ID   CXCR1_MACMU             Reviewed;         351 AA.
AC   Q2YEG0;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   RecName: Full=C-X-C chemokine receptor type 1;
DE            Short=CXC-R1;
DE            Short=CXCR-1;
DE   AltName: Full=High affinity interleukin-8 receptor A;
DE            Short=IL-8R A;
DE   AltName: Full=IL-8 receptor type 1;
DE   AltName: CD_antigen=CD181;
GN   Name=CXCR1; Synonyms=IL8RA;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16205979; DOI=10.1007/s00239-005-0039-x;
RA   Liu Y., Yang S., Lin A.A., Cavalli-Sforza L.L., Su B.;
RT   "Molecular evolution of CXCR1, a G protein-coupled receptor involved in
RT   signal transduction of neutrophils.";
RL   J. Mol. Evol. 61:691-696(2005).
CC   -!- FUNCTION: Receptor to interleukin-8, which is a powerful neutrophils
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.
CC       {ECO:0000250|UniProtKB:P25024}.
CC   -!- SUBUNIT: Interacts with IL8. Interacts with GNAI2.
CC       {ECO:0000250|UniProtKB:P25024}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY916770; AAY21520.1; -; Genomic_DNA.
DR   RefSeq; NP_001035510.1; NM_001040420.1.
DR   RefSeq; XP_014966445.1; XM_015110959.1.
DR   RefSeq; XP_014966446.1; XM_015110960.1.
DR   RefSeq; XP_014966447.1; XM_015110961.1.
DR   RefSeq; XP_014966448.1; XM_015110962.1.
DR   AlphaFoldDB; Q2YEG0; -.
DR   SMR; Q2YEG0; -.
DR   STRING; 9544.ENSMMUP00000065767; -.
DR   GlyCosmos; Q2YEG0; 4 sites, No reported glycans.
DR   PaxDb; 9544-ENSMMUP00000025429; -.
DR   Ensembl; ENSMMUT00000027182.4; ENSMMUP00000025429.2; ENSMMUG00000019351.4.
DR   Ensembl; ENSMMUT00000098782.1; ENSMMUP00000065767.1; ENSMMUG00000019351.4.
DR   GeneID; 692074; -.
DR   KEGG; mcc:692074; -.
DR   CTD; 3577; -.
DR   VEuPathDB; HostDB:ENSMMUG00000019351; -.
DR   VGNC; VGNC:71616; CXCR1.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01050000244848; -.
DR   HOGENOM; CLU_009579_8_3_1; -.
DR   InParanoid; Q2YEG0; -.
DR   OMA; SPVCYEV; -.
DR   OrthoDB; 5347598at2759; -.
DR   TreeFam; TF330966; -.
DR   Proteomes; UP000006718; Chromosome 12.
DR   Bgee; ENSMMUG00000019351; Expressed in spermatid and 5 other cell types or tissues.
DR   ExpressionAtlas; Q2YEG0; baseline.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA: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:0019959; F:interleukin-8 binding; IEA:Ensembl.
DR   GO; GO:0004918; F:interleukin-8 receptor activity; IEA:Ensembl.
DR   GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
DR   GO; GO:0006955; P:immune response; IBA:GO_Central.
DR   GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR   GO; GO:0031623; P:receptor internalization; IEA:Ensembl.
DR   CDD; cd15178; 7tmA_CXCR1_2; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR001355; Chemokine_CXCR1.
DR   InterPro; IPR000174; Chemokine_CXCR_1/2.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR10489:SF916; C-X-C CHEMOKINE RECEPTOR TYPE 1; 1.
DR   PANTHER; PTHR10489; CELL ADHESION MOLECULE; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00427; INTRLEUKIN8R.
DR   PRINTS; PR00572; INTRLEUKN8AR.
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   3: Inferred from homology;
KW   Cell membrane; Chemotaxis; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..351
FT                   /note="C-X-C chemokine receptor type 1"
FT                   /id="PRO_0000237619"
FT   TOPO_DOM        1..46
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        47..67
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        68..76
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..97
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        98..112
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..133
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        134..154
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        155..175
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        176..204
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        205..225
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        226..243
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        244..264
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        265..289
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        290..310
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        311..351
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        3
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        17
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        182
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        194
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        111..188
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   351 AA;  39811 MW;  050FDC46423AD4A1 CRC64;
     MSNATDPQMG DDDYDLNFTG MPPTDEDYSP CRLETQSLNK YVVIVTYALV FLLSLLGNSL
     VMLVILYRRV GRSVTDVYLL NLAMADLLFA LTLPIWAASK VNGWIFGTFL CKVVSLLKEV
     NFYSGILLLA CISVDRYLAI VHATRTLIQK RHSVKFVCLS CWGLSVILSL PFFLFRQAYH
     PNNSTPVCYE VLGNDTAKWR MVLRILPHTF GFTLPLLIML FCYGFTLHTL FKAHIGQKHR
     AMRVIFAVVL IFLLCWLPYN LVLLADTLMR THLIKESCER RNDIGRALDA TEILGFLHSC
     LNPIIYAFIG QNFRHGFLKI LATHGLVSKE FLARHHVTSY TSSSVNVSSN L
//