CXCR1_RAT
ID CXCR1_RAT Reviewed; 349 AA.
AC P70612;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 145.
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 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 [GENOMIC DNA].
RC STRAIN=Wistar; TISSUE=Lung;
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 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}.
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DR EMBL; U71089; AAC52962.1; -; Genomic_DNA.
DR RefSeq; NP_062183.1; NM_019310.1.
DR RefSeq; XP_006245335.2; XM_006245273.3.
DR AlphaFoldDB; P70612; -.
DR SMR; P70612; -.
DR STRING; 10116.ENSRNOP00000066188; -.
DR GlyGen; P70612; 1 site.
DR PhosphoSitePlus; P70612; -.
DR PaxDb; P70612; -.
DR Ensembl; ENSRNOT00000090868; ENSRNOP00000070273; ENSRNOG00000048239.
DR GeneID; 54258; -.
DR KEGG; rno:54258; -.
DR UCSC; RGD:2905; rat.
DR CTD; 3577; -.
DR RGD; 2905; Cxcr1.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244848; -.
DR InParanoid; P70612; -.
DR OMA; CMGIWVV; -.
DR OrthoDB; 865441at2759; -.
DR PhylomeDB; P70612; -.
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:P70612; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000048239; Expressed in lung.
DR Genevisible; P70612; RN.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:RGD.
DR GO; GO:0004918; F:interleukin-8 receptor activity; ISO:RGD.
DR GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
DR GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:RGD.
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:RGD.
DR InterPro; IPR000174; Chemokine_CXCR_1/2.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00427; INTRLEUKIN8R.
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..349
FT /note="C-X-C chemokine receptor type 1"
FT /id="PRO_0000069333"
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..349
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 349 AA; 39945 MW; 9B1CDCE61568EABA CRC64;
MAEAEYFIWI APEGDFEEEF GNITRMLPTG EYFSPCKRVP MTNRQAVVVF YALVFLLSLL
GNSLVMLVIL YRRRTRSVTD VYVLNLAIAD LLFSLTLPFL AVSKWKGWIF GTPLCKMVSL
LKEVNFFSGI LLLACISVDR YLAIVHATRT LTRKRYLVKF VCMGTWGLSL VLSLPFAIFR
QAYKPYRSGT VCYEVLGEAT ADLRITLRGL SHIFGFLLPL FIMLVCYGLT LRTLFKAHMR
QKRRAMWVIF AVVLVFLLCC LPYNLVLLSD TLLGAHLIQD TCERRNNIDQ ALYITEILGF
SHSCLNPVIY AFVGQSFRHE FLKILANLVH KEVLTHHSAS FRTSLTTIY
