CXCR6_MOUSE
ID CXCR6_MOUSE Reviewed; 351 AA.
AC Q9EQ16; Q4VA95; Q9ERH5;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=C-X-C chemokine receptor type 6;
DE Short=CXC-R6;
DE Short=CXCR-6;
DE AltName: CD_antigen=CD186;
GN Name=Cxcr6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=C57BL/6J;
RX PubMed=11017100; DOI=10.1038/79738;
RA Matloubian M., David A., Engel S., Ryan J.E., Cyster J.G.;
RT "A transmembrane CXC chemokine is a ligand for HIV-coreceptor Bonzo.";
RL Nat. Immunol. 1:298-304(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RA Sato H., Taniguchi M.;
RT "Molecular cloning of a putative chemokine receptor preferentially
RT expressed in mouse lymphocytes.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Heart, Thymus, and Vagina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6NCr; TISSUE=Hematopoietic stem cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 116-145, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
CC -!- FUNCTION: Receptor for the C-X-C chemokine CXCL16.
CC {ECO:0000269|PubMed:11017100}.
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; AF301018; AAG34367.1; -; mRNA.
DR EMBL; AF305709; AAG31284.1; -; mRNA.
DR EMBL; AK052901; BAC35196.1; -; mRNA.
DR EMBL; AK137703; BAE23469.1; -; mRNA.
DR EMBL; AK153914; BAE32252.1; -; mRNA.
DR EMBL; BC096491; AAH96491.1; -; mRNA.
DR CCDS; CCDS23664.1; -.
DR RefSeq; NP_109637.3; NM_030712.4.
DR AlphaFoldDB; Q9EQ16; -.
DR SMR; Q9EQ16; -.
DR BioGRID; 219838; 1.
DR STRING; 10090.ENSMUSP00000060776; -.
DR BindingDB; Q9EQ16; -.
DR ChEMBL; CHEMBL4630853; -.
DR GlyGen; Q9EQ16; 2 sites.
DR PhosphoSitePlus; Q9EQ16; -.
DR EPD; Q9EQ16; -.
DR PaxDb; Q9EQ16; -.
DR PRIDE; Q9EQ16; -.
DR ProteomicsDB; 277930; -.
DR Antibodypedia; 12723; 726 antibodies from 44 providers.
DR DNASU; 80901; -.
DR Ensembl; ENSMUST00000049810; ENSMUSP00000060776; ENSMUSG00000048521.
DR GeneID; 80901; -.
DR KEGG; mmu:80901; -.
DR UCSC; uc009sgt.2; mouse.
DR CTD; 10663; -.
DR MGI; MGI:1934582; Cxcr6.
DR VEuPathDB; HostDB:ENSMUSG00000048521; -.
DR eggNOG; ENOG502QSJQ; Eukaryota.
DR GeneTree; ENSGT01030000234667; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; Q9EQ16; -.
DR OrthoDB; 886529at2759; -.
DR PhylomeDB; Q9EQ16; -.
DR TreeFam; TF330966; -.
DR Reactome; R-MMU-380108; Chemokine receptors bind chemokines.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 80901; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q9EQ16; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9EQ16; protein.
DR Bgee; ENSMUSG00000048521; Expressed in peripheral lymph node and 63 other tissues.
DR ExpressionAtlas; Q9EQ16; baseline and differential.
DR Genevisible; Q9EQ16; MM.
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:0019958; F:C-X-C chemokine binding; IPI:UniProtKB.
DR GO; GO:0016494; F:C-X-C chemokine receptor activity; IDA:MGI.
DR GO; GO:0015026; F:coreceptor activity; 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:0006954; P:inflammatory response; IEA:InterPro.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR CDD; cd15173; 7tmA_CXCR6; 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; PTHR10489:SF705; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00657; CCCHEMOKINER.
DR PRINTS; PR01105; CXCCHMKINER6.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..351
FT /note="C-X-C chemokine receptor type 6"
FT /id="PRO_0000303230"
FT TOPO_DOM 1..41
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..68
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..112
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..134
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..196
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..224
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..268
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..284
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..302
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 111..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 119
FT /note="T -> A (in Ref. 4; AAH96491)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="L -> R (in Ref. 2; AAG31284)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="R -> W (in Ref. 4; AAH96491)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="L -> Q (in Ref. 4; AAH96491)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="S -> P (in Ref. 4; AAH96491)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 351 AA; 40468 MW; 5658788372B4C65A CRC64;
MDDGHQESAL YDGHYEGDFW LFNNSSDNSQ ENKRFLKFKE VFLPCVYLVV FVFGLLGNSL
VLIIYIFYQK LRTLTDVFLL NLPLADLVFV CTLPFWAYAG TYEWVFGTVM CKTLRGMYTM
NFYVSMLTLT CITVDRFIVV VQATKAFNRQ AKWKIWGQVI CLLIWVVSLL VSLPQIIYGH
VQDIDKLICQ YHSEEISTMV LVIQMTLGFF LPLLTMILCY SGIIKTLLHA RNFQKHKSLK
IIFLVVAVFL LTQTPFNLAM LIQSTSWEYY TITSFKYAIV VTEAIAYFRA CLNPVLYAFV
GLKFRKNVWK LMKDIGCLSH LGVSSQWKSS EDSSKTCSAS HNVETTSMFQ L
