ID I3NHI2_ICTTR Unreviewed; 484 AA.
AC I3NHI2;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=C3a anaphylatoxin chemotactic receptor {ECO:0000256|ARBA:ARBA00022343};
GN Name=C3AR1 {ECO:0000313|Ensembl:ENSSTOP00000023829.1};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000023829.1, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000023829.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 {ECO:0000256|ARBA:ARBA00025640}.
CC -!- SUBUNIT: Interacts with VGF-derived peptide TLQP-21.
CC {ECO:0000256|ARBA:ARBA00025827}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000256|RuleBase:RU000688}.
CC -!- SIMILARITY: Belongs to the chemokine-like receptor (CMKLR) family.
CC {ECO:0000256|ARBA:ARBA00025736}.
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DR EMBL; AGTP01115667; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005341779.1; XM_005341722.1.
DR AlphaFoldDB; I3NHI2; -.
DR STRING; 43179.ENSSTOP00000023829; -.
DR Ensembl; ENSSTOT00000027411.1; ENSSTOP00000023829.1; ENSSTOG00000023824.1.
DR GeneID; 101967646; -.
DR CTD; 719; -.
DR eggNOG; ENOG502R35Z; Eukaryota.
DR GeneTree; ENSGT01100000263564; -.
DR HOGENOM; CLU_009579_35_0_1; -.
DR InParanoid; I3NHI2; -.
DR OMA; MKPVWCQ; -.
DR OrthoDB; 5356571at2759; -.
DR TreeFam; TF330976; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004876; F:complement component C3a receptor activity; IEA:Ensembl.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0019722; P:calcium-mediated signaling; IEA:Ensembl.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR GO; GO:0045766; P:positive regulation of angiogenesis; 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 Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 2.
DR InterPro; IPR001644; Anaphtx_C3AR1.
DR InterPro; IPR002234; Anphylx_rcpt_C3a/C5a1-2.
DR InterPro; IPR000826; Formyl_rcpt-rel.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24225:SF28; C3A ANAPHYLATOXIN CHEMOTACTIC RECEPTOR; 1.
DR PANTHER; PTHR24225; CHEMOTACTIC RECEPTOR; 1.
DR Pfam; PF00001; 7tm_1; 2.
DR PRINTS; PR01104; ANPHYLATOXNR.
DR PRINTS; PR01060; C3ANPHYLTXNR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 3: Inferred from homology;
KW G-protein coupled receptor {ECO:0000256|RuleBase:RU000688};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000688};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Transducer {ECO:0000256|RuleBase:RU000688};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000688};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 23..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 139..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 382..404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 419..438
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..435
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
SQ SEQUENCE 484 AA; 54915 MW; CB28BF89D8ADABE1 CRC64;
MESFSAETNS TDPLSQPLYE PQIILSMVIL GLTFLLGLPG NGLVLWVAGL KMQRTVNTVW
FLHLTLADFL CCLSLPFSLA HLALHGYWPY GRFLCKLIPS IIILNMFASV FLLTAISVDR
CLMVLRPIWC QNHRRVRTAF AICGCIWMMS FAMCIPVFMY RETFTVDDYK MCIYNFGFTS
SDYSDYTYDP DELENGSFTN SIVQQPGKMD DKLNFSSFQA NNYPWTAPTI LQSQTLGRHS
GDLIPGESTR LSRRYPSYNN FKPPNISSAS PSGFLTEDHK TDVLHNPNNL LPTDLDLYPR
AYSDNFYEPE QSQDFQDYNL SQFPGDSQVQ KTMMIITITR LVLGFLLPFI IIVCCYSIIV
FRMRRSQLTK SRNKTFRVTM MVVTVFLVCW TPYHIIGVLL LVISPGSSLR GTLLSWDNVA
LALASANSCF NPFLYALLGK DFRKKAKQSV KGILEAAFSE ELTHSTSCFQ NKVFTERNSI
STGV
//
