C3AR_MOUSE
ID C3AR_MOUSE Reviewed; 477 AA.
AC O09047; O35951;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=C3a anaphylatoxin chemotactic receptor;
DE Short=C3AR;
DE Short=C3a-R;
DE AltName: Full=Complement component 3a receptor 1;
GN Name=C3ar1; Synonyms=C3r1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=129/SvJ, and C57BL/6J; TISSUE=Brain;
RX PubMed=9164946;
RA Tornetta M.A., Foley J.J., Sarau H.M., Ames R.S.;
RT "The mouse anaphylatoxin C3a receptor: molecular cloning, genomic
RT organization, and functional expression.";
RL J. Immunol. 158:5277-5282(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=9382922; DOI=10.1007/s002510050327;
RA Hsu M.H., Ember J.A., Wang M., Prossnitz E.R., Hugli T.E., Ye R.D.;
RT "Cloning and functional characterization of the mouse C3a anaphylatoxin
RT receptor gene.";
RL Immunogenetics 47:64-72(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=9694514; DOI=10.1016/s0161-5890(98)00021-2;
RA Hollmann T.J., Haviland D.L., Kildsgaard J., Watts K., Wetsel R.A.;
RT "Cloning, expression, sequence determination, and chromosome localization
RT of the mouse complement C3a anaphylatoxin receptor gene.";
RL Mol. Immunol. 35:137-148(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452 AND THR-456, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP INTERACTION WITH VGF.
RX PubMed=25456411; DOI=10.1016/j.str.2014.10.001;
RA Cero C., Vostrikov V.V., Verardi R., Severini C., Gopinath T., Braun P.D.,
RA Sassano M.F., Gurney A., Roth B.L., Vulchanova L., Possenti R., Veglia G.,
RA Bartolomucci A.;
RT "The TLQP-21 peptide activates the G-protein-coupled receptor C3aR1 via a
RT folding-upon-binding mechanism.";
RL Structure 22:1744-1753(2014).
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:25456411}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Detected in varying levels in all tissues examined
CC except the spleen. Especially abundant in heart and lung.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U77461; AAC53204.1; -; Genomic_DNA.
DR EMBL; U77460; AAC53203.1; -; mRNA.
DR EMBL; U97537; AAB71814.1; -; Genomic_DNA.
DR EMBL; AF053757; AAC40193.1; -; Genomic_DNA.
DR EMBL; BC003728; AAH03728.1; -; mRNA.
DR CCDS; CCDS20504.1; -.
DR RefSeq; NP_033909.1; NM_009779.2.
DR AlphaFoldDB; O09047; -.
DR SMR; O09047; -.
DR STRING; 10090.ENSMUSP00000048092; -.
DR GlyGen; O09047; 4 sites.
DR iPTMnet; O09047; -.
DR PhosphoSitePlus; O09047; -.
DR jPOST; O09047; -.
DR PaxDb; O09047; -.
DR PRIDE; O09047; -.
DR ProteomicsDB; 281715; -.
DR Antibodypedia; 3999; 550 antibodies from 34 providers.
DR DNASU; 12267; -.
DR Ensembl; ENSMUST00000042081; ENSMUSP00000048092; ENSMUSG00000040552.
DR GeneID; 12267; -.
DR KEGG; mmu:12267; -.
DR UCSC; uc009dps.1; mouse.
DR CTD; 719; -.
DR MGI; MGI:1097680; C3ar1.
DR VEuPathDB; HostDB:ENSMUSG00000040552; -.
DR eggNOG; ENOG502R35Z; Eukaryota.
DR GeneTree; ENSGT01020000230336; -.
DR HOGENOM; CLU_009579_35_0_1; -.
DR InParanoid; O09047; -.
DR OMA; WVVAFVM; -.
DR OrthoDB; 1003587at2759; -.
DR PhylomeDB; O09047; -.
DR TreeFam; TF330976; -.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-977606; Regulation of Complement cascade.
DR BioGRID-ORCS; 12267; 3 hits in 74 CRISPR screens.
DR PRO; PR:O09047; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; O09047; protein.
DR Bgee; ENSMUSG00000040552; Expressed in stroma of bone marrow and 137 other tissues.
DR ExpressionAtlas; O09047; baseline and differential.
DR Genevisible; O09047; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001850; F:complement component C3a binding; ISO:MGI.
DR GO; GO:0004876; F:complement component C3a receptor activity; ISO:MGI.
DR GO; GO:0004875; F:complement receptor activity; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISO:MGI.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0002430; P:complement receptor mediated signaling pathway; ISO:MGI.
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; IMP:BHF-UCL.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; ISO:MGI.
DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; ISO:MGI.
DR GO; GO:0072126; P:positive regulation of glomerular mesangial cell proliferation; ISO:MGI.
DR GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IMP:BHF-UCL.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IMP:BHF-UCL.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IMP:BHF-UCL.
DR GO; GO:0008217; P:regulation of blood pressure; ISO:MGI.
DR GO; GO:0002462; P:tolerance induction to nonself antigen; ISO:MGI.
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..477
FT /note="C3a anaphylatoxin chemotactic receptor"
FT /id="PRO_0000069204"
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..333
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..353
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 354..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..393
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 394..410
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..431
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 432..477
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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 312
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 456
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 9
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
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"
FT CONFLICT 173
FT /note="R -> K (in Ref. 2; AAB71814)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="E -> K (in Ref. 2; AAB71814)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="D -> N (in Ref. 2; AAB71814)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="D -> N (in Ref. 2; AAB71814)"
FT /evidence="ECO:0000305"
FT CONFLICT 380..382
FT /note="FIC -> LS (in Ref. 2; AAB71814)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="V -> I (in Ref. 2; AAB71814)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="N -> S (in Ref. 2; AAB71814)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 477 AA; 53576 MW; 9873F464A1520984 CRC64;
MESFDADTNS TDLHSRPLFQ PQDIASMVIL GLTCLLGLLG NGLVLWVAGV KMKTTVNTVW
FLHLTLADFL CCLSLPFSLA HLILQGHWPY GLFLCKLIPS IIILNMFASV FLLTAISLDR
CLIVHKPIWC QNHRNVRTAF AICGCVWVVA FVMCVPVFVY RDLFIMDNRS ICRYNFDSSR
SYDYWDYVYK LSLPESNSTD NSTAQLTGHM NDRSAPSSVQ ARDYFWTVTT ALQSQPFLTS
PEDSFSLDSA NQQPHYGGKP PNVLTAAVPS GFPVEDRKSN TLNADAFLSA HTELFPTASS
GHLYPYDFQG DYVDQFTYDN HVPTPLMAIT ITRLVVGFLV PFFIMVICYS LIVFRMRKTN
FTKSRNKTFR VAVAVVTVFF ICWTPYHLVG VLLLITDPES SLGEAVMSWD HMSIALASAN
SCFNPFLYAL LGKDFRKKAR QSIKGILEAA FSEELTHSTN CTQDKASSKR NNMSTDV
