;
RA Akatsu H., Miwa T., Sakurada C., Fukuoka Y., Ember J., Yamamoto T.,
RA Hugli T.E., Okada H.;
RT "cDNA cloning and characterization of rat C5a anaphylatoxin receptor.";
RL Microbiol. Immunol. 41:575-580(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH ARRB1 AND ARRB2, AND SUBCELLULAR LOCATION.
RX PubMed=12464600; DOI=10.1074/jbc.m210120200;
RA Braun L., Christophe T., Boulay F.;
RT "Phosphorylation of key serine residues is required for internalization of
RT the complement 5a (C5a) anaphylatoxin receptor via a beta-arrestin,
RT dynamin, and clathrin-dependent pathway.";
RL J. Biol. Chem. 278:4277-4285(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326; SER-329 AND SER-334, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Receptor for the chemotactic and inflammatory peptide
CC anaphylatoxin C5a (PubMed:9464523). 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:9464523}.
CC -!- SUBUNIT: Homodimer. May also form higher-order oligomers (By
CC similarity). Interacts (when phosphorylated) with ARRB1 and ARRB2; the
CC interaction is associated with internalization of C5aR
CC (PubMed:12464600). {ECO:0000250|UniProtKB:P21730,
CC ECO:0000269|PubMed:12464600}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12464600,
CC ECO:0000269|PubMed:9464523}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P21730}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:12464600}. Note=Phosphorylated C5aR colocalizes
CC with ARRB1 and ARRB2 in cytoplasmic vesicles.
CC {ECO:0000269|PubMed:12464600}.
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 the ligand. {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; Y09613; CAA70825.1; -; mRNA.
DR EMBL; AB003042; BAA20263.1; -; mRNA.
DR EMBL; BC078770; AAH78770.1; -; mRNA.
DR RefSeq; NP_446071.1; NM_053619.1.
DR AlphaFoldDB; P97520; -.
DR SMR; P97520; -.
DR STRING; 10116.ENSRNOP00000064558; -.
DR BindingDB; P97520; -.
DR ChEMBL; CHEMBL5770; -.
DR GlyGen; P97520; 1 site.
DR iPTMnet; P97520; -.
DR PhosphoSitePlus; P97520; -.
DR PaxDb; P97520; -.
DR GeneID; 113959; -.
DR KEGG; rno:113959; -.
DR CTD; 728; -.
DR RGD; 70553; C5ar1.
DR eggNOG; ENOG502R35Z; Eukaryota.
DR HOGENOM; CLU_009579_8_0_1; -.
DR InParanoid; P97520; -.
DR OMA; YTFLLIR; -.
DR OrthoDB; 978188at2759; -.
DR PhylomeDB; P97520; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:P97520; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000047800; Expressed in lung and 19 other tissues.
DR Genevisible; P97520; RN.
DR GO; GO:0045177; C:apical part of cell; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0001856; F:complement component C5a binding; IDA:RGD.
DR GO; GO:0004878; F:complement component C5a receptor activity; IDA:RGD.
DR GO; GO:0004875; F:complement receptor activity; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISO:RGD.
DR GO; GO:0097242; P:amyloid-beta clearance; ISO:RGD.
DR GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR GO; GO:0006915; P:apoptotic process; IMP:RGD.
DR GO; GO:0048143; P:astrocyte activation; ISO:RGD.
DR GO; GO:0021534; P:cell proliferation in hindbrain; IMP:RGD.
DR GO; GO:0050890; P:cognition; ISO:RGD.
DR GO; GO:0038178; P:complement component C5a signaling pathway; ISO:RGD.
DR GO; GO:0002430; P:complement receptor mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; IEP:RGD.
DR GO; GO:0001774; P:microglial cell activation; ISO:RGD.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:RGD.
DR GO; GO:0030593; P:neutrophil chemotaxis; ISO:RGD.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:RGD.
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 GO; GO:0010759; P:positive regulation of macrophage chemotaxis; ISO:RGD.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; ISO:RGD.
DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISO:RGD.
DR GO; GO:0099172; P:presynapse organization; ISO:RGD.
DR GO; GO:1902947; P:regulation of tau-protein kinase activity; ISO:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0032494; P:response to peptidoglycan; ISO:RGD.
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 1: Evidence at protein 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..352
FT /note="C5a anaphylatoxin chemotactic receptor 1"
FT /id="PRO_0000069215"
FT TOPO_DOM 1..38
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 39..65
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 66..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 71..94
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 95..111
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 112..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 134..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 155..175
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 176..202
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 203..228
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 229..244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 245..267
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 268..284
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 285..305
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 306..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT MOD_RES 15
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 110..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 352 AA; 39417 MW; 30878580C12650DB CRC64;
MDPISNDSSE ITYDYSDGTP NPDMPADGVY IPKMEPGDIA ALIIYLAVFL VGVTGNALVV
WVTAFEAKRT VNAIWFLNLA VADLLSCLAL PILFTSIVKH NHWPFGDQAC IVLPSLILLN
MYSSILLLAT ISADRFLLVF KPIWCQKFRR PGLAWMACGV TWVLALLLTI PSFVFRRIHK
DPYSDSILCN IDYSKGPFFI EKAIAILRLM VGFVLPLLTL NICYTFLLIR TWSRKATRST
KTLKVVMAVV TCFFVFWLPY QVTGVILAWL PRSSSTFQSV ERLNSLCVSL AYINCCVNPI
IYVMAGQGFH GRLRRSLPSI IRNVLSEDSL GRDSKSFTRS TMDTSTQKSQ AV
