C3AR_HUMAN
ID C3AR_HUMAN Reviewed; 482 AA.
AC Q16581; O43771; Q92868;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=C3a anaphylatoxin chemotactic receptor;
DE Short=C3AR;
DE Short=C3a-R;
GN Name=C3AR1; Synonyms=AZ3B, C3R1, HNFAG09;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8605247; DOI=10.1016/0167-4781(95)00209-x;
RA Roglic A., Prossnitz E.R., Cavanagh S.L., Pan Z., Zou A., Ye R.D.;
RT "cDNA cloning of a novel G protein-coupled receptor with a large
RT extracellular loop structure.";
RL Biochim. Biophys. Acta 1305:39-43(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8765043; DOI=10.1002/eji.1830260840;
RA Crass T., Raffetseder U., Martin U., Grove M., Klos A., Koehl J.,
RA Bautsch W.;
RT "Expression cloning of the human C3a anaphylatoxin receptor (C3aR) from
RT differentiated U-937 cells.";
RL Eur. J. Immunol. 26:1944-1950(1996).
RN [3]
RP SEQUENCE REVISION.
RA Bautsch W.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8702752; DOI=10.1074/jbc.271.34.20231;
RA Ames R.S., Li Y., Sarau H.M., Nuthulaganti P., Foley J.J., Ellis C.,
RA Zeng Z., Su K., Jurewicz A.J., Hertzberg R.P., Bergsma D.J., Kumar C.;
RT "Molecular cloning and characterization of the human anaphylatoxin C3a
RT receptor.";
RL J. Biol. Chem. 271:20231-20234(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S.,
RA Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
RT "Genome-wide discovery and analysis of human seven transmembrane helix
RT receptor genes.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kopatz S.A., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-136.
RG SeattleSNPs variation discovery resource;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
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 [9]
RP SULFATION AT TYR-174; TYR-184 AND TYR-318.
RX PubMed=12871936; DOI=10.1074/jbc.m306061200;
RA Gao J., Choe H., Bota D., Wright P.L., Gerard C., Gerard N.P.;
RT "Sulfation of tyrosine 174 in the human C3a receptor is essential for
RT binding of C3a anaphylatoxin.";
RL J. Biol. Chem. 278:37902-37908(2003).
RN [10]
RP GLYCOSYLATION AT SER-266, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23234360; DOI=10.1021/pr300963h;
RA Halim A., Ruetschi U., Larson G., Nilsson J.;
RT "LC-MS/MS characterization of O-glycosylation sites and glycan structures
RT of human cerebrospinal fluid glycoproteins.";
RL J. Proteome Res. 12:573-584(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 (By similarity).
CC {ECO:0000250|UniProtKB:O09047}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Widely expressed in several differentiated
CC hematopoietic cell lines, in the lung, spleen, ovary, placenta, small
CC intestine, throughout the brain, heart, and endothelial cells. Mostly
CC expressed in lymphoid tissues.
CC -!- PTM: Among the sulfation sites Tyr-174 is essential for binding of C3a
CC anaphylatoxin. {ECO:0000269|PubMed:12871936}.
CC -!- PTM: O-glycosylated. {ECO:0000269|PubMed:23234360}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/c3ar1/";
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DR EMBL; U28488; AAC50374.1; -; mRNA.
DR EMBL; Z73157; CAA97504.1; -; mRNA.
DR EMBL; U62027; AAC50657.1; -; mRNA.
DR EMBL; AB065870; BAC06088.1; -; Genomic_DNA.
DR EMBL; AY268431; AAP23198.1; -; Genomic_DNA.
DR EMBL; AY455929; AAR13862.1; -; Genomic_DNA.
DR EMBL; BC020742; AAH20742.1; -; mRNA.
DR CCDS; CCDS8588.1; -.
DR PIR; S65766; S65766.
DR RefSeq; NP_001313404.1; NM_001326475.1.
DR RefSeq; NP_001313406.1; NM_001326477.1.
DR RefSeq; NP_004045.1; NM_004054.3.
DR AlphaFoldDB; Q16581; -.
DR SMR; Q16581; -.
DR BioGRID; 107180; 124.
DR IntAct; Q16581; 91.
DR STRING; 9606.ENSP00000302079; -.
DR BindingDB; Q16581; -.
DR ChEMBL; CHEMBL4761; -.
DR GuidetoPHARMACOLOGY; 31; -.
DR GlyConnect; 811; 1 O-Linked glycan (1 site).
DR GlyGen; Q16581; 5 sites, 2 O-linked glycans (3 sites).
DR iPTMnet; Q16581; -.
DR PhosphoSitePlus; Q16581; -.
DR BioMuta; C3AR1; -.
DR DMDM; 37538305; -.
DR CPTAC; CPTAC-1177; -.
DR jPOST; Q16581; -.
DR MassIVE; Q16581; -.
DR PaxDb; Q16581; -.
DR PeptideAtlas; Q16581; -.
DR PRIDE; Q16581; -.
DR ProteomicsDB; 60928; -.
DR ABCD; Q16581; 16 sequenced antibodies.
DR Antibodypedia; 3999; 550 antibodies from 34 providers.
DR DNASU; 719; -.
DR Ensembl; ENST00000307637.5; ENSP00000302079.4; ENSG00000171860.5.
DR GeneID; 719; -.
DR KEGG; hsa:719; -.
DR MANE-Select; ENST00000307637.5; ENSP00000302079.4; NM_004054.4; NP_004045.1.
DR UCSC; uc001qtv.2; human.
DR CTD; 719; -.
DR DisGeNET; 719; -.
DR GeneCards; C3AR1; -.
DR HGNC; HGNC:1319; C3AR1.
DR HPA; ENSG00000171860; Tissue enhanced (lymphoid).
DR MIM; 605246; gene.
DR neXtProt; NX_Q16581; -.
DR OpenTargets; ENSG00000171860; -.
DR PharmGKB; PA25898; -.
DR VEuPathDB; HostDB:ENSG00000171860; -.
DR eggNOG; ENOG502R35Z; Eukaryota.
DR GeneTree; ENSGT01020000230336; -.
DR HOGENOM; CLU_009579_35_0_1; -.
DR InParanoid; Q16581; -.
DR OMA; WVVAFVM; -.
DR OrthoDB; 1003587at2759; -.
DR PhylomeDB; Q16581; -.
DR TreeFam; TF330976; -.
DR PathwayCommons; Q16581; -.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-9660826; Purinergic signaling in leishmaniasis infection.
DR Reactome; R-HSA-977606; Regulation of Complement cascade.
DR SignaLink; Q16581; -.
DR SIGNOR; Q16581; -.
DR BioGRID-ORCS; 719; 6 hits in 1081 CRISPR screens.
DR ChiTaRS; C3AR1; human.
DR GeneWiki; C3a_receptor; -.
DR GenomeRNAi; 719; -.
DR Pharos; Q16581; Tchem.
DR PRO; PR:Q16581; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q16581; protein.
DR Bgee; ENSG00000171860; Expressed in monocyte and 179 other tissues.
DR ExpressionAtlas; Q16581; baseline and differential.
DR Genevisible; Q16581; HS.
DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0004876; F:complement component C3a receptor activity; IDA:UniProtKB.
DR GO; GO:0004875; F:complement receptor activity; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IPI:UniProtKB.
DR GO; GO:0008015; P:blood circulation; TAS:ProtInc.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0002430; P:complement receptor mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
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; IEA:Ensembl.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IPI:UniProtKB.
DR GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IEA:Ensembl.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IEA:Ensembl.
DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IEA:Ensembl.
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..482
FT /note="C3a anaphylatoxin chemotactic receptor"
FT /id="PRO_0000069202"
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..340
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..360
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..400
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 401..417
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 439..482
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 174
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:12871936"
FT MOD_RES 184
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:12871936"
FT MOD_RES 318
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:12871936"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O09047"
FT MOD_RES 463
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O09047"
FT CARBOHYD 9
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:23234360"
FT DISULFID 95..172
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 136
FT /note="V -> A (in dbSNP:rs11567806)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_019164"
FT CONFLICT 151
FT /note="F -> C (in Ref. 4; AAC50657)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="P -> R (in Ref. 1; AAC50374)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 482 AA; 53864 MW; 287E219D98CED203 CRC64;
MASFSAETNS TDLLSQPWNE PPVILSMVIL SLTFLLGLPG NGLVLWVAGL KMQRTVNTIW
FLHLTLADLL CCLSLPFSLA HLALQGQWPY GRFLCKLIPS IIVLNMFASV FLLTAISLDR
CLVVFKPIWC QNHRNVGMAC SICGCIWVVA FVMCIPVFVY REIFTTDNHN RCGYKFGLSS
SLDYPDFYGD PLENRSLENI VQPPGEMNDR LDPSSFQTND HPWTVPTVFQ PQTFQRPSAD
SLPRGSARLT SQNLYSNVFK PADVVSPKIP SGFPIEDHET SPLDNSDAFL STHLKLFPSA
SSNSFYESEL PQGFQDYYNL GQFTDDDQVP TPLVAITITR LVVGFLLPSV IMIACYSFIV
FRMQRGRFAK SQSKTFRVAV VVVAVFLVCW TPYHIFGVLS LLTDPETPLG KTLMSWDHVC
IALASANSCF NPFLYALLGK DFRKKARQSI QGILEAAFSE ELTRSTHCPS NNVISERNST
TV
