ID CXCR1_MOUSE Reviewed; 351 AA. AC Q810W6; DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 24-JAN-2024, entry version 146. 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: CD_antigen=CD181; GN Name=Cxcr1; Synonyms=Il8ra; 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 [MRNA]. RA Xiong S.S., Hickey G.E., Humphrey J.E.; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/cJ; RX PubMed=15967374; DOI=10.1016/j.cyto.2005.02.005; RA Fu W., Zhang Y., Zhang J., Chen W.F.; RT "Cloning and characterization of mouse homolog of the CXC chemokine RT receptor CXCR1."; RL Cytokine 31:9-17(2005). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; RX PubMed=16084593; DOI=10.1016/j.molimm.2005.06.043; RA Moepps B., Nuesseler E., Braun M., Gierschik P.; RT "A homolog of the human chemokine receptor CXCR1 is expressed in the RT mouse."; RL Mol. Immunol. 43:897-914(2006). RN [4] RP PROTEIN SEQUENCE OF 340-351, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. 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; Multi-pass membrane protein. 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; AY227797; AAO72727.1; -; mRNA. DR EMBL; AY749637; AAU87365.1; -; mRNA. DR EMBL; AY390263; AAQ84305.1; -; mRNA. DR CCDS; CCDS15041.1; -. DR RefSeq; NP_839972.1; NM_178241.4. DR RefSeq; XP_011236803.1; XM_011238501.2. DR RefSeq; XP_011236805.1; XM_011238503.2. DR AlphaFoldDB; Q810W6; -. DR SMR; Q810W6; -. DR STRING; 10090.ENSMUSP00000139555; -. DR GlyCosmos; Q810W6; 1 site, No reported glycans. DR GlyGen; Q810W6; 1 site. DR PhosphoSitePlus; Q810W6; -. DR EPD; Q810W6; -. DR PaxDb; 10090-ENSMUSP00000139555; -. DR Antibodypedia; 4267; 681 antibodies from 47 providers. DR DNASU; 227288; -. DR Ensembl; ENSMUST00000053389.5; ENSMUSP00000049714.5; ENSMUSG00000048480.6. DR Ensembl; ENSMUST00000190313.2; ENSMUSP00000139555.2; ENSMUSG00000048480.6. DR GeneID; 227288; -. DR KEGG; mmu:227288; -. DR UCSC; uc007blm.1; mouse. DR AGR; MGI:2448715; -. DR CTD; 3577; -. DR MGI; MGI:2448715; Cxcr1. DR VEuPathDB; HostDB:ENSMUSG00000048480; -. DR eggNOG; KOG3656; Eukaryota. DR GeneTree; ENSGT01050000244848; -. DR HOGENOM; CLU_009579_8_3_1; -. DR InParanoid; Q810W6; -. DR OMA; SPVCYEV; -. DR OrthoDB; 5347598at2759; -. DR PhylomeDB; Q810W6; -. 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; 227288; 1 hit in 77 CRISPR screens. DR ChiTaRS; Cxcr2; mouse. DR PRO; PR:Q810W6; -. DR Proteomes; UP000000589; Chromosome 1. DR RNAct; Q810W6; Protein. DR Bgee; ENSMUSG00000048480; Expressed in granulocyte and 5 other cell types or tissues. 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; ISO:MGI. DR GO; GO:0004918; F:interleukin-8 receptor activity; ISO:MGI. DR GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central. DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:MGI. 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; ISO:MGI. DR CDD; cd15178; 7tmA_CXCR1_2; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. 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 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 1: Evidence at protein level; KW Cell membrane; Chemotaxis; Direct protein sequencing; Disulfide bond; KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Reference proteome; Transducer; Transmembrane; Transmembrane helix. FT CHAIN 1..351 FT /note="C-X-C chemokine receptor type 1" FT /id="PRO_0000277473" FT TOPO_DOM 1..44 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 45..71 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 72..80 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 81..101 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 102..116 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 117..138 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 139..159 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 160..179 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 180..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..247 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 248..269 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 270..290 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 291..313 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 314..351 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT CARBOHYD 22 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 115..192 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" SQ SEQUENCE 351 AA; 40032 MW; E4B73073A72B8B13 CRC64; MAEAEYFIWT NPEGDFEKEF GNITGMLPTG DYFIPCKRVP ITNRQALVVF YALVSLLSLL GNSLVMLVIL YRRRTRSVMD VYVLNLAIAD LLFSLTLPFL AVSKLKGWIF GTPLCKMVSL LKEFNFFSGI LLLACISVDR YLAIVHATRT LARKRYLVKF VCVGIWGLSL ILSLPFAIFR QAYKPFRSGT VCYEVLGEAT TDFRMTLRGL SHIFGFLLPL LTMLVCYGLT LRMLFKTHMR QKHRAMGVIF AVVLVFLLCC LPYNLVLLSD TLLGAHLIED TCERRNDIDQ ALYITEILGF SHSCLNPIIY AFVGQNFRHE FLKILANHGL VRKEVLTHRR VAFHTSLTAI Y //