CXCR1_PANTR
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 03-AUG-2022, entry version 118.
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}.
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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 PaxDb; P55920; -.
DR GeneID; 470645; -.
DR KEGG; ptr:470645; -.
DR CTD; 3577; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P55920; -.
DR Proteomes; UP000002277; Unplaced.
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; 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
