C5AR1_ONCMY
ID C5AR1_ONCMY Reviewed; 350 AA.
AC Q6UNA4; Q6T3R0;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 75.
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 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 [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Head, and Kidney;
RX PubMed=14628104; DOI=10.1007/s00251-003-0623-4;
RA Fujiki K., Liu L., Sundick R.S., Dixon B.;
RT "Molecular cloning and characterization of rainbow trout (Oncorhynchus
RT mykiss) C5a anaphylatoxin receptor.";
RL Immunogenetics 55:640-646(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-346, FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=15034053; DOI=10.4049/jimmunol.172.7.4381;
RA Boshra H., Li J., Peters R., Hansen J., Matlapudi A., Sunyer J.O.;
RT "Cloning, expression, cellular distribution, and role in chemotaxis of a
RT C5a receptor in rainbow trout: the first identification of a C5a receptor
RT in a nonmammalian species.";
RL J. Immunol. 172:4381-4390(2004).
CC -!- FUNCTION: Receptor for the chemotactic and inflammatory peptide
CC anaphylatoxin C5a. This receptor stimulates chemotaxis, granule enzyme
CC release and superoxide anion production. {ECO:0000269|PubMed:15034053}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14628104};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P21730}.
CC -!- TISSUE SPECIFICITY: High expression in head, kidney and posterior
CC kidney, lower levels in peripheral blood leukocytes and spleen, low
CC expression in brain and gills, heart, intestine and very low expression
CC in liver and muscle. {ECO:0000269|PubMed:14628104,
CC ECO:0000269|PubMed:15034053}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AY366353; AAR12187.1; -; mRNA.
DR EMBL; AY366354; AAR12188.1; -; Genomic_DNA.
DR EMBL; AY438032; AAR97322.1; -; mRNA.
DR RefSeq; NP_001117939.1; NM_001124467.2.
DR AlphaFoldDB; Q6UNA4; -.
DR SMR; Q6UNA4; -.
DR GeneID; 100136191; -.
DR KEGG; omy:100136191; -.
DR CTD; 100136191; -.
DR OrthoDB; 978188at2759; -.
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:0001856; F:complement component C5a binding; IPI:AgBase.
DR GO; GO:0004878; F:complement component C5a receptor activity; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISS:UniProtKB.
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 GO; GO:0071624; P:positive regulation of granulocyte chemotaxis; IDA:AgBase.
DR GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; IMP:AgBase.
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 SMART; SM01381; 7TM_GPCR_Srsx; 1.
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..350
FT /note="C5a anaphylatoxin chemotactic receptor 1"
FT /id="PRO_0000343796"
FT TOPO_DOM 1..37
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 38..64
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 65..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 70..93
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 94..110
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 111..132
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 133..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 155..174
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 175..197
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 198..223
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 224..247
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 248..270
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 271..287
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 288..308
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 309..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 17
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 109..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 286
FT /note="A -> V (in Ref. 2; AAR97322)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 350 AA; 39323 MW; 949F76B24CB597F1 CRC64;
MDDMCSILTE EELSLYNITD CEFVKPGGLG PVLGPRHLSA LVFYGLVFLL GVPGNALVVW
VTGFRMPRSV TSLWFLNLAL ADLLCCLSLP LLMVPLAMDQ HWPFGPVACK LLKGLLYLIM
FCSVLLLVLI SLDRFLLVSW PVWCQNWRRP RKAGWVCVGV WLLALLGSIP QFVYVKEVQL
STSKSECLGL YTVASAWANT TARFLVGFVL PFITIVTCHW VVYSRARRGS GVGPGRVSEA
RSRRTLRVIV AVSLSFFLCW FPLHILDFLV LSTPRHSSHS ANIQLAHTLA LCLAYCNSCL
NPLLYVCLGR GFKQNINRSL RNMFNFATEE SVTRQSMFKS TSERTQEMNM
