CXCR2_MOUSE
ID CXCR2_MOUSE Reviewed; 359 AA.
AC P35343; Q53X27;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=C-X-C chemokine receptor type 2;
DE Short=CXC-R2;
DE Short=CXCR-2;
DE AltName: Full=GRO/MGSA receptor;
DE AltName: Full=High affinity interleukin-8 receptor B;
DE Short=IL-8R B;
DE AltName: CD_antigen=CD182;
GN Name=Cxcr2; Synonyms=Cmkar2, Gpcr16, Il8rb;
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=8288247; DOI=10.1006/geno.1993.1486;
RA Cerretti D.P., Nelson N., Kozlosky C.J., Morrissey P.J., Copeland N.G.,
RA Gilbert D.J., Jenkins N.A., Dosik J.K., Mock B.A.;
RT "The murine homologue of the human interleukin-8 receptor type B maps near
RT the Ity-Lsh-Bcg disease resistance locus.";
RL Genomics 18:410-413(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7518426; DOI=10.1016/s0021-9258(17)32295-0;
RA Suzuki H., Prado G.N., Wilkinson N., Navarro J.;
RT "The N-terminus of interleukin-8 (IL-8) receptor confers high affinity
RT binding to human IL-8.";
RL J. Biol. Chem. 269:18263-18266(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ;
RX PubMed=7961909; DOI=10.1016/s0021-9258(18)43882-3;
RA Bozic C.R., Gerard N.P., von Uexkull-Guldenband C., Kolakowski L.F. Jr.,
RA Conklyn M.J., Breslow R., Showell H.J., Gerard C.;
RT "The murine interleukin 8 type B receptor homologue and its ligands.
RT Expression and biological characterization.";
RL J. Biol. Chem. 269:29355-29358(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=7636264;
RA Lee J., Cacalano G., Camerato T., Toy K., Moore M.W., Wood W.I.;
RT "Chemokine binding and activities mediated by the mouse IL-8 receptor.";
RL J. Immunol. 155:2158-2164(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8194768; DOI=10.1016/0378-1119(94)90278-x;
RA Harada A., Kuno K., Nomura H., Mukaida N., Murakami S., Matsushima K.;
RT "Cloning of a cDNA encoding a mouse homolog of the interleukin-8
RT receptor.";
RL Gene 142:297-300(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Inner ear;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trophoblast;
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 [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 145-258.
RC TISSUE=Testis;
RX PubMed=8288218; DOI=10.1006/geno.1993.1452;
RA Wilkie T.M., Chen Y., Gilbert D.J., Moore K.J., Yu L., Simon M.I.,
RA Copeland N.G., Jenkins N.A.;
RT "Identification, chromosomal location, and genome organization of mammalian
RT G-protein-coupled receptors.";
RL Genomics 18:175-184(1993).
RN [10]
RP FUNCTION.
RX PubMed=14764687; DOI=10.4049/jimmunol.172.4.2201;
RA Nolan K.F., Strong V., Soler D., Fairchild P.J., Cobbold S.P., Croxton R.,
RA Gonzalo J.-A., Rubio A., Wells M., Waldmann H.;
RT "IL-10-conditioned dendritic cells, decommissioned for recruitment of
RT adaptive immunity, elicit innate inflammatory gene products in response to
RT danger signals.";
RL J. Immunol. 172:2201-2209(2004).
CC -!- FUNCTION: Receptor for interleukin-8 which is a powerful neutrophil
CC chemotactic factor. Binding of IL-8 to the receptor causes activation
CC of neutrophils. This response is mediated via a G-protein that
CC activates a phosphatidylinositol-calcium second messenger system. Binds
CC to IL-8 with high affinity. Also binds with high affinity to CXCL3,
CC GRO/MGSA and NAP-2. {ECO:0000250|UniProtKB:P25025}.
CC -!- SUBUNIT: Interacts with IL8. Interacts with GNAI2.
CC {ECO:0000250|UniProtKB:P25025}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- PTM: Phosphorylated upon ligand binding; which is required for
CC desensitization. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; L23637; AAA39305.1; -; Genomic_DNA.
DR EMBL; L26549; AAL31314.1; -; Genomic_DNA.
DR EMBL; L13239; AAA62109.1; -; Genomic_DNA.
DR EMBL; U31207; AAC52239.1; -; Genomic_DNA.
DR EMBL; D17630; BAA04536.1; -; mRNA.
DR EMBL; AK158234; BAE34417.1; -; mRNA.
DR EMBL; CH466548; EDL00307.1; -; Genomic_DNA.
DR EMBL; BC051677; AAH51677.1; -; mRNA.
DR EMBL; L20337; AAA16853.1; -; mRNA.
DR CCDS; CCDS15040.1; -.
DR PIR; A48921; A48921.
DR RefSeq; NP_034039.1; NM_009909.3.
DR RefSeq; XP_006495701.1; XM_006495638.3.
DR AlphaFoldDB; P35343; -.
DR SMR; P35343; -.
DR CORUM; P35343; -.
DR STRING; 10090.ENSMUSP00000102512; -.
DR BindingDB; P35343; -.
DR ChEMBL; CHEMBL4105830; -.
DR GuidetoPHARMACOLOGY; 69; -.
DR GlyGen; P35343; 1 site.
DR iPTMnet; P35343; -.
DR PhosphoSitePlus; P35343; -.
DR EPD; P35343; -.
DR MaxQB; P35343; -.
DR PaxDb; P35343; -.
DR PRIDE; P35343; -.
DR ProteomicsDB; 279245; -.
DR DNASU; 12765; -.
DR Ensembl; ENSMUST00000027372; ENSMUSP00000027372; ENSMUSG00000026180.
DR Ensembl; ENSMUST00000106899; ENSMUSP00000102512; ENSMUSG00000026180.
DR GeneID; 12765; -.
DR KEGG; mmu:12765; -.
DR UCSC; uc007bll.1; mouse.
DR CTD; 3579; -.
DR MGI; MGI:105303; Cxcr2.
DR VEuPathDB; HostDB:ENSMUSG00000026180; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244848; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; P35343; -.
DR OMA; FIFREAY; -.
DR OrthoDB; 865441at2759; -.
DR PhylomeDB; P35343; -.
DR TreeFam; TF330966; -.
DR Reactome; R-MMU-380108; Chemokine receptors bind chemokines.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 12765; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Cxcr2; mouse.
DR PRO; PR:P35343; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P35343; protein.
DR Bgee; ENSMUSG00000026180; Expressed in granulocyte and 17 other tissues.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042629; C:mast cell granule; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0019957; F:C-C chemokine binding; IBA:GO_Central.
DR GO; GO:0016493; F:C-C chemokine receptor activity; IBA:GO_Central.
DR GO; GO:0016494; F:C-X-C chemokine receptor activity; ISO:MGI.
DR GO; GO:0004950; F:chemokine receptor activity; IDA:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISO:MGI.
DR GO; GO:0019959; F:interleukin-8 binding; ISO:MGI.
DR GO; GO:0004918; F:interleukin-8 receptor activity; ISO:MGI.
DR GO; GO:0002438; P:acute inflammatory response to antigenic stimulus; ISO:MGI.
DR GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
DR GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:MGI.
DR GO; GO:0006968; P:cellular defense response; ISO:MGI.
DR GO; GO:0006935; P:chemotaxis; ISO:MGI.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0038112; P:interleukin-8-mediated signaling pathway; ISO:MGI.
DR GO; GO:0072173; P:metanephric tubule morphogenesis; ISO:MGI.
DR GO; GO:0030901; P:midbrain development; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0033030; P:negative regulation of neutrophil apoptotic process; ISO:MGI.
DR GO; GO:0042119; P:neutrophil activation; ISO:MGI.
DR GO; GO:0030593; P:neutrophil chemotaxis; ISO:MGI.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; ISO:MGI.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; ISO:MGI.
DR GO; GO:0043117; P:positive regulation of vascular permeability; ISO:MGI.
DR GO; GO:0031623; P:receptor internalization; ISO:MGI.
DR InterPro; IPR000057; Chemokine_CXCR2.
DR InterPro; IPR000174; Chemokine_CXCR_1/2.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00427; INTRLEUKIN8R.
DR PRINTS; PR00573; INTRLEUKN8BR.
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; Phosphoprotein; Receptor; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..359
FT /note="C-X-C chemokine receptor type 2"
FT /id="PRO_0000069339"
FT TOPO_DOM 1..47
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..74
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..119
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..141
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..182
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..207
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..230
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..272
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..293
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..359
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 118..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 359 AA; 40425 MW; 74BD166E9B679F88 CRC64;
MGEFKVDKFN IEDFFSGDLD IFNYSSGMPS ILPDAVPCHS ENLEINSYAV VVIYVLVTLL
SLVGNSLVML VILYNRSTCS VTDVYLLNLA IADLFFALTL PVWAASKVNG WTFGSTLCKI
FSYVKEVTFY SSVLLLACIS MDRYLAIVHA TSTLIQKRHL VKFVCIAMWL LSVILALPIL
ILRNPVKVNL STLVCYEDVG NNTSRLRVVL RILPQTFGFL VPLLIMLFCY GFTLRTLFKA
HMGQKHRAMR VIFAVVLVFL LCWLPYNLVL FTDTLMRTKL IKETCERRDD IDKALNATEI
LGFLHSCLNP IIYAFIGQKF RHGLLKIMAT YGLVSKEFLA KEGRPSFVSS SSANTSTTL
