CXCR1_GORGO
ID CXCR1_GORGO Reviewed; 350 AA.
AC P55919; P55921; Q2YEG3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 102.
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 Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
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; X91110; CAB37671.1; -; Genomic_DNA.
DR EMBL; AY916767; AAY21517.1; -; Genomic_DNA.
DR AlphaFoldDB; P55919; -.
DR BMRB; P55919; -.
DR SMR; P55919; -.
DR STRING; 9593.ENSGGOP00000008892; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P55919; -.
DR Proteomes; UP000001519; Unplaced.
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: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:0060326; P:cell chemotaxis; 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 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_0000069329"
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; AAY21517)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="S -> G (in Ref. 2; AAY21517)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="T -> S (in Ref. 2; AAY21517)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 350 AA; 39790 MW; DB99591CD6C10757 CRC64;
MSNITDPQMW DFDDLNFTGM PPIDEDYSPC RLETETLNKY VVIITYALAF LLSLLGNSLV
MLVILYSRGG RSVTDVYLLN LALADLLFAL TLPIWAASKV NGWIFGTFLC KVVSLLKEVN
FYSGILLLAC ISVDRYLAIV HATRTLTQKR HLVKFVCLGC WGLSMILSLP FFLFRQAYHP
NNSSPVCYEV LGNDTAKWRM VLRILPHTFG FIVPLFVMLF CYGFTLRTLF KAHMGQKHRA
MRVIFAVVLI FLLCWLPYNL VLLADTLMRT QVIQESCERR NNVSLALDAT EILGFLHSCL
NPIIYAFIGQ NFRHGFLKIL AMHGLVSKEF LARHRVTSYT SSSVNVSSNL
