C5AR2_MOUSE
ID C5AR2_MOUSE Reviewed; 344 AA.
AC Q8BW93; B2RQI1; Q3TVM8;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 135.
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 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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=15833747; DOI=10.1074/jbc.m406921200;
RA Kalant D., MacLaren R., Cui W., Samanta R., Monk P.N., Laporte S.A.,
RA Cianflone K.;
RT "C5L2 is a functional receptor for acylation-stimulating protein.";
RL J. Biol. Chem. 280:23936-23944(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
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 (By similarity). {ECO:0000250}.
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 -!- TISSUE SPECIFICITY: Highly expressed in liver and spleen. Lower levels
CC in intestine, brain and kidney. Also expressed in adipose tissues with
CC highest levels in gonadal and ingual fat depots. Lower levels in brown
CC tissue. {ECO:0000269|PubMed:15833747}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE35590.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK053187; BAC35303.1; -; mRNA.
DR EMBL; AK160050; BAE35590.1; ALT_INIT; mRNA.
DR EMBL; BC137941; AAI37942.1; -; mRNA.
DR EMBL; BC145834; AAI45835.1; -; mRNA.
DR CCDS; CCDS52036.2; -.
DR RefSeq; NP_001139477.1; NM_001146005.1.
DR RefSeq; NP_795886.2; NM_176912.4.
DR RefSeq; XP_006540112.2; XM_006540049.2.
DR RefSeq; XP_006540115.1; XM_006540052.3.
DR RefSeq; XP_006540116.1; XM_006540053.3.
DR RefSeq; XP_006540117.1; XM_006540054.3.
DR RefSeq; XP_006540118.1; XM_006540055.3.
DR RefSeq; XP_006540119.1; XM_006540056.2.
DR AlphaFoldDB; Q8BW93; -.
DR SMR; Q8BW93; -.
DR IntAct; Q8BW93; 1.
DR STRING; 10090.ENSMUSP00000133056; -.
DR GuidetoPHARMACOLOGY; 33; -.
DR GlyGen; Q8BW93; 1 site.
DR PhosphoSitePlus; Q8BW93; -.
DR MaxQB; Q8BW93; -.
DR PaxDb; Q8BW93; -.
DR PRIDE; Q8BW93; -.
DR Antibodypedia; 2937; 414 antibodies from 36 providers.
DR DNASU; 319430; -.
DR Ensembl; ENSMUST00000171425; ENSMUSP00000133056; ENSMUSG00000074361.
DR Ensembl; ENSMUST00000238927; ENSMUSP00000158951; ENSMUSG00000074361.
DR GeneID; 319430; -.
DR KEGG; mmu:319430; -.
DR CTD; 27202; -.
DR MGI; MGI:2442013; C5ar2.
DR VEuPathDB; HostDB:ENSMUSG00000074361; -.
DR eggNOG; ENOG502R35Z; Eukaryota.
DR GeneTree; ENSGT01020000230336; -.
DR InParanoid; Q8BW93; -.
DR OMA; CHGALLC; -.
DR OrthoDB; 978188at2759; -.
DR PhylomeDB; Q8BW93; -.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR Reactome; R-MMU-977606; Regulation of Complement cascade.
DR BioGRID-ORCS; 319430; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q8BW93; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BW93; protein.
DR Bgee; ENSMUSG00000074361; Expressed in granulocyte and 26 other tissues.
DR ExpressionAtlas; Q8BW93; baseline and differential.
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; IEA:UniProtKB-KW.
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: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; IPR001274; Anaphtx_C5AR1/C5AR2.
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; PR00426; C5ANPHYLTXNR.
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..344
FT /note="C5a anaphylatoxin chemotactic receptor 2"
FT /id="PRO_0000303083"
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..344
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q695P6"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 113..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 6
FT /note="T -> N (in Ref. 1; BAE35590)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 38199 MW; 508FFD23F01B31C8 CRC64;
MMNHTTSEYY DYEYDHEHYS DLPDVPVDCP AGTCFTSDVY LIVLLVLYAA VFLVGVPGNT
LVAWVTWKES RHRLGASWFL HLTMADLLCC VSLPFLAVPI AQKGHWPYGA AGCWLLSSIT
ILSMYASVLL LTGLSGDLFL LAFRPSWKGA DHRTFGVRVV QASSWMLGLL LTVPSAVYRR
LLQEHYPPRL VCGIDYGGSV SAEVAITTVR FLFGFLGPLV FMAGCHGILQ RQMARRHWPL
GTAVVVGFFI CWTPYHVLRV IIAAAPPHSL LLARVLEAEP LFNGLALAHS ALNPIMFLYF
GRKQLCKSLQ AACHWALRDP QDEESAVTKV SISTSHEMVS EMPV
