C5AR2_RAT
ID C5AR2_RAT Reviewed; 343 AA.
AC Q695P6;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=C5a anaphylatoxin chemotactic receptor 2;
DE AltName: Full=Complement component 5a receptor 2;
DE AltName: Full=G-protein coupled receptor 77;
GN Name=C5ar2; Synonyms=C5l2, Gpr77;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Long Evans;
RA Gao H., Neff T., Younkin E., Hoesel M., Man Y., Sarma V., Guo R.-F.,
RA Tomlins S., Riedemann N., Speyer C., Zetoune F., Ward P.;
RT "Molecular cloning and expression of C5L2, a new C5a orphan receptor in
RT sepsis.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Receptor for the chemotactic and inflammatory C3a, C4a and
CC C5a anaphylatoxin peptides and also for their dearginated forms
CC ASP/C3adesArg, C4adesArg and C5adesArg respectively. Couples weakly to
CC G(i)-mediated signaling pathways.
CC -!- SUBUNIT: Interacts with C3 (the anaphylatoxin peptide C3a and the
CC adipogenic hormone ASP); the interaction occurs with higher affinity
CC for ASP, enhancing the phosphorylation and activation of GPR77,
CC recruitment of ARRB2 to the cell surface and endocytosis of GRP77.
CC {ECO:0000250}.
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; AY600435; AAT12287.1; -; mRNA.
DR RefSeq; NP_001003710.2; NM_001003710.2.
DR RefSeq; XP_006228415.1; XM_006228353.3.
DR AlphaFoldDB; Q695P6; -.
DR SMR; Q695P6; -.
DR STRING; 10116.ENSRNOP00000067721; -.
DR GlyGen; Q695P6; 1 site.
DR iPTMnet; Q695P6; -.
DR PhosphoSitePlus; Q695P6; -.
DR PaxDb; Q695P6; -.
DR Ensembl; ENSRNOT00000102131; ENSRNOP00000081314; ENSRNOG00000049028.
DR GeneID; 445269; -.
DR KEGG; rno:445269; -.
DR CTD; 27202; -.
DR RGD; 1303027; C5ar2.
DR eggNOG; ENOG502R35Z; Eukaryota.
DR GeneTree; ENSGT01020000230336; -.
DR HOGENOM; CLU_009579_8_0_1; -.
DR InParanoid; Q695P6; -.
DR OMA; CHGALLC; -.
DR OrthoDB; 978188at2759; -.
DR PhylomeDB; Q695P6; -.
DR PRO; PR:Q695P6; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000049028; Expressed in liver and 17 other tissues.
DR GO; GO:0045177; C:apical part of cell; ISS:UniProtKB.
DR GO; GO:0009925; C:basal plasma membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; TAS:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004878; F:complement component C5a receptor activity; IBA:GO_Central.
DR GO; GO:0004875; F:complement receptor activity; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR GO; GO:0002430; P:complement receptor mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:RGD.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; ISS:UniProtKB.
DR GO; GO:0090024; P:negative regulation of neutrophil chemotaxis; ISS:UniProtKB.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISS:UniProtKB.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:InterPro.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:InterPro.
DR GO; GO:0032677; P:regulation of interleukin-8 production; ISS:UniProtKB.
DR InterPro; IPR027809; Anaphtx_C5AR2.
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:SF1; PTHR24225:SF1; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..343
FT /note="C5a anaphylatoxin chemotactic receptor 2"
FT /id="PRO_0000303084"
FT TOPO_DOM 1..44
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..67
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..101
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..120
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..143
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..178
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..208
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..231
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..243
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..266
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..280
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..300
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..343
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 113..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 343 AA; 38123 MW; BB3C9C9E517003C0 CRC64;
MLNDTTSKDY EYEYDQEQYS DLLNVPVDCP AGNCFSNDAY LIVLLGLYSV IFLVGVPGNT
LLAWVTWKES RHRLGASWFL HLTMADLLCC VSLPFLAVPI AQKGHWPYGT AGCWLLSSIT
VLSMYASVLL LTGLSGDLFL LAFRPSWKNA DQRTCGVRVV QVSSWMLALL LTVPGAVYRK
LLQEHYPPRL VCGTNYGGSV TAEVTITTVR FLFGFLVPLV FMASCHGILQ RQMARRHWPL
GTAVVVGFFI CWTPFHLLRV IIAVASSHSP LLAWALEAEP LVTGLALAHS ALNPIMFLYF
GRKQLCKSLQ AACHWALRDL QDEEESAVTK VSTSQEMVSE MPV
