CXCR2_GORGO
ID CXCR2_GORGO Reviewed; 353 AA.
AC Q28422;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 99.
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 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).
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}.
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; X91114; CAA62564.1; -; Genomic_DNA.
DR AlphaFoldDB; Q28422; -.
DR SMR; Q28422; -.
DR STRING; 9593.ENSGGOP00000008894; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q28422; -.
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; IPR000057; Chemokine_CXCR2.
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; PR00573; INTRLEUKN8BR.
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..>353
FT /note="C-X-C chemokine receptor type 2"
FT /id="PRO_0000069336"
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..>353
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 NON_TER 1
FT NON_TER 353
SQ SEQUENCE 353 AA; 39919 MW; 1FF04E31A7E825E4 CRC64;
FNMESDSFED FWKGEDLSNY SYSSALPPFL LDASPCEPES LEINKYFVVI IYALVFLLSL
LGNSLVILVI LYSRVGRSVT DVYLLNLALA DLLFALTLPI WAASKVNGWI FGTFLCKVVS
LLKEVNFYSG ILLLACISVD RYLAIVHATR TLTQKRYLVK FICLSIWGLS LLLALPVLLF
RRTIYPSNVS PVCYEDMGNN TANWRMLLRI LPQSFGFIVP LLIMLFCYGF TLRTLFKAHM
GQKHRAMRVI FAVVLIFLLC WLPYNLVLLA DTLMRTQVIQ ETCERRNHIN QALDATEILG
ILHSCLNPLI YAFIGQKFCH GLLKILAIHG LISKDSLPKD SRPSFVGSSS GHT
