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   04-NOV-2026, entry version 193.
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; DOI=10.4049/jimmunol.155.4.2158;
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).
RN   [11]
RP   FUNCTION.
RX   PubMed=20947763; DOI=10.1126/science.1195491;
RA   McDonald B., Pittman K., Menezes G.B., Hirota S.A., Slaba I.,
RA   Waterhouse C.C., Beck P.L., Muruve D.A., Kubes P.;
RT   "Intravascular danger signals guide neutrophils to sites of sterile
RT   inflammation.";
RL   Science 330:362-366(2010).
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 (By similarity). Involved in the homeostatic wound
CC       healing response to tissue injury, a multistep cascade that guides
CC       neutrophil migration to necrotic sites while avoiding collateral damage
CC       of healthy tissues. Signals intravascular neutrophil chemotaxis to the
CC       injury site (PubMed:20947763). {ECO:0000250|UniProtKB:P25025,
CC       ECO:0000269|PubMed:20947763}.
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_006495638.5.
DR   AlphaFoldDB; P35343; -.
DR   SMR; P35343; -.
DR   CORUM; P35343; -.
DR   FunCoup; P35343; 856.
DR   STRING; 10090.ENSMUSP00000102512; -.
DR   BindingDB; P35343; -.
DR   ChEMBL; CHEMBL4105830; -.
DR   GuidetoPHARMACOLOGY; 69; -.
DR   GlyCosmos; P35343; 2 sites, No reported glycans.
DR   GlyGen; P35343; 1 site.
DR   iPTMnet; P35343; -.
DR   PhosphoSitePlus; P35343; -.
DR   PaxDb; 10090-ENSMUSP00000102512; -.
DR   ProteomicsDB; 279245; -.
DR   DNASU; 12765; -.
DR   Ensembl; ENSMUST00000106899.4; ENSMUSP00000102512.3; ENSMUSG00000026180.10.
DR   GeneID; 12765; -.
DR   KEGG; mmu:12765; -.
DR   UCSC; uc007bll.1; mouse.
DR   AGR; MGI:105303; -.
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; AACIYAS; -.
DR   OrthoDB; 9946013at2759; -.
DR   PhylomeDB; P35343; -.
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 77 CRISPR screens.
DR   PRO; PR:P35343; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; P35343; protein.
DR   Bgee; ENSMUSG00000026180; Expressed in granulocyte and 20 other cell types or tissues.
DR   GO; GO:0009986; C:cell surface; ISO:GO_Central.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0097648; C:G protein-coupled receptor complex; ISO:GO_Central.
DR   GO; GO:0042629; C:mast cell granule; ISO:GO_Central.
DR   GO; GO:0016020; C:membrane; ISO:GO_Central.
DR   GO; GO:0015630; C:microtubule cytoskeleton; ISO:GO_Central.
DR   GO; GO:0072686; C:mitotic spindle; ISO:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; ISO:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISO:GO_Central.
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:GO_Central.
DR   GO; GO:0004950; F:chemokine receptor activity; IDA:MGI.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; ISO:GO_Central.
DR   GO; GO:0019959; F:interleukin-8 binding; ISO:GO_Central.
DR   GO; GO:0004918; F:interleukin-8 receptor activity; ISO:GO_Central.
DR   GO; GO:0032148; P:activation of protein kinase B activity; ISO:GO_Central.
DR   GO; GO:0002438; P:acute inflammatory response to antigenic stimulus; ISO:GO_Central.
DR   GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:GO_Central.
DR   GO; GO:0006968; P:cellular defense response; ISO:GO_Central.
DR   GO; GO:0006935; P:chemotaxis; ISO:GO_Central.
DR   GO; GO:0070371; P:ERK1 and ERK2 cascade; ISO:GO_Central.
DR   GO; GO:0006955; P:immune response; IBA:GO_Central.
DR   GO; GO:0038112; P:interleukin-8-mediated signaling pathway; ISO:GO_Central.
DR   GO; GO:0002522; P:leukocyte migration involved in immune response; ISO:GO_Central.
DR   GO; GO:0072173; P:metanephric tubule morphogenesis; ISO:GO_Central.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR   GO; GO:0033030; P:negative regulation of neutrophil apoptotic process; ISO:GO_Central.
DR   GO; GO:0042119; P:neutrophil activation; ISO:GO_Central.
DR   GO; GO:0030593; P:neutrophil chemotaxis; ISO:GO_Central.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISO:GO_Central.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; ISO:GO_Central.
DR   GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; ISO:GO_Central.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:GO_Central.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:GO_Central.
DR   GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; ISO:GO_Central.
DR   GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; ISO:GO_Central.
DR   GO; GO:0043117; P:positive regulation of vascular permeability; ISO:GO_Central.
DR   GO; GO:0031623; P:receptor internalization; ISO:GO_Central.
DR   GO; GO:0045765; P:regulation of angiogenesis; ISO:GO_Central.
DR   CDD; cd15178; 7tmA_CXCR1_2; 1.
DR   FunFam; 1.20.1070.10:FF:000157; C-X-C chemokine receptor type 2; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR050119; CCR1-9-like.
DR   InterPro; IPR000057; Chemokine_CXCR2.
DR   InterPro; IPR000174; Chemokine_CXCR_1/2.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR10489:SF689; C-X-C CHEMOKINE RECEPTOR TYPE 2; 1.
DR   PANTHER; PTHR10489; CELL ADHESION MOLECULE; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00427; INTRLEUKIN8R.
DR   PRINTS; PR00573; INTRLEUKN8BR.
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   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
//