CXCR2_CANLF
ID CXCR2_CANLF Reviewed; 356 AA.
AC O97571;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 121.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Beagle;
RX PubMed=10647821; DOI=10.3109/10425179909033945;
RA Chang Y.F., Novosel V., Chang C.F.;
RT "The isolation and sequence of canine interleukin-8 receptor.";
RL DNA Seq. 10:183-187(1999).
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; AF047047; AAC98968.1; -; mRNA.
DR AlphaFoldDB; O97571; -.
DR SMR; O97571; -.
DR STRING; 9615.ENSCAFP00000021547; -.
DR PaxDb; O97571; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; O97571; -.
DR Proteomes; UP000002254; 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 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..356
FT /note="C-X-C chemokine receptor type 2"
FT /id="PRO_0000069335"
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..269
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..290
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..356
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 356 AA; 40505 MW; 2B67DD4E8DD39B15 CRC64;
MEYINWDNYS LEDLFGDIDN YTYNTEMPII PADSAPCRPE SLDINKYAVV VIYVLVFVLN
LLGNSLVIMV VLYSRVSHSV TDVYLLNLAI ADLLFALTLP IWAVSKVKGW IFGTPLCKIV
SLLKEVNFYS GILLLASISM DRYLAIVHAT RRLTQKKHWV KFICLGIWAL SLILSLPIFV
FRRAINPPYS SPVCYEDMGT NTTKLRIVMR ALPQTFGFIV PLMIMLFCYG LTLRTLFEAH
MGQKHRAMRV IFAVVLVFLL CWLPYNLVAD TLMRLQAIEE TCQRRNDIGR ALDATEILGF
FHSCLNPLIY AFIGQKFRHG LLKIMAFHGL ISKEYLPKDS RPSFVGSSSA NTSTTF
