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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
 
 
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