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Database: UniProt
Entry: Q9BDS6
LinkDB: Q9BDS6
Original site: Q9BDS6 
ID   CXCR6_MACFA             Reviewed;         343 AA.
AC   Q9BDS6;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   24-JAN-2024, entry version 97.
DE   RecName: Full=C-X-C chemokine receptor type 6;
DE            Short=CXC-R6;
DE            Short=CXCR-6;
DE   AltName: Full=G-protein coupled receptor STRL33;
DE   AltName: Full=G-protein coupled receptor bonzo;
DE   AltName: CD_antigen=CD186;
GN   Name=CXCR6; Synonyms=BONZO, STRL33;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11242524; DOI=10.1089/08892220150503744;
RA   Wade-Evans A.M., Russell J., Jenkins A., Javan C.;
RT   "Cloning and sequencing of cynomolgus macaque CCR3, GPR15, and STRL33:
RT   potential coreceptors for HIV type 1, HIV type 2, and SIV.";
RL   AIDS Res. Hum. Retroviruses 17:371-375(2001).
CC   -!- FUNCTION: Receptor for the C-X-C chemokine CXCL16. Used as a coreceptor
CC       by SIVs and by strains of HIV-2 and m-tropic HIV-1.
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; AF291671; AAK25742.1; -; mRNA.
DR   RefSeq; NP_001306326.1; NM_001319397.1.
DR   AlphaFoldDB; Q9BDS6; -.
DR   SMR; Q9BDS6; -.
DR   STRING; 9541.ENSMFAP00000045217; -.
DR   GlyCosmos; Q9BDS6; 1 site, No reported glycans.
DR   eggNOG; ENOG502QSJQ; Eukaryota.
DR   OrthoDB; 5322216at2759; -.
DR   Proteomes; UP000233100; Unplaced.
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:0015026; F:coreceptor activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   GO; GO:0006954; P:inflammatory response; IEA:InterPro.
DR   CDD; cd15173; 7tmA_CXCR6; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR002235; Chemokine_CXCR6.
DR   InterPro; IPR000355; Chemokine_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR10489:SF705; C-X-C CHEMOKINE RECEPTOR TYPE 6; 1.
DR   PANTHER; PTHR10489; CELL ADHESION MOLECULE; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00657; CCCHEMOKINER.
DR   PRINTS; PR01105; CXCCHMKINER6.
DR   PRINTS; PR00237; GPCRRHODOPSN.
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   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..343
FT                   /note="C-X-C chemokine receptor type 6"
FT                   /id="PRO_0000069366"
FT   TOPO_DOM        1..33
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        34..60
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        61..69
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        70..90
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        91..104
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        105..126
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        127..144
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..165
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        166..188
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..216
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        217..232
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..260
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        261..276
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        277..294
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        295..343
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        17
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        103..181
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   343 AA;  39473 MW;  0961328F948E7784 CRC64;
     MAEYDHYEDD GFLNSFNDSS QEEHQDFLQF RKVFLPCMYL VVFVCGLVGN SLVLVISIFY
     HKLQSLTDVF LVNLPLADLV FVCTLPFWTY AGIHEWIFGQ VMCKTLLGVY TINFYTSMLI
     LTCITVDRFI VVVKATKAYN QQAKRMTWGK VICLLIWVIS LLVSLPQIIY GNVFNLDKLI
     CGYHDEEIST VVLATQMTLG FFLPLLAMIV CYSVIIKTLL HAGGFQKHRS LKIIFLVMAV
     FLLTQTPFNL VKLIRSTRWE YYAMTSFHYT IIVTEAIAYL RACLNPVLYA FVSLKFRKNF
     WKLVKDIGCL PYLGVSHQWK SSEDNSKTFS ASHNVEATSM FQL
//
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