C3AR_MACFA
ID C3AR_MACFA Reviewed; 481 AA.
AC Q6TAC8;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=C3a anaphylatoxin chemotactic receptor;
DE Short=C3AR;
DE Short=C3a-R;
GN Name=C3AR1;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Blood;
RA Therien A.G., Gervais F.G.;
RT "Coding region of the anaphylatoxin C3a receptor of Macaca fascicularis.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for the chemotactic and inflammatory peptide
CC anaphylatoxin C3a. This receptor stimulates chemotaxis, granule enzyme
CC release and superoxide anion production (By similarity). {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AY426336; AAR06214.1; -; mRNA.
DR RefSeq; NP_001306304.1; NM_001319375.1.
DR AlphaFoldDB; Q6TAC8; -.
DR SMR; Q6TAC8; -.
DR STRING; 9541.XP_005570092.1; -.
DR GeneID; 102118947; -.
DR CTD; 719; -.
DR eggNOG; ENOG502R35Z; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
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; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
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 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..481
FT /note="C3a anaphylatoxin chemotactic receptor"
FT /id="PRO_0000069203"
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..337
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..357
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 358..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..397
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..414
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 436..481
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 315
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O09047"
FT MOD_RES 460
FT /note="Phosphothreonine"
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 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..172
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 481 AA; 53578 MW; 4C64DCBAB006BA4F CRC64;
MAPFSAETNS TDLLSQPWNE SPVILSMVIL SLTFLLGLPG NGLVLWVAGL KMQRTVNTVW
FLHLTLADLL CCLSLPFSLA HLALQGQWPY GRFLCKLIPS IIVLNMFASV FLLTAITLDR
CLVVFKPIWC QNHRNVGTAC TICGCIWVVA FVMCIPVFVY REIFTTDNHS KCGYKFDLSG
SLDYLDFYGN PLENRSLENI FQLPGEMNDR LDPSSFQAND HPWTVTTAFH TQTFQRPSAD
SLPKDSASHS PYSNVFKPAG VASPKIPSGF PIEGHKTSPL DDSDAFLSTH LKLFPSAASN
SLYEYELPQD FQDYYSLGQF TYDNQVSTPL VAITITRLVV GFLLPSVIMI ACYSFIVLRM
QRGRFAKSQG KTLRVAVVVV TVFLVCWAPY HISGVLSLFT DPETPLGKTL MSWDHVFTAL
ASANSCFNPF LYALLGKDFR KKARQSIQSI LEAAFSEELT HSTHCSSNNV FSERNSISTT
V