ID CXCR2_PANTR Reviewed; 357 AA.
AC Q28807; Q8HZN8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 24-JAN-2024, entry version 130.
DE RecName: Full=C-X-C chemokine receptor type 2;
DE Short=CXC-R2;
DE Short=CXCR-2;
DE AltName: Full=High affinity interleukin-8 receptor B;
DE Short=IL-8R B;
DE AltName: CD_antigen=CD182;
DE Flags: Fragment;
GN Name=CXCR2; Synonyms=IL8RB;
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] OF 1-353.
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] OF 3-357.
RA Horlick R.A., Zhao J., Swanson R.N., Webb M.L., Strohl B., Baldwin J.J.,
RA Auld D.S.;
RT "Orthologs of human receptors and methods of use.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for interleukin-8 which is a powerful neutrophil
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. Binds
CC to IL-8 with high affinity. Also binds with high affinity to CXCL3,
CC GRO/MGSA and NAP-2. {ECO:0000250|UniProtKB:P25025}.
CC -!- SUBUNIT: Interacts with IL8. Interacts with GNAI2.
CC {ECO:0000250|UniProtKB:P25025}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- PTM: Phosphorylated upon ligand binding; which is required for
CC desensitization. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; X91113; CAA62563.1; -; Genomic_DNA.
DR EMBL; AF540789; AAN17315.1; -; Genomic_DNA.
DR AlphaFoldDB; Q28807; -.
DR SMR; Q28807; -.
DR STRING; 9598.ENSPTRP00000076345; -.
DR GlyCosmos; Q28807; 1 site, No reported glycans.
DR PaxDb; 9598-ENSPTRP00000022068; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q28807; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
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: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 CDD; cd15178; 7tmA_CXCR1_2; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR000057; Chemokine_CXCR2.
DR InterPro; IPR000174; Chemokine_CXCR_1/2.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR10489:SF689; C-X-C CHEMOKINE RECEPTOR TYPE 2; 1.
DR PANTHER; PTHR10489; CELL ADHESION MOLECULE; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00427; INTRLEUKIN8R.
DR PRINTS; PR00573; INTRLEUKN8BR.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
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; Phosphoprotein; Receptor; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN <1..357
FT /note="C-X-C chemokine receptor type 2"
FT /id="PRO_0000069340"
FT TOPO_DOM <1..45
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..72
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..117
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..139
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..180
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..205
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..228
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..270
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 271..291
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..357
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 116..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 210
FT /note="I -> M (in Ref. 2; CAA62563)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="D -> N (in Ref. 2; CAA62563)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 357 AA; 40384 MW; 6C6E44CD9426CFF7 CRC64;
FNMESDSFED FWKGEDLSNY SYSSTLPPFL LDAAPCEPES LEINKYFVVI IYALVFLLSL
LGNSLVMLVI LYSRVGRSVT DVYLLNLALA DLLFALTLPI WAASKVNGWI FGTFLCKVVS
LLKEVNFYSG ILLLACISVD RYLAIVHATR TLTQKRYLVK FICLSIWGLS LLLALPVLLF
RRTVYSSNVS PACYEDMGNN TANWRMLLRI LPQSFGFIVP LLIMLFCYGF TLRTLFKAHM
GQKHRAMRVI FAVVLIFLLC WLPYNLVLLA DTLMRTQVIQ ETCERRNHID RALDATEILG
ILHSCLNPLI YAFIGQKFRH GLLKILAIHG LISKDSLPKD SRPSFVGSSS GHTSTTL
//
