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C5a anaphylatoxin chemotactic receptor 1 (C5a anaphylatoxin chemotactic receptor) (C5a-R) (C5aR) (CD antigen CD88)

 C5AR1_MOUSE             Reviewed;         351 AA.
P30993; Q3TZ86;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
07-JAN-2015, sequence version 2.
23-MAY-2018, entry version 146.
RecName: Full=C5a anaphylatoxin chemotactic receptor 1;
AltName: Full=C5a anaphylatoxin chemotactic receptor;
Short=C5a-R;
Short=C5aR;
AltName: CD_antigen=CD88;
Name=C5ar1; Synonyms=C5ar, C5r1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1401897;
Gerard C., Bao L., Orozco O., Pearson M., Kunz D., Gerard N.P.;
"Structural diversity in the extracellular faces of peptidergic G-
protein-coupled receptors. Molecular cloning of the mouse C5a
anaphylatoxin receptor.";
J. Immunol. 149:2600-2606(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAP50849.1};
TISSUE=Lung {ECO:0000312|EMBL:AAP50849.1};
PubMed=16230349; DOI=10.1074/jbc.M509245200;
Waters S.M., Brodbeck R.M., Steflik J., Yu J., Baltazar C., Peck A.E.,
Severance D., Zhang L.Y., Currie K., Chenard B.L., Hutchison A.J.,
Maynard G., Krause J.E.;
"Molecular characterization of the gerbil C5a receptor and
identification of a transmembrane domain V amino acid that is crucial
for small molecule antagonist interaction.";
J. Biol. Chem. 280:40617-40623(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE34324.1};
TISSUE=Inner ear {ECO:0000312|EMBL:BAE34324.1};
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain {ECO:0000312|EMBL:AAI25642.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325 AND SER-333, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Receptor for the chemotactic and inflammatory peptide
anaphylatoxin C5a. The ligand interacts with at least two sites on
the receptor: a high-affinity site on the extracellular N-
terminus, and a second site in the transmembrane region which
activates downstream signaling events. Receptor activation
stimulates chemotaxis, granule enzyme release, intracellular
calcium release and superoxide anion production.
{ECO:0000250|UniProtKB:P21730}.
-!- SUBUNIT: Homodimer. May also form higher-order oligomers.
Interacts (when phosphorylated) with ARRB1 and ARRB2; the
interaction is associated with internalization of C5aR.
{ECO:0000250|UniProtKB:P21730}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P21730}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P21730}. Cytoplasmic vesicle
{ECO:0000250|UniProtKB:P21730}. Note=Phosphorylated C5aR
colocalizes with ARRB1 and ARRB2 in cytoplasmic vesicles.
{ECO:0000250|UniProtKB:P21730}.
-!- PTM: Sulfation plays a critical role in the association of C5aR
with C5a, but no significant role in the ability of the receptor
to transduce a signal and mobilize calcium in response to a small
peptide agonist. {ECO:0000250|UniProtKB:P21730}.
-!- PTM: Phosphorylated on serine residues in response to C5a binding,
resulting in internalization of the receptor and short-term
desensitization to C5a. {ECO:0000250|UniProtKB:P21730}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-----------------------------------------------------------------------
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EMBL; S46665; AAB97774.1; -; Genomic_DNA.
EMBL; S50577; AAB97774.1; JOINED; Genomic_DNA.
EMBL; AY220494; AAP50849.1; -; mRNA.
EMBL; AK158027; BAE34324.1; -; mRNA.
EMBL; AC156630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC125641; AAI25642.1; -; mRNA.
EMBL; BC125643; AAI25644.1; -; mRNA.
CCDS; CCDS20846.1; -.
PIR; A46525; A46525.
RefSeq; NP_001167021.1; NM_001173550.1.
RefSeq; NP_031603.2; NM_007577.4.
UniGene; Mm.247623; -.
ProteinModelPortal; P30993; -.
SMR; P30993; -.
IntAct; P30993; 1.
STRING; 10090.ENSMUSP00000060003; -.
ChEMBL; CHEMBL5746; -.
GuidetoPHARMACOLOGY; 32; -.
iPTMnet; P30993; -.
PhosphoSitePlus; P30993; -.
PaxDb; P30993; -.
PeptideAtlas; P30993; -.
PRIDE; P30993; -.
Ensembl; ENSMUST00000050770; ENSMUSP00000060003; ENSMUSG00000049130.
Ensembl; ENSMUST00000168818; ENSMUSP00000129972; ENSMUSG00000049130.
GeneID; 12273; -.
KEGG; mmu:12273; -.
UCSC; uc009fhl.2; mouse.
CTD; 728; -.
MGI; MGI:88232; C5ar1.
eggNOG; ENOG410IF0K; Eukaryota.
eggNOG; ENOG410Y9HH; LUCA.
GeneTree; ENSGT00760000118990; -.
HOGENOM; HOG000234122; -.
HOVERGEN; HBG107547; -.
InParanoid; P30993; -.
KO; K04010; -.
OMA; YINCCIN; -.
OrthoDB; EOG091G0DT8; -.
Reactome; R-MMU-375276; Peptide ligand-binding receptors.
Reactome; R-MMU-418594; G alpha (i) signalling events.
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-977606; Regulation of Complement cascade.
PRO; PR:P30993; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000049130; -.
CleanEx; MM_C5AR1; -.
ExpressionAtlas; P30993; baseline and differential.
Genevisible; P30993; MM.
GO; GO:0045177; C:apical part of cell; ISS:UniProtKB.
GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0004878; F:complement component C5a receptor activity; IDA:MGI.
GO; GO:0004930; F:G-protein coupled receptor activity; IBA:GO_Central.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:MGI.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0030593; P:neutrophil chemotaxis; IMP:MGI.
GO; GO:0007200; P:phospholipase C-activating G-protein coupled receptor signaling pathway; IBA:GO_Central.
GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IMP:BHF-UCL.
GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IMP:BHF-UCL.
GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IMP:BHF-UCL.
GO; GO:0032494; P:response to peptidoglycan; IMP:MGI.
InterPro; IPR001274; Anaphtx_C5AR1/C5AR2.
InterPro; IPR002234; Anphylx_rcpt.
InterPro; IPR000826; Formyl_rcpt-rel.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
PANTHER; PTHR24225; PTHR24225; 1.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR01104; ANPHYLATOXNR.
PRINTS; PR00426; C5ANPHYLTXNR.
PRINTS; PR00237; GPCRRHODOPSN.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
Cell membrane; Chemotaxis; Complete proteome; Cytoplasmic vesicle;
Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane;
Phosphoprotein; Receptor; Reference proteome; Sulfation; Transducer;
Transmembrane; Transmembrane helix.
CHAIN 1 351 C5a anaphylatoxin chemotactic receptor 1.
{ECO:0000305}.
/FTId=PRO_0000069211.
TOPO_DOM 1 37 Extracellular. {ECO:0000305}.
TRANSMEM 38 64 Helical; Name=1.
{ECO:0000250|UniProtKB:P21730}.
TOPO_DOM 65 69 Cytoplasmic. {ECO:0000305}.
TRANSMEM 70 93 Helical; Name=2.
{ECO:0000250|UniProtKB:P21730}.
TOPO_DOM 94 110 Extracellular. {ECO:0000305}.
TRANSMEM 111 132 Helical; Name=3.
{ECO:0000250|UniProtKB:P21730}.
TOPO_DOM 133 153 Cytoplasmic. {ECO:0000305}.
TRANSMEM 154 174 Helical; Name=4.
{ECO:0000250|UniProtKB:P21730}.
TOPO_DOM 175 201 Extracellular. {ECO:0000305}.
TRANSMEM 202 227 Helical; Name=5.
{ECO:0000250|UniProtKB:P21730}.
TOPO_DOM 228 243 Cytoplasmic. {ECO:0000305}.
TRANSMEM 244 266 Helical; Name=6.
{ECO:0000250|UniProtKB:P21730}.
TOPO_DOM 267 283 Extracellular. {ECO:0000305}.
TRANSMEM 284 304 Helical; Name=7.
{ECO:0000250|UniProtKB:P21730}.
TOPO_DOM 305 351 Cytoplasmic. {ECO:0000305}.
MOD_RES 13 13 Sulfotyrosine.
{ECO:0000250|UniProtKB:P21730}.
MOD_RES 16 16 Sulfotyrosine.
{ECO:0000250|UniProtKB:P21730}.
MOD_RES 315 315 Phosphoserine.
{ECO:0000250|UniProtKB:P21730}.
MOD_RES 318 318 Phosphoserine.
{ECO:0000250|UniProtKB:P21730}.
MOD_RES 325 325 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 328 328 Phosphoserine.
{ECO:0000250|UniProtKB:P21730}.
MOD_RES 333 333 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 339 339 Phosphoserine.
{ECO:0000250|UniProtKB:P21730}.
CARBOHYD 6 6 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 109 188 {ECO:0000255|PROSITE-ProRule:PRU00521}.
CONFLICT 66 70 ARRAV -> PDGPS (in Ref. 1; AAB97774).
{ECO:0000305}.
CONFLICT 89 89 L -> M (in Ref. 1; AAB97774).
{ECO:0000305}.
CONFLICT 341 341 T -> D (in Ref. 1; AAB97774).
{ECO:0000305}.
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


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