ID CXCR1_PANTR Reviewed; 350 AA. AC P55920; Q2YEG9; Q2YEH0; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 08-NOV-2023, entry version 123. 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 Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Pan. OX NCBI_TaxID=9598; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9110929; DOI=10.1007/bf02440993; RA Alvarez V., Coto E., Setien F., Gonzalez S., Gonzalez-Roces S., RA Lopez-Larrea C.; RT "Characterization of interleukin-8 receptors in non-human primates."; RL Immunogenetics 43:261-267(1996). RN [2] 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; 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; X91109; CAB37850.1; -; Genomic_DNA. DR EMBL; AY916760; AAY21510.1; -; Genomic_DNA. DR EMBL; AY916761; AAY21511.1; -; Genomic_DNA. DR RefSeq; NP_001035537.1; NM_001040447.1. DR AlphaFoldDB; P55920; -. DR BMRB; P55920; -. DR SMR; P55920; -. DR STRING; 9598.ENSPTRP00000022066; -. DR GlyCosmos; P55920; 2 sites, No reported glycans. DR PaxDb; 9598-ENSPTRP00000022066; -. DR GeneID; 470645; -. DR KEGG; ptr:470645; -. DR CTD; 3577; -. DR eggNOG; KOG3656; Eukaryota. DR InParanoid; P55920; -. DR OrthoDB; 5347598at2759; -. DR Proteomes; UP000002277; Unplaced. 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:0016494; F:C-X-C chemokine receptor activity; IEA:InterPro. DR GO; GO:0019959; F:interleukin-8 binding; IEA:InterPro. 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 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..350 FT /note="C-X-C chemokine receptor type 1" FT /id="PRO_0000069331" FT TOPO_DOM 1..39 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 40..66 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 67..75 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 76..96 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 97..111 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 112..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..174 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 175..199 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 200..220 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 221..242 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 243..264 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 265..285 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 286..308 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 309..350 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT CARBOHYD 3 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 16 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 110..187 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" FT CONFLICT 5 FT /note="T -> I (in Ref. 2; AAY21510/AAY21511)" FT /evidence="ECO:0000305" FT CONFLICT 12 FT /note="F -> Y (in Ref. 2; AAY21510/AAY21511)" FT /evidence="ECO:0000305" FT CONFLICT 49 FT /note="V -> A (in Ref. 2; AAY21510/AAY21511)" FT /evidence="ECO:0000305" FT CONFLICT 73 FT /note="V -> I (in Ref. 2; AAY21510/AAY21511)" FT /evidence="ECO:0000305" FT CONFLICT 101 FT /note="N -> T (in Ref. 2; AAY21510/AAY21511)" FT /evidence="ECO:0000305" FT CONFLICT 108 FT /note="F -> L (in Ref. 2; AAY21510/AAY21511)" FT /evidence="ECO:0000305" FT CONFLICT 166 FT /note="N -> I (in Ref. 2; AAY21510/AAY21511)" FT /evidence="ECO:0000305" FT CONFLICT 227 FT /note="R -> H (in Ref. 2; AAY21510)" FT /evidence="ECO:0000305" FT CONFLICT 243 FT /note="V -> I (in Ref. 2; AAY21510)" FT /evidence="ECO:0000305" SQ SEQUENCE 350 AA; 39818 MW; A56FD0246EA1D440 CRC64; MSNITDPQMW DFDDLNFTGM PPTDEGYSPC RLETETLNKY VVIITYALVF LLSLLGNSLV MLVILYSRVG RSVTDVYLLN LALADLLFAL TLPIWAASKV NGWIFGTFLC KVVSLLKEVN FYSGILLLAC ISVDRYLAIV HATRTLTQKR HLVKFVCLGC WGLSMNLSLP FFLFRQAYHP NNSSPVCYEV LGNDTAKWRM VLRILPHTFG FIVPLFVMLF CYGFTLRTLF KAHMGQKHRA MRVIFAVVLI FLLCWLPYNL VLLADTLMRT QVIQESCERR NNIGRALDAT EILGFLHSCL NPIIYAFIGQ NFRHGFLKIL AMHGLVSKEF LARHRVTSYT SSSVNVSSNL //