C3AR_CAVPO
ID C3AR_CAVPO Reviewed; 475 AA.
AC O88680; Q9QWG9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=C3a anaphylatoxin chemotactic receptor;
DE Short=C3AR;
DE Short=C3a-R;
GN Name=C3AR1;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=9725198;
RA Lienenklaus S., Ames R.S., Tornetta M.A., Sarau H.M., Foley J.J., Crass T.,
RA Sohns B., Raffetseder U., Grove M., Hoelzer A., Klos A., Koehl J.,
RA Bautsch W.;
RT "Human anaphylatoxin C4a is a potent agonist of the guinea pig but not the
RT human C3a receptor.";
RL J. Immunol. 161:2089-2093(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC STRAIN=Hartley; TISSUE=Spleen;
RX PubMed=9743361;
RA Fukuoka Y., Ember J.A., Hugli T.E.;
RT "Molecular cloning of two isoforms of the guinea pig C3a anaphylatoxin
RT receptor: alternative splicing in the large extracellular loop.";
RL J. Immunol. 161:2977-2984(1998).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=gpC3aR-L;
CC IsoId=O88680-1; Sequence=Displayed;
CC Name=2; Synonyms=gpC3aR-S;
CC IsoId=O88680-2; Sequence=VSP_010628;
CC -!- TISSUE SPECIFICITY: Expressed in the heart, kidney, lung, liver,
CC peritoneal macrophages and spleen. {ECO:0000269|PubMed:9743361}.
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; AJ006402; CAA07002.1; -; Genomic_DNA.
DR EMBL; U86378; AAC36503.1; -; mRNA.
DR RefSeq; NP_001166589.1; NM_001173118.1.
DR AlphaFoldDB; O88680; -.
DR SMR; O88680; -.
DR STRING; 10141.ENSCPOP00000019559; -.
DR Ensembl; ENSCPOT00000009625; ENSCPOP00000019559; ENSCPOG00000026687. [O88680-1]
DR GeneID; 100379246; -.
DR KEGG; cpoc:100379246; -.
DR CTD; 719; -.
DR eggNOG; ENOG502R35Z; Eukaryota.
DR GeneTree; ENSGT01020000230336; -.
DR HOGENOM; CLU_009579_35_0_1; -.
DR InParanoid; O88680; -.
DR OMA; WVVAFVM; -.
DR OrthoDB; 1003587at2759; -.
DR TreeFam; TF330976; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000026687; Expressed in liver and 12 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004876; F:complement component C3a receptor activity; IDA: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:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Chemotaxis; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Sulfation; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..475
FT /note="C3a anaphylatoxin chemotactic receptor"
FT /id="PRO_0000069201"
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..331
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..351
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 352..368
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..391
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..408
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 430..475
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 174
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 183
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O09047"
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 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..172
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 254..288
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9743361"
FT /id="VSP_010628"
FT CONFLICT 2
FT /note="E -> D (in Ref. 2; AAC36503)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="V -> A (in Ref. 2; AAC36503)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 475 AA; 53570 MW; 0D6FFF5627A53330 CRC64;
MESSSAETNS TGLHLEPQYQ PETILAMAIL GLTFVLGLPG NGLVLWVAGL KMRRTVNTVW
FLHLTVADFV CCLSLPFSMA HLALRGYWPY GEILCKFIPT VIIFNMFASV FLLTAISLDR
CLMVLKPIWC QNHRNVRTAC IICGCIWLVA FVLCIPVFVY RETFTLENHT ICTYNFSPGS
FDYLDYAYDR DAWGYGTPDP IVQLPGEMEH RSDPSSFQTQ DGPWSVTTTL YSQTSQRPSE
DSFHMDSAKL SGQGKYVDVV LPTNLCGLPM EENRTNTLHN AAFLSSDLDV SNATQKCLST
PEPPQDFWDD LSPFTHEYRT PRLLKVITFT RLVVGFLLPM IIMVACYTLI IFRMRRVRVV
KSWNKALHLA MVVVTIFLIC WAPYHVFGVL ILFINPESRV GAALLSWDHV SIALASANSC
FNPFLYALLG RDLRKRVRQS MKGILEAAFS EDISKSTSFI QAKAFSEKHS LSTNV
