ID   CXCR2_RAT               Reviewed;         359 AA.
AC   P35407;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   02-SEP-2026, entry version 186.
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=Il8rb;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Lung;
RX   PubMed=9218548; DOI=10.1016/s0005-2736(97)00065-5;
RA   Gobl A.E., Huang M.R., Wang S., Zhou Y., Oeberg K.;
RT   "Molecular cloning and characterization of a cDNA encoding the rat
RT   interleukin-8 receptor.";
RL   Biochim. Biophys. Acta 1326:171-177(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Wistar; TISSUE=Liver;
RA   Konishi K., Shibata F., Watanabe K., Tsurufuji S., Nakagawa H., Fujioka M.;
RL   Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Wistar; TISSUE=Lung, and Spleen;
RX   PubMed=8955112; DOI=10.1074/jbc.271.51.32770;
RA   Dunstan C.-A.N., Salafranca M.N., Adhikari S., Xia Y., Feng L.,
RA   Harrison J.K.;
RT   "Identification of two rat genes orthologous to the human interleukin-8
RT   receptors.";
RL   J. Biol. Chem. 271:32770-32776(1996).
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 (By similarity). {ECO:0000250|UniProtKB:P25025,
CC       ECO:0000250|UniProtKB:P35343}.
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; X77797; CAA54824.1; -; mRNA.
DR   EMBL; D63584; BAA09797.1; -; Genomic_DNA.
DR   EMBL; U70988; AAC52961.1; -; Genomic_DNA.
DR   PIR; S42096; S42096.
DR   RefSeq; NP_058879.1; NM_017183.2.
DR   AlphaFoldDB; P35407; -.
DR   SMR; P35407; -.
DR   BioGRID; 248037; 3.
DR   FunCoup; P35407; 364.
DR   IntAct; P35407; 1.
DR   MINT; P35407; -.
DR   STRING; 10116.ENSRNOP00000019109; -.
DR   GlyCosmos; P35407; 4 sites, No reported glycans.
DR   GlyGen; P35407; 4 sites.
DR   PhosphoSitePlus; P35407; -.
DR   PaxDb; 10116-ENSRNOP00000019109; -.
DR   Ensembl; ENSRNOT00000101059.2; ENSRNOP00000093296.1; ENSRNOG00000063618.2.
DR   Ensembl; ENSRNOT00000144913.1; ENSRNOP00000110815.1; ENSRNOG00000063618.2.
DR   Ensembl; ENSRNOT00055016067; ENSRNOP00055012901; ENSRNOG00055009510.
DR   Ensembl; ENSRNOT00060011670; ENSRNOP00060008782; ENSRNOG00060007107.
DR   Ensembl; ENSRNOT00065013752; ENSRNOP00065010201; ENSRNOG00065008665.
DR   GeneID; 29385; -.
DR   KEGG; rno:29385; -.
DR   UCSC; RGD:2906; rat.
DR   AGR; RGD:2906; -.
DR   CTD; 3579; -.
DR   RGD; 2906; Cxcr2.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01050000244848; -.
DR   HOGENOM; CLU_009579_8_3_1; -.
DR   InParanoid; P35407; -.
DR   OMA; YSPCEIS; -.
DR   OrthoDB; 9946013at2759; -.
DR   PhylomeDB; P35407; -.
DR   Reactome; R-RNO-380108; Chemokine receptors bind chemokines.
DR   Reactome; R-RNO-418594; G alpha (i) signalling events.
DR   Reactome; R-RNO-6798695; Neutrophil degranulation.
DR   PRO; PR:P35407; -.
DR   Proteomes; UP000002494; Chromosome 9.
DR   Bgee; ENSRNOG00000014269; Expressed in esophagus and 10 other cell types or tissues.
DR   ExpressionAtlas; P35407; baseline.
DR   GO; GO:0009986; C:cell surface; ISO:RGD.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0042629; C:mast cell granule; ISO:RGD.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
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:RGD.
DR   GO; GO:0004950; F:chemokine receptor activity; ISO:RGD.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; ISO:RGD.
DR   GO; GO:0019959; F:interleukin-8 binding; ISO:RGD.
DR   GO; GO:0004918; F:interleukin-8 receptor activity; ISO:RGD.
DR   GO; GO:0002438; P:acute inflammatory response to antigenic stimulus; IMP:RGD.
DR   GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:RGD.
DR   GO; GO:0006968; P:cellular defense response; ISO:RGD.
DR   GO; GO:0006935; P:chemotaxis; ISO:RGD.
DR   GO; GO:0006955; P:immune response; IBA:GO_Central.
DR   GO; GO:0038112; P:interleukin-8-mediated signaling pathway; ISO:RGD.
DR   GO; GO:0072173; P:metanephric tubule morphogenesis; IMP:RGD.
DR   GO; GO:0030901; P:midbrain development; IEP:RGD.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR   GO; GO:0033030; P:negative regulation of neutrophil apoptotic process; IMP:RGD.
DR   GO; GO:0042119; P:neutrophil activation; ISO:RGD.
DR   GO; GO:0030593; P:neutrophil chemotaxis; IMP:RGD.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISO:RGD.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IMP:RGD.
DR   GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; IMP:RGD.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:RGD.
DR   GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; IMP:RGD.
DR   GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IMP:RGD.
DR   GO; GO:0043117; P:positive regulation of vascular permeability; IMP:RGD.
DR   GO; GO:0031623; P:receptor internalization; ISO:RGD.
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_0000069342"
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..296
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        297..314
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        315..359
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        8
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        23
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        201
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        202
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;  40532 MW;  EF547326A074ABDD CRC64;
     MGEIRVDNFS LEDFFSGDID SYNYSSDPPF TLSDAAPCPS ANLDINRYAV VVIYVLVTLL
     SLVGNSLVML VILYNRSTCS VTDVYLLNLA IADLFFALTL PVWAASKVNG WIFGSFLCKV
     FSFLQEITFY SSVLLLACIS MDRYLAIVHA TSTLIQKRHL VKFVCITMWF LSLVLSLPIF
     ILRTTVKANP STVVCYENIG NNTSKWRVVL RILPQTYGFL LPLLIMLFCY GFTLRTLFKA
     HMGQKHRAMR VIFAVVLVFL LCWLPYNIVL FTDTLMRTKL IKETCERQNE INKALEATEI
     LGFLHSCLNP IIYAFIGQKF RHGLLKIMAN YGLVSKEFLA KEGRPSFVGS SSANTSTTL
//