CXCR2_RABIT
ID CXCR2_RABIT Reviewed; 358 AA.
AC P35344;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=C-X-C chemokine receptor type 2;
DE Short=CXC-R2;
DE Short=CXCR-2;
DE AltName: Full=GRO/MGSA receptor;
DE AltName: Full=High affinity interleukin-8 receptor B;
DE Short=IL-8R B;
DE AltName: CD_antigen=CD182;
GN Name=CXCR2; Synonyms=IL8RB;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Albino; TISSUE=Blood;
RX PubMed=8175642; DOI=10.1016/s0021-9258(18)99883-2;
RA Prado G.N., Thomas K.M., Suzuki H., Larosa G.J., Wilkinson N.C., Folco E.,
RA Navarro J.;
RT "Molecular characterization of a novel rabbit interleukin-8 receptor
RT isotype.";
RL J. Biol. Chem. 269:12391-12394(1994).
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 -!- TISSUE SPECIFICITY: Expressed preferentially in neutrophils.
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; L24445; AAA31378.1; -; mRNA.
DR PIR; A53752; A53752.
DR RefSeq; NP_001164561.1; NM_001171090.1.
DR AlphaFoldDB; P35344; -.
DR SMR; P35344; -.
DR BindingDB; P35344; -.
DR ChEMBL; CHEMBL1075198; -.
DR PRIDE; P35344; -.
DR GeneID; 100328627; -.
DR KEGG; ocu:100328627; -.
DR CTD; 3579; -.
DR InParanoid; P35344; -.
DR OrthoDB; 865441at2759; -.
DR PRO; PR:P35344; -.
DR Proteomes; UP000001811; 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; 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 2: Evidence at transcript level;
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..358
FT /note="C-X-C chemokine receptor type 2"
FT /id="PRO_0000069341"
FT TOPO_DOM 1..46
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..73
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..118
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..140
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..181
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..206
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..229
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..271
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..292
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..358
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 117..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 358 AA; 40632 MW; 6899716944D6126A CRC64;
MQEFTWENYS YEDFFGDFSN YSYSTDLPPT LLDSAPCRSE SLETNSYVVL ITYILVFLLS
LLGNSLVMLV ILYSRSTCSV TDVYLLNLAI ADLLFATTLP IWAASKVHGW TFGTPLCKVV
SLVKEVNFYS GILLLACISV DRYLAIVHAT RTMIQKRHLV KFICLSMWGV SLILSLPILL
FRNAIFPPNS SPVCYEDMGN STAKWRMVLR ILPQTFGFIL PLLVMLFCYV FTLRTLFQAH
MGQKHRAMRV IFAVVLIFLL CWLPYNLVLL TDTLMRTHVI QETCERRNDI DRALDATEIL
GFLHSCLNPI IYAFIGQKFR YGLLKILAAH GLISKEFLAK ESRPSFVASS SGNTSTTL
