C3AR_RAT
ID C3AR_RAT Reviewed; 473 AA.
AC O55197;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=C3a anaphylatoxin chemotactic receptor;
DE Short=C3AR;
DE Short=C3a-R;
GN Name=C3ar1;
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].
RC STRAIN=Wistar; TISSUE=Lung;
RX PubMed=9464274; DOI=10.1006/bbrc.1997.8034;
RA Fukuoka Y., Ember J.A., Hugli T.E.;
RT "Cloning and characterization of rat C3a receptor: differential expression
RT of rat C3a and C5a receptors by LPS stimulation.";
RL Biochem. Biophys. Res. Commun. 242:663-668(1998).
RN [2]
RP INTERACTION WITH VGF.
RX PubMed=23940034; DOI=10.1074/jbc.m113.497214;
RA Hannedouche S., Beck V., Leighton-Davies J., Beibel M., Roma G.,
RA Oakeley E.J., Lannoy V., Bernard J., Hamon J., Barbieri S., Preuss I.,
RA Lasbennes M.C., Sailer A.W., Suply T., Seuwen K., Parker C.N.,
RA Bassilana F.;
RT "Identification of the C3a receptor (C3AR1) as the target of the VGF-
RT derived peptide TLQP-21 in rodent cells.";
RL J. Biol. Chem. 288:27434-27443(2013).
CC -!- FUNCTION: Receptor for the chemotactic and inflammatory peptide
CC anaphylatoxin C3a. This receptor stimulates chemotaxis, granule enzyme
CC release and superoxide anion production.
CC -!- SUBUNIT: Interacts with VGF-derived peptide TLQP-21.
CC {ECO:0000269|PubMed:23940034}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U86379; AAC40071.1; -; mRNA.
DR PIR; JC5835; JC5835.
DR RefSeq; NP_114449.1; NM_032060.1.
DR AlphaFoldDB; O55197; -.
DR SMR; O55197; -.
DR STRING; 10116.ENSRNOP00000012216; -.
DR GlyGen; O55197; 2 sites.
DR PhosphoSitePlus; O55197; -.
DR PaxDb; O55197; -.
DR GeneID; 84007; -.
DR KEGG; rno:84007; -.
DR UCSC; RGD:620537; rat.
DR CTD; 719; -.
DR RGD; 620537; C3ar1.
DR eggNOG; ENOG502R35Z; Eukaryota.
DR InParanoid; O55197; -.
DR OrthoDB; 1003587at2759; -.
DR PhylomeDB; O55197; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-977606; Regulation of Complement cascade.
DR PRO; PR:O55197; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0001850; F:complement component C3a binding; IDA:RGD.
DR GO; GO:0004876; F:complement component C3a 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:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0002430; P:complement receptor mediated signaling pathway; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
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:0030335; P:positive regulation of cell migration; IMP:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:RGD.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; ISO:RGD.
DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IMP:RGD.
DR GO; GO:0072126; P:positive regulation of glomerular mesangial cell proliferation; IMP:RGD.
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:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISO:RGD.
DR GO; GO:0008217; P:regulation of blood pressure; IDA:RGD.
DR GO; GO:0002462; P:tolerance induction to nonself antigen; IMP:RGD.
DR InterPro; IPR001644; Anaphtx_C3AR1.
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; 2.
DR PRINTS; PR01104; ANPHYLATOXNR.
DR PRINTS; PR01060; C3ANPHYLTXNR.
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; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Phosphoprotein; Receptor; Reference proteome;
KW Sulfation; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..473
FT /note="C3a anaphylatoxin chemotactic receptor"
FT /id="PRO_0000069205"
FT TOPO_DOM 1..23
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..46
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..57
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..80
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..96
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..118
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..329
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..349
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..389
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 390..406
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..473
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 233..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 174
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 184
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 308
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O09047"
FT MOD_RES 452
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O09047"
FT CARBOHYD 9
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..172
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 473 AA; 52896 MW; 722F16F6F4B16451 CRC64;
MESFTADTNS TDLHSRPLFK PQDIASMVIL SLTCLLGLPG NGLVLWVAGV KMKRTVNTVW
FLHLTLADFL CCLSLPFSVA HLILRGHWPY GLFLCKLIPS VIILNMFASV FLLTAISLDR
CLMVHKPIWC QNHRSVRTAF AVCGCVWVVT FVMCIPVFVY RDLLVVDDYS VCGYNFDSSR
AYDYWDYMYN SHLPEINPPD NSTGHVDDRT APSSSVPARD LWTATTALQS QTFHTSPEDP
FSQDSASQQP HYGGKPPTVL IATIPGGFPV EDHKSNTLNT GAFLSAHTEP SLTASSSPLY
AHDFPDDYFD QLMYGNHAWT PQVAITISRL VVGFLVPFFI MITCYSLIVF RMRKTNLTKS
RNKTLRVAVA VVTVFFVCWI PYHIVGILLV ITDQESALRE VVLPWDHMSI ALASANSCFN
PFLYALLGKD FRKKARQSVK GILEAAFSEE LTHSTSCTQD KAPSKRNHMS TDV
