CXCR1_HOOHO
ID CXCR1_HOOHO Reviewed; 351 AA.
AC Q2YEG2;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 57.
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 Hoolock hoolock (Western hoolock gibbon) (Bunopithecus hoolock).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Hoolock.
OX NCBI_TaxID=61851;
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; AY916768; AAY21518.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2YEG2; -.
DR SMR; Q2YEG2; -.
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 3: Inferred from homology;
KW Cell membrane; Chemotaxis; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..351
FT /note="C-X-C chemokine receptor type 1"
FT /id="PRO_0000237618"
FT TOPO_DOM 1..41
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..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 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; 40048 MW; F4116B2A5A1E111E CRC64;
MWNITDPQGW DYDGDLYFTG MPPIDEDFSP CKLETETLNK YVVIITYALV FLLSLLGNSL
VMLVILYSRV GRSVTDIYLL NLALADLLFA LTLPIWAASK VNGWIFGTFL CKVVSLLKEV
NFYSGILLLA CISVDRYLAI VHATRTLTQK RHLVKFVCVG CWGLSMILSL PFFLFRQAYH
PNNSSPVCYE VLGNDTAKWR MVLRILPHTF GFIVPLLVML FCYGFTLHTL FKAHMGQKHR
AMRVVFAVVL IFLLCWLPYN LVLFTDTLMR TQLIKESCER RKDISKALEA TEILGFFHSC
LNPIIYAFIG QNFRHGFLKI LAMHGLVSKE FLARHHVTSY TSSSVNVSSN L
