ID   C3AR_ONCMY              Reviewed;         364 AA.
AC   Q2WED0;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=C3a anaphylatoxin chemotactic receptor;
DE            Short=C3AR;
DE            Short=C3a-R;
GN   Name=c3ar1;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Wang T., Secombes C.J.;
RT   "Sequence analysis of rainbow trout (Oncorhynchus mykiss) genes modulated
RT   by bacterial infection.";
RL   Submitted (DEC-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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC   -!- CAUTION: Lacks an insertion found in the C3ar family. It remains
CC       uncertain whether it belongs to the C3ar or the C5ar family.
CC       {ECO:0000305}.
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; AJ616902; CAE83615.1; -; mRNA.
DR   RefSeq; NP_001117875.1; NM_001124403.1.
DR   AlphaFoldDB; Q2WED0; -.
DR   SMR; Q2WED0; -.
DR   PRIDE; Q2WED0; -.
DR   Ensembl; ENSOMYT00000079038; ENSOMYP00000072576; ENSOMYG00000033575.
DR   GeneID; 100136104; -.
DR   KEGG; omy:100136104; -.
DR   CTD; 719; -.
DR   GeneTree; ENSGT01020000230336; -.
DR   OrthoDB; 1003587at2759; -.
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; IPR000826; Formyl_rcpt-rel.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR24225; PTHR24225; 2.
DR   PANTHER; PTHR24225:SF28; PTHR24225:SF28; 2.
DR   Pfam; PF00001; 7tm_1; 1.
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; Receptor; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..364
FT                   /note="C3a anaphylatoxin chemotactic receptor"
FT                   /id="PRO_0000343794"
FT   TOPO_DOM        1..50
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        51..71
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        72..82
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..103
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        104..120
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        121..141
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        142..159
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        160..180
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        181..220
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        221..241
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        242..256
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        257..277
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        278..295
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        296..316
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        317..364
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        13
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        34
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        119..198
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   364 AA;  40960 MW;  F6ADB60F0FAAD0AD CRC64;
     MGDNMDFSEH YGNFSENYVT ESYGEFDLYY DPLNETSLSE QGHRSIWVLS IVLCSIACVL
     GITGNAFVIW IAGVKMKRTV NTIWFVNLAA ADLLCCVSIP FSIADIILNS HWPYGEAMCK
     ILPSMVVLNM FASVFTLVLI SLDRFALVIL PVWAQNHRSI TLAWLLCGLV WVLGLLLSLP
     SMIYREIVVH DDMNITLCIY NHLQDKTEGN QSAIKAIHVT RLILGFLIPL LVIAVCYLLI
     GRRVSSGRFK SQRAFQIILV VVTTFFVCWL PYHVIGLVIE YGKEASQVMA RALDPLAISL
     AYVNSCLNPV LYVFMGQDFK ERVRVSLRKI FEKVFSEDVT LRSSVYSKGQ SQLSRATNSS
     EAQV