ID C5AR1_MOUSE Reviewed; 351 AA.
AC P30993; Q3TZ86;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 07-JAN-2015, sequence version 2.
DT 27-MAR-2024, entry version 182.
DE RecName: Full=C5a anaphylatoxin chemotactic receptor 1;
DE AltName: Full=C5a anaphylatoxin chemotactic receptor;
DE Short=C5a-R;
DE Short=C5aR;
DE AltName: CD_antigen=CD88;
GN Name=C5ar1; Synonyms=C5ar, C5r1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1401897;
RA Gerard C., Bao L., Orozco O., Pearson M., Kunz D., Gerard N.P.;
RT "Structural diversity in the extracellular faces of peptidergic G-protein-
RT coupled receptors. Molecular cloning of the mouse C5a anaphylatoxin
RT receptor.";
RL J. Immunol. 149:2600-2606(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAP50849.1};
RC TISSUE=Lung {ECO:0000312|EMBL:AAP50849.1};
RX PubMed=16230349; DOI=10.1074/jbc.m509245200;
RA Waters S.M., Brodbeck R.M., Steflik J., Yu J., Baltazar C., Peck A.E.,
RA Severance D., Zhang L.Y., Currie K., Chenard B.L., Hutchison A.J.,
RA Maynard G., Krause J.E.;
RT "Molecular characterization of the gerbil C5a receptor and identification
RT of a transmembrane domain V amino acid that is crucial for small molecule
RT antagonist interaction.";
RL J. Biol. Chem. 280:40617-40623(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE34324.1};
RC TISSUE=Inner ear {ECO:0000312|EMBL:BAE34324.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:AAI25642.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325 AND SER-333, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Receptor for the chemotactic and inflammatory peptide
CC anaphylatoxin C5a. The ligand interacts with at least two sites on the
CC receptor: a high-affinity site on the extracellular N-terminus, and a
CC second site in the transmembrane region which activates downstream
CC signaling events. Receptor activation stimulates chemotaxis, granule
CC enzyme release, intracellular calcium release and superoxide anion
CC production. {ECO:0000250|UniProtKB:P21730}.
CC -!- SUBUNIT: Homodimer. May also form higher-order oligomers. Interacts
CC (when phosphorylated) with ARRB1 and ARRB2; the interaction is
CC associated with internalization of C5aR.
CC {ECO:0000250|UniProtKB:P21730}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P21730};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P21730}. Cytoplasmic
CC vesicle {ECO:0000250|UniProtKB:P21730}. Note=Phosphorylated C5aR
CC colocalizes with ARRB1 and ARRB2 in cytoplasmic vesicles.
CC {ECO:0000250|UniProtKB:P21730}.
CC -!- PTM: Sulfation plays a critical role in the association of C5aR with
CC C5a, but no significant role in the ability of the receptor to
CC transduce a signal and mobilize calcium in response to a small peptide
CC agonist. {ECO:0000250|UniProtKB:P21730}.
CC -!- PTM: Phosphorylated on serine residues in response to C5a binding,
CC resulting in internalization of the receptor and short-term
CC desensitization to C5a. {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; S46665; AAB97774.1; -; Genomic_DNA.
DR EMBL; S50577; AAB97774.1; JOINED; Genomic_DNA.
DR EMBL; AY220494; AAP50849.1; -; mRNA.
DR EMBL; AK158027; BAE34324.1; -; mRNA.
DR EMBL; AC156630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC125641; AAI25642.1; -; mRNA.
DR EMBL; BC125643; AAI25644.1; -; mRNA.
DR CCDS; CCDS20846.1; -.
DR PIR; A46525; A46525.
DR RefSeq; NP_001167021.1; NM_001173550.1.
DR RefSeq; NP_031603.2; NM_007577.4.
DR PDB; 8HPT; EM; 3.39 A; A=2-351.
DR PDB; 8HQC; EM; 3.89 A; A=2-351.
DR PDBsum; 8HPT; -.
DR PDBsum; 8HQC; -.
DR AlphaFoldDB; P30993; -.
DR EMDB; EMD-34943; -.
DR EMDB; EMD-34947; -.
DR SMR; P30993; -.
DR IntAct; P30993; 3.
DR MINT; P30993; -.
DR STRING; 10090.ENSMUSP00000129972; -.
DR BindingDB; P30993; -.
DR ChEMBL; CHEMBL5746; -.
DR GuidetoPHARMACOLOGY; 32; -.
DR GlyCosmos; P30993; 1 site, No reported glycans.
DR GlyGen; P30993; 1 site.
DR iPTMnet; P30993; -.
DR PhosphoSitePlus; P30993; -.
DR jPOST; P30993; -.
DR PaxDb; 10090-ENSMUSP00000129972; -.
DR PeptideAtlas; P30993; -.
DR ProteomicsDB; 273861; -.
DR Antibodypedia; 2966; 1124 antibodies from 38 providers.
DR DNASU; 12273; -.
DR Ensembl; ENSMUST00000050770.6; ENSMUSP00000060003.6; ENSMUSG00000049130.7.
DR Ensembl; ENSMUST00000168818.2; ENSMUSP00000129972.2; ENSMUSG00000049130.7.
DR GeneID; 12273; -.
DR KEGG; mmu:12273; -.
DR UCSC; uc009fhl.2; mouse.
DR AGR; MGI:88232; -.
DR CTD; 728; -.
DR MGI; MGI:88232; C5ar1.
DR VEuPathDB; HostDB:ENSMUSG00000049130; -.
DR eggNOG; ENOG502R35Z; Eukaryota.
DR GeneTree; ENSGT01100000263564; -.
DR HOGENOM; CLU_009579_8_0_1; -.
DR InParanoid; P30993; -.
DR OMA; VAVWCLA; -.
DR OrthoDB; 4264357at2759; -.
DR PhylomeDB; P30993; -.
DR TreeFam; TF330976; -.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-977606; Regulation of Complement cascade.
DR BioGRID-ORCS; 12273; 3 hits in 77 CRISPR screens.
DR PRO; PR:P30993; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P30993; Protein.
DR Bgee; ENSMUSG00000049130; Expressed in granulocyte and 89 other cell types or tissues.
DR ExpressionAtlas; P30993; baseline and differential.
DR Genevisible; P30993; MM.
DR GO; GO:0045177; C:apical part of cell; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001856; F:complement component C5a binding; ISO:MGI.
DR GO; GO:0004878; F:complement component C5a receptor activity; IDA:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISO:MGI.
DR GO; GO:0097242; P:amyloid-beta clearance; IGI:ARUK-UCL.
DR GO; GO:0048143; P:astrocyte activation; IGI:ARUK-UCL.
DR GO; GO:0021534; P:cell proliferation in hindbrain; ISO:MGI.
DR GO; GO:0050890; P:cognition; IGI:ARUK-UCL.
DR GO; GO:0038178; P:complement component C5a signaling pathway; ISO:MGI.
DR GO; GO:0002430; P:complement receptor mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0001774; P:microglial cell activation; IGI:ARUK-UCL.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0030593; P:neutrophil chemotaxis; IMP:MGI.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
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:0010759; P:positive regulation of macrophage chemotaxis; IMP:BHF-UCL.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IMP:BHF-UCL.
DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IMP:BHF-UCL.
DR GO; GO:0099172; P:presynapse organization; IGI:ARUK-UCL.
DR GO; GO:1902947; P:regulation of tau-protein kinase activity; IGI:ARUK-UCL.
DR GO; GO:0032494; P:response to peptidoglycan; IMP:MGI.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
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:SF29; C5A ANAPHYLATOXIN CHEMOTACTIC RECEPTOR 1; 1.
DR PANTHER; PTHR24225; CHEMOTACTIC RECEPTOR; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01104; ANPHYLATOXNR.
DR PRINTS; PR00426; C5ANPHYLTXNR.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Chemotaxis; Cytoplasmic vesicle;
KW Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Sulfation; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..351
FT /note="C5a anaphylatoxin chemotactic receptor 1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000069211"
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..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 154..174
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 175..201
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 202..227
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 228..243
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 244..266
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 267..283
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 284..304
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT TOPO_DOM 305..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 329..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT MOD_RES 16
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21730"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 109..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 66..70
FT /note="ARRAV -> PDGPS (in Ref. 1; AAB97774)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="L -> M (in Ref. 1; AAB97774)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="T -> D (in Ref. 1; AAB97774)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 351 AA; 39023 MW; 1186314DBAECC8F2 CRC64;
MDPIDNSSFE INYDHYGTMD PNIPADGIHL PKRQPGDVAA LIIYSVVFLV GVPGNALVVW
VTAFEARRAV NAIWFLNLAV ADLLSCLALP VLFTTVLNHN YWYFDATACI VLPSLILLNM
YASILLLATI SADRFLLVFK PIWCQKVRGT GLAWMACGVA WVLALLLTIP SFVYREAYKD
FYSEHTVCGI NYGGGSFPKE KAVAILRLMV GFVLPLLTLN ICYTFLLLRT WSRKATRSTK
TLKVVMAVVI CFFIFWLPYQ VTGVMIAWLP PSSPTLKRVE KLNSLCVSLA YINCCVNPII
YVMAGQGFHG RLLRSLPSII RNALSEDSVG RDSKTFTPST TDTSTRKSQA V
//
