CXCR1_RABIT
ID CXCR1_RABIT Reviewed; 355 AA.
AC P21109;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 2.
DT 03-AUG-2022, entry version 119.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1898400; DOI=10.1016/0006-291x(91)91885-g;
RA Beckmann M.P., Munger W.E., Kozlosky C., Vanden Bos T., Price V., Lyman S.,
RA Gerard N.P., Gerard C., Cerretti D.P.;
RT "Molecular characterization of the interleukin-8 receptor.";
RL Biochem. Biophys. Res. Commun. 179:784-789(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Albino; TISSUE=Neutrophil;
RX PubMed=1700779; DOI=10.1016/s0021-9258(17)30465-9;
RA Thomas K.M., Pyun H.Y., Navarro J.;
RT "Molecular cloning of the fMet-Leu-Phe receptor from neutrophils.";
RL J. Biol. Chem. 265:20061-20064(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Neutrophil;
RX PubMed=1737938;
RA Lee J., Kuang W.-J., Rice G.C., Wood W.I.;
RT "Characterization of complementary DNA clones encoding the rabbit IL-8
RT receptor.";
RL J. Immunol. 148:1261-1264(1992).
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 -!- TISSUE SPECIFICITY: Neutrophils.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- CAUTION: Was originally thought to be the receptor for fMet-Leu-Phe (N-
CC formyl peptide receptor). {ECO:0000305|PubMed:1700779}.
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DR EMBL; M74240; AAA31375.1; -; Genomic_DNA.
DR EMBL; M58021; AAA31377.1; -; mRNA.
DR EMBL; M82873; AAA31376.1; -; mRNA.
DR PIR; A23669; A23669.
DR PIR; JQ1231; JQ1231.
DR RefSeq; NP_001164553.1; NM_001171082.1.
DR RefSeq; XP_017198124.1; XM_017342635.1.
DR AlphaFoldDB; P21109; -.
DR SMR; P21109; -.
DR Ensembl; ENSOCUT00000015104; ENSOCUP00000027727; ENSOCUG00000015108.
DR GeneID; 100328622; -.
DR KEGG; ocu:100328622; -.
DR CTD; 3577; -.
DR GeneTree; ENSGT01050000244848; -.
DR InParanoid; P21109; -.
DR OrthoDB; 865441at2759; -.
DR Proteomes; UP000001811; Chromosome 7.
DR Bgee; ENSOCUG00000015108; Expressed in blood and 19 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR InterPro; IPR001355; Chemokine_CXCR1.
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 PRINTS; PR00572; INTRLEUKN8AR.
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; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..355
FT /note="C-X-C chemokine receptor type 1"
FT /id="PRO_0000069332"
FT TOPO_DOM 1..40
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..67
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..92
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..114
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..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..184
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..204
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..232
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..247
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..270
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 271..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..355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 7
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 115..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 90..111
FT /note="DLLFALTMPIWAVSKEKGWIFG -> PAFCPDHAYLGRLQGKRLDFR (in
FT Ref. 2; AAA31377)"
FT /evidence="ECO:0000305"
FT CONFLICT 146..147
FT /note="HA -> QS (in Ref. 2; AAA31377)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="R -> C (in Ref. 2; AAA31377)"
FT /evidence="ECO:0000305"
FT CONFLICT 287..288
FT /note="DI -> EL (in Ref. 2; AAA31377)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 355 AA; 40622 MW; EFE49ACB9D1E0F21 CRC64;
MEVNVWNMTD LWTWFEDEFA NATGMPPVEK DYSPCLVVTQ TLNKYVVVVI YALVFLLSLL
GNSLVMLVIL YSRSNRSVTD VYLLNLAMAD LLFALTMPIW AVSKEKGWIF GTPLCKVVSL
VKEVNFYSGI LLLACISVDR YLAIVHATRT LTQKRHLVKF ICLGIWALSL ILSLPFFLFR
QVFSPNNSSP VCYEDLGHNT AKWRMVLRIL PHTFGFILPL LVMLFCYGFT LRTLFQAHMG
QKHRAMRVIF AVVLIFLLCW LPYNLVLLAD TLMRTHVIQE TCQRRNDIDR ALDATEILGF
LHSCLNPIIY AFIGQNFRNG FLKMLAARGL ISKEFLTRHR VTSYTSSSTN VPSNL