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C5AR1_DANRE
ID   C5AR1_DANRE             Reviewed;         346 AA.
AC   P0C7U5;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=C5a anaphylatoxin chemotactic receptor 1;
DE   AltName: Full=C5a anaphylatoxin chemotactic receptor;
DE            Short=C5a-R;
DE            Short=C5aR;
GN   Name=c5ar1;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
CC   -!- FUNCTION: Receptor for the chemotactic and inflammatory peptide
CC       anaphylatoxin C5a. This receptor stimulates chemotaxis, granule enzyme
CC       release and superoxide anion production.
CC       {ECO:0000250|UniProtKB:Q6UNA4}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P21730};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:P21730}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; CAAK04023738; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005159331.1; XM_005159274.3.
DR   AlphaFoldDB; P0C7U5; -.
DR   SMR; P0C7U5; -.
DR   STRING; 7955.ENSDARP00000059000; -.
DR   PaxDb; P0C7U5; -.
DR   Ensembl; ENSDART00000059001; ENSDARP00000059000; ENSDARG00000040319.
DR   GeneID; 100000959; -.
DR   KEGG; dre:100000959; -.
DR   CTD; 728; -.
DR   eggNOG; ENOG502R35Z; Eukaryota.
DR   GeneTree; ENSGT01020000230336; -.
DR   HOGENOM; CLU_009579_8_0_1; -.
DR   InParanoid; P0C7U5; -.
DR   OMA; YTFLLIR; -.
DR   OrthoDB; 978188at2759; -.
DR   PhylomeDB; P0C7U5; -.
DR   TreeFam; TF330976; -.
DR   Reactome; R-DRE-375276; Peptide ligand-binding receptors.
DR   Reactome; R-DRE-418594; G alpha (i) signalling events.
DR   Reactome; R-DRE-6798695; Neutrophil degranulation.
DR   Reactome; R-DRE-977606; Regulation of Complement cascade.
DR   PRO; PR:P0C7U5; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 18.
DR   Bgee; ENSDARG00000040319; Expressed in granulocyte and 10 other tissues.
DR   GO; GO:0045177; C:apical part of cell; ISS:UniProtKB.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004878; F:complement component C5a receptor activity; ISS:UniProtKB.
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:UniProtKB-KW.
DR   GO; GO:0002430; P:complement receptor mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR   GO; GO:0042789; P:mRNA transcription by RNA polymerase II; 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; ISS:UniProtKB.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR   InterPro; IPR000826; Formyl_rcpt-rel.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR24225; PTHR24225; 1.
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   3: Inferred from homology;
KW   Cell membrane; Chemotaxis; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..346
FT                   /note="C5a anaphylatoxin chemotactic receptor 1"
FT                   /id="PRO_0000343795"
FT   TOPO_DOM        1..33
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        34..60
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250|UniProtKB:P21730"
FT   TOPO_DOM        61..65
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        66..89
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250|UniProtKB:P21730"
FT   TOPO_DOM        90..106
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        107..128
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250|UniProtKB:P21730"
FT   TOPO_DOM        129..149
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        150..170
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250|UniProtKB:P21730"
FT   TOPO_DOM        171..194
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        195..220
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250|UniProtKB:P21730"
FT   TOPO_DOM        221..238
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        239..261
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250|UniProtKB:P21730"
FT   TOPO_DOM        262..279
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        280..300
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250|UniProtKB:P21730"
FT   TOPO_DOM        301..346
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          323..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        324..339
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        4
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        15
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        105..183
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   346 AA;  39115 MW;  832164A475DCA5AA CRC64;
     MDDNNSDWTS YDFGNDTIPS PNEISLSHIG TRHWITLVCY GIVFLLGVPG NALVVWVTGF
     RMPNSVNAQW FLNLAIADLL CCLSLPILMV PLAQDQHWPF GALACKLFSG IFYMMMYCSV
     LLLVVISLDR FLLVTKPVWC QNNRQPRQAR ILCFIIWILG LLGSSPYFAH MEIQHHSETK
     TVCTGSYSSL GHAWAITIIR SFLFFLLPFL IICISHWKVY HMTSSGRRQR DKSSRTLRVI
     LALVLGFFLC WTPLHIVDLL ILVSDQPSER FEVNLNLAHV LTLCLAYINS CLNPLLYVCL
     GRGFKENLIS SLRSVLHFAS EAPTHGPSMT TNSKSTTDGV FREKPV
 
 
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