CXCR3_HUMAN
ID CXCR3_HUMAN Reviewed; 368 AA.
AC P49682; B2R982; O15185; Q7Z710; Q9P2T4; Q9P2T5;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=C-X-C chemokine receptor type 3;
DE Short=CXC-R3;
DE Short=CXCR-3;
DE AltName: Full=CKR-L2;
DE AltName: Full=G protein-coupled receptor 9;
DE AltName: Full=Interferon-inducible protein 10 receptor;
DE Short=IP-10 receptor;
DE AltName: CD_antigen=CD183;
GN Name=CXCR3; Synonyms=GPR9;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Blood;
RX PubMed=9064356; DOI=10.1084/jem.184.3.963;
RA Loetscher M., Gerber B., Loetscher P., Jones S.A., Piali L.,
RA Clark-Lewis I., Baggiolini M., Moser B.;
RT "Chemokine receptor specific for IP10 and mig: structure, function, and
RT expression in activated T-lymphocytes.";
RL J. Exp. Med. 184:963-969(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (ISOFORMS 1 AND 2),
RP SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RX PubMed=12782716; DOI=10.1084/jem.20021897;
RA Lasagni L., Francalanci M., Annunziato F., Lazzeri E., Giannini S.,
RA Cosmi L., Sagrinati C., Mazzinghi B., Orlando C., Maggi E., Marra F.,
RA Romagnani S., Serio M., Romagnani P.;
RT "An alternatively spliced variant of CXCR3 mediates the inhibition of
RT endothelial cell growth induced by IP-10, Mig, and I-TAC, and acts as
RT functional receptor for platelet factor 4.";
RL J. Exp. Med. 197:1537-1549(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND FUNCTION.
RC TISSUE=Endothelial cell, and Thymus;
RX PubMed=18291705; DOI=10.1016/j.biocel.2008.01.008;
RA Petrai I., Rombouts K., Lasagni L., Annunziato F., Cosmi L.,
RA Romanelli R.G., Sagrinati C., Mazzinghi B., Pinzani M., Romagnani S.,
RA Romagnani P., Marra F.;
RT "Activation of p38(MAPK) mediates the angiostatic effect of the chemokine
RT receptor CXCR3-B.";
RL Int. J. Biochem. Cell Biol. 40:1764-1774(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
RA Gutierrez J., Varona R., Zaballos A., Lind P., Marquez G.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Leukocyte;
RA Warren C.N., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Lung, and Testis;
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-368.
RX PubMed=8666380; DOI=10.1006/geno.1995.9996;
RA Marchese A., Heiber M., Nguyen T., Heng H.H.Q., Saldivia V.R., Cheng R.,
RA Murphy P.M., Tsui L.-C., Shi X., Gregor P., George S.R., O'Dowd B.F.,
RA Docherty J.M.;
RT "Cloning and chromosomal mapping of three novel genes, GPR9, GPR10, and
RT GPR14, encoding receptors related to interleukin 8, neuropeptide Y, and
RT somatostatin receptors.";
RL Genomics 29:335-344(1995).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 278-368, AND VARIANTS GLN-292 AND
RP THR-363.
RX PubMed=11196695; DOI=10.1038/sj.gene.6363682;
RA Kato H., Tsuchiya N., Tokunaga K.;
RT "Single nucleotide polymorphisms in the coding regions of human CXC-
RT chemokine receptors CXCR1, CXCR2 and CXCR3.";
RL Genes Immun. 1:330-337(2000).
RN [10]
RP ALTERNATIVE SPLICING (ISOFORM 3), AND FUNCTION.
RX PubMed=15528361; DOI=10.4049/jimmunol.173.10.6234;
RA Ehlert J.E., Addison C.A., Burdick M.D., Kunkel S.L., Strieter R.M.;
RT "Identification and partial characterization of a variant of human CXCR3
RT generated by posttranscriptional exon skipping.";
RL J. Immunol. 173:6234-6240(2004).
RN [11]
RP LIGAND-BINDING.
RC TISSUE=Fetal astrocyte;
RX PubMed=9625760; DOI=10.1084/jem.187.12.2009;
RA Cole K.E., Strick C.A., Paradis T.J., Ogborne K.T., Loetscher M.,
RA Gladue R.P., Lin W., Boyd J.G., Moser B., Wood D.E., Sahagan B.G.,
RA Neote K.;
RT "Interferon-inducible T cell alpha chemoattractant (I-TAC): a novel non-ELR
RT CXC chemokine with potent activity on activated T cells through selective
RT high affinity binding to CXCR3.";
RL J. Exp. Med. 187:2009-2021(1998).
RN [12]
RP SULFATION AT TYR-27, AND MUTAGENESIS OF 1-MET--VAL-16; GLU-4; GLU-21;
RP TYR-27; 27-TYR--TYR-29; TYR-29; ASP-112; ARG-197; ARG-212; ARG-216;
RP ASP-278; ASP-282 AND GLU-293.
RX PubMed=16847335; DOI=10.1128/mcb.00556-06;
RA Colvin R.A., Campanella G.S., Manice L.A., Luster A.D.;
RT "CXCR3 requires tyrosine sulfation for ligand binding and a second
RT extracellular loop arginine residue for ligand-induced chemotaxis.";
RL Mol. Cell. Biol. 26:5838-5849(2006).
RN [13]
RP SULFATION AT TYR-27 AND TYR-29, AND MUTAGENESIS OF TYR-27 AND TYR-29.
RX PubMed=19151743; DOI=10.1038/aps.2008.24;
RA Gao J.M., Xiang R.L., Jiang L., Li W.H., Feng Q.P., Guo Z.J., Sun Q.,
RA Zeng Z.P., Fang F.D.;
RT "Sulfated tyrosines 27 and 29 in the N-terminus of human CXCR3 participate
RT in binding native IP-10.";
RL Acta Pharmacol. Sin. 30:193-201(2009).
RN [14]
RP FUNCTION.
RX PubMed=20855888; DOI=10.1074/jbc.m110.170324;
RA Datta D., Banerjee P., Gasser M., Waaga-Gasser A.M., Pal S.;
RT "CXCR3-B can mediate growth-inhibitory signals in human renal cancer cells
RT by down-regulating the expression of heme oxygenase-1.";
RL J. Biol. Chem. 285:36842-36848(2010).
RN [15]
RP SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=23121557; DOI=10.1111/bph.12042;
RA Vinet J., van Zwam M., Dijkstra I.M., Brouwer N., van Weering H.R.,
RA Watts A., Meijer M., Fokkens M.R., Kannan V., Verzijl D., Vischer H.F.,
RA Smit M.J., Leurs R., Biber K., Boddeke H.W.;
RT "Inhibition of CXCR3-mediated chemotaxis by the human chemokine receptor-
RT like protein CCX-CKR.";
RL Br. J. Pharmacol. 168:1375-1387(2013).
CC -!- FUNCTION: [Isoform 1]: Receptor for the C-X-C chemokine CXCL9, CXCL10
CC and CXCL11 and mediates the proliferation, survival and angiogenic
CC activity of human mesangial cells (HMC) through a heterotrimeric G-
CC protein signaling pathway (PubMed:12782716). Binds to CCL21. Probably
CC promotes cell chemotaxis response. {ECO:0000269|PubMed:12782716}.
CC -!- FUNCTION: [Isoform 2]: Receptor for the C-X-C chemokine CXCL4 and also
CC mediates the inhibitory activities of CXCL9, CXCL10 and CXCL11 on the
CC proliferation, survival and angiogenic activity of human microvascular
CC endothelial cells (HMVEC) through a cAMP-mediated signaling pathway
CC (PubMed:12782716). Does not promote cell chemotaxis respons.
CC Interaction with CXCL4 or CXCL10 leads to activation of the p38MAPK
CC pathway and contributes to inhibition of angiogenesis. Overexpression
CC in renal cancer cells down-regulates expression of the anti-apoptotic
CC protein HMOX1 and promotes apoptosis. {ECO:0000269|PubMed:12782716}.
CC -!- FUNCTION: [Isoform 3]: Mediates the activity of CXCL11.
CC -!- SUBUNIT: Homomer. Forms heteromers with ACKR4.
CC {ECO:0000269|PubMed:23121557}.
CC -!- INTERACTION:
CC P49682; O14523: C2CD2L; NbExp=3; IntAct=EBI-12836456, EBI-12822627;
CC P49682; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-12836456, EBI-12256978;
CC P49682; P61073: CXCR4; NbExp=5; IntAct=EBI-12836456, EBI-489411;
CC P49682; Q9Y6G1: TMEM14A; NbExp=3; IntAct=EBI-12836456, EBI-2800360;
CC P49682-3; Q969F0: FATE1; NbExp=3; IntAct=EBI-16432539, EBI-743099;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:12782716}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12782716}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane
CC {ECO:0000269|PubMed:12782716}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12782716}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=CXCR3-A;
CC IsoId=P49682-1; Sequence=Displayed;
CC Name=2; Synonyms=CXCR3-B;
CC IsoId=P49682-2; Sequence=VSP_015684;
CC Name=3; Synonyms=CXCR3-alt;
CC IsoId=P49682-3; Sequence=VSP_015685;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are mainly expressed in
CC heart, kidney, liver and skeletal muscle. Isoform 1 is also expressed
CC in placenta. Isoform 2 is expressed in endothelial cells. Expressed in
CC T-cells (at protein level). {ECO:0000269|PubMed:12782716,
CC ECO:0000269|PubMed:23121557}.
CC -!- PTM: Sulfation on Tyr-27 and Tyr-29 is essential for CXCL10 binding and
CC subsequent signal transduction induction. {ECO:0000269|PubMed:16847335,
CC ECO:0000269|PubMed:19151743}.
CC -!- PTM: N-glycosylated.
CC -!- MISCELLANEOUS: [Isoform 3]: Due to exon skipping. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CXCR3ID40224chXq13.html";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CXC chemokine receptors entry;
CC URL="https://en.wikipedia.org/wiki/CXC_chemokine_receptors";
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DR EMBL; X95876; CAA65126.1; -; mRNA.
DR EMBL; AF469635; AAP55851.1; -; mRNA.
DR EMBL; Z79783; CAB02143.1; -; Genomic_DNA.
DR EMBL; AY242128; AAO92295.1; -; mRNA.
DR EMBL; AK313679; BAG36429.1; -; mRNA.
DR EMBL; BC034403; AAH34403.1; -; mRNA.
DR EMBL; U32674; AAC50505.1; -; Genomic_DNA.
DR EMBL; AB032735; BAA92297.1; -; Genomic_DNA.
DR EMBL; AB032736; BAA92298.1; -; Genomic_DNA.
DR CCDS; CCDS14416.1; -. [P49682-1]
DR CCDS; CCDS48135.1; -. [P49682-2]
DR RefSeq; NP_001136269.1; NM_001142797.1. [P49682-2]
DR RefSeq; NP_001495.1; NM_001504.1. [P49682-1]
DR RefSeq; XP_016884924.1; XM_017029435.1. [P49682-2]
DR AlphaFoldDB; P49682; -.
DR SMR; P49682; -.
DR BioGRID; 109094; 498.
DR DIP; DIP-5891N; -.
DR IntAct; P49682; 9.
DR STRING; 9606.ENSP00000362795; -.
DR BindingDB; P49682; -.
DR ChEMBL; CHEMBL4441; -.
DR GuidetoPHARMACOLOGY; 70; -.
DR GlyGen; P49682; 2 sites.
DR iPTMnet; P49682; -.
DR PhosphoSitePlus; P49682; -.
DR BioMuta; CXCR3; -.
DR DMDM; 2829400; -.
DR jPOST; P49682; -.
DR MassIVE; P49682; -.
DR PaxDb; P49682; -.
DR PeptideAtlas; P49682; -.
DR PRIDE; P49682; -.
DR ProteomicsDB; 56047; -. [P49682-1]
DR ProteomicsDB; 56048; -. [P49682-2]
DR ProteomicsDB; 56049; -. [P49682-3]
DR Antibodypedia; 566; 1007 antibodies from 45 providers.
DR DNASU; 2833; -.
DR Ensembl; ENST00000373691.4; ENSP00000362795.4; ENSG00000186810.8. [P49682-2]
DR Ensembl; ENST00000373693.4; ENSP00000362797.3; ENSG00000186810.8. [P49682-1]
DR GeneID; 2833; -.
DR KEGG; hsa:2833; -.
DR MANE-Select; ENST00000373693.4; ENSP00000362797.3; NM_001504.2; NP_001495.1.
DR UCSC; uc004eaf.3; human. [P49682-1]
DR CTD; 2833; -.
DR DisGeNET; 2833; -.
DR GeneCards; CXCR3; -.
DR HGNC; HGNC:4540; CXCR3.
DR HPA; ENSG00000186810; Tissue enhanced (bone marrow, intestine, lymphoid tissue).
DR MIM; 300574; gene.
DR neXtProt; NX_P49682; -.
DR OpenTargets; ENSG00000186810; -.
DR PharmGKB; PA35049; -.
DR VEuPathDB; HostDB:ENSG00000186810; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244848; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; P49682; -.
DR OMA; VCISFDR; -.
DR OrthoDB; 794531at2759; -.
DR PhylomeDB; P49682; -.
DR TreeFam; TF330966; -.
DR PathwayCommons; P49682; -.
DR Reactome; R-HSA-380108; Chemokine receptors bind chemokines.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; P49682; -.
DR SIGNOR; P49682; -.
DR BioGRID-ORCS; 2833; 15 hits in 690 CRISPR screens.
DR GeneWiki; CXCR3; -.
DR GenomeRNAi; 2833; -.
DR Pharos; P49682; Tchem.
DR PRO; PR:P49682; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P49682; protein.
DR Bgee; ENSG00000186810; Expressed in granulocyte and 109 other tissues.
DR Genevisible; P49682; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0016494; F:C-X-C chemokine receptor activity; IEA:InterPro.
DR GO; GO:0019956; F:chemokine binding; IPI:BHF-UCL.
DR GO; GO:0004950; F:chemokine receptor activity; TAS:ProtInc.
DR GO; GO:0038023; F:signaling receptor activity; IDA:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0006935; P:chemotaxis; TAS:ProtInc.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IEA:InterPro.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IDA:UniProtKB.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IDA:UniProtKB.
DR GO; GO:1900118; P:negative regulation of execution phase of apoptosis; IDA:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0050921; P:positive regulation of chemotaxis; IDA:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:1900119; P:positive regulation of execution phase of apoptosis; IDA:UniProtKB.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0030155; P:regulation of cell adhesion; IDA:UniProtKB.
DR GO; GO:0002685; P:regulation of leukocyte migration; IEA:InterPro.
DR InterPro; IPR004070; Chemokine_CXCR3.
DR InterPro; IPR000355; Chemokine_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00657; CCCHEMOKINER.
DR PRINTS; PR01532; CXCCHMKINER3.
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 Alternative splicing; Angiogenesis; Apoptosis; Cell membrane; Chemotaxis;
KW Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Sulfation; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..368
FT /note="C-X-C chemokine receptor type 3"
FT /id="PRO_0000069346"
FT TOPO_DOM 1..53
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..80
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..125
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..147
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..189
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..212
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..255
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..277
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..298
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..321
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..368
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 342..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:16847335,
FT ECO:0000269|PubMed:19151743"
FT MOD_RES 29
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:19151743"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 124..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 1..4
FT /note="MVLE -> MELRKYGPGRLAGTVIGGAAQSKSQTKSDSITKEFLPGLYTAPS
FT SPFPPSQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12782716,
FT ECO:0000303|PubMed:18291705"
FT /id="VSP_015684"
FT VAR_SEQ 210..368
FT /note="VGRTALRVLQLVAGFLLPLLVMAYCYAHILAVLLVSRGQRRLRAMRLVVVVV
FT VAFALCWTPYHLVVLVDILMDLGALARNCGRESRVDVAKSVTSGLGYMHCCLNPLLYAF
FT VGVKFRERMWMLLLRLGCPNQRGLQRQPSSSRRDSSWSETSEASYSGL -> GSSSGSG
FT CGCCSCAWAAPTREGSRGSHRLPAGIHPGLRPQRPPTRACEAGIRAPLSPI (in
FT isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_015685"
FT VARIANT 292
FT /note="R -> Q (in dbSNP:rs139226823)"
FT /evidence="ECO:0000269|PubMed:11196695"
FT /id="VAR_016240"
FT VARIANT 363
FT /note="A -> T (in dbSNP:rs766348940)"
FT /evidence="ECO:0000269|PubMed:11196695"
FT /id="VAR_016241"
FT MUTAGEN 1..16
FT /note="Missing: Reduces binding to CXCL10 and CXCL11, and
FT reduces CXCL10- and CXCL11-induced chemotaxis and
FT activation. Does not affect CXCL9-induced chemotaxis and
FT activation."
FT /evidence="ECO:0000269|PubMed:16847335"
FT MUTAGEN 4
FT /note="E->K: Does not affect binding to CXCL9, CXCL10 and
FT CXCL11 or activation."
FT /evidence="ECO:0000269|PubMed:16847335"
FT MUTAGEN 21
FT /note="E->K: Reduces slightly CXCL9-, CXCL10- and CXCL11-
FT induced chemotaxis."
FT /evidence="ECO:0000269|PubMed:16847335"
FT MUTAGEN 27..29
FT /note="YDY->ADA: Abolishes binding to CXCL10 and CXCL11 and
FT CXCL9-, CXCL10- and CXCL11-induced chemotaxis."
FT /evidence="ECO:0000269|PubMed:16847335"
FT MUTAGEN 27
FT /note="Y->F: Reduces sulfation and CXCL9-, CXCL10- and
FT CXCL11-induced chemotaxis. Abolishes binding to CXCL10.
FT Abolishes sulfation, binding to CXCL11, ligand-induced
FT receptor internalization and CXCL9-, CXCL10- and CXCL11-
FT induced chemotaxis; when associated with F-29."
FT /evidence="ECO:0000269|PubMed:16847335,
FT ECO:0000269|PubMed:19151743"
FT MUTAGEN 29
FT /note="Y->F: Reduces sulfation, binding to CXCL10 and
FT CXCL9-, CXCL10- and CXCL11-induced chemotaxis. Abolishes
FT sulfation, binding to CXCL10 and CXCL11 and CXCL9-,
FT CXCL10- and CXCL11-induced chemotaxis; when associated with
FT F-27."
FT /evidence="ECO:0000269|PubMed:16847335,
FT ECO:0000269|PubMed:19151743"
FT MUTAGEN 112
FT /note="D->A: Abolishes binding to CXCL10 and CXCL11.
FT Reduces CXCL9-, CXCL10- and CXCL11-induced chemotaxis."
FT /evidence="ECO:0000269|PubMed:16847335"
FT MUTAGEN 112
FT /note="D->K: Abolishes binding to CXCL10 and CXCL11 and
FT CXCL10- and CXCL11-induced chemotaxis. Reduces CXCL9-
FT induced chemotaxis."
FT /evidence="ECO:0000269|PubMed:16847335"
FT MUTAGEN 197
FT /note="R->A: Abolishes binding to CXCL10 and CXCL11 and
FT CXCL9-, CXCL10- and CXCL11-induced chemotaxis. Reduces
FT ligand-induced receptor internalization."
FT /evidence="ECO:0000269|PubMed:16847335"
FT MUTAGEN 212
FT /note="R->A: Abolishes CXCL10-induced chemotaxis. Reduces
FT CXCL9- and CXCL11-induced chemotaxis. Does not affect
FT binding to CXCL10 and CXCL11."
FT /evidence="ECO:0000269|PubMed:16847335"
FT MUTAGEN 216
FT /note="R->A: Reduces CXCL9-, CXCL10- and CXCL11-induced
FT chemotaxis. Does not affect binding to CXCL10 and CXCL11 or
FT receptor internalization."
FT /evidence="ECO:0000269|PubMed:16847335"
FT MUTAGEN 278
FT /note="D->A: Abolishes binding to CXCL10 and CXCL11 and
FT CXCL11-induced chemotaxis. Reduces CXCL9 and CXCL10-induced
FT chemotaxis."
FT /evidence="ECO:0000269|PubMed:16847335"
FT MUTAGEN 278
FT /note="D->K: Abolishes binding to CXCL10 and CXCL11 and
FT CXCL9-, CXCL10- and CXCL11-induced chemotaxis."
FT /evidence="ECO:0000269|PubMed:16847335"
FT MUTAGEN 282
FT /note="D->A: Reduces binding to CXCL10 and CXCL9-,
FT CXCL10- and CXCL11-induced chemotaxis. Abolishes binding to
FT CXCL11."
FT /evidence="ECO:0000269|PubMed:16847335"
FT MUTAGEN 282
FT /note="D->K: Reduces binding to CXCL10 and CXCL11 and
FT CXCL9-, CXCL10- and CXCL11-induced chemotaxis."
FT /evidence="ECO:0000269|PubMed:16847335"
FT MUTAGEN 293
FT /note="E->A: Reduces binding to CXCL10 and CXCL9- and
FT CXCL11-induced chemotaxis. Abolishes binding to CXCL11 and
FT CXCL10-induced chemotaxis."
FT /evidence="ECO:0000269|PubMed:16847335"
FT MUTAGEN 293
FT /note="E->K: Abolishes binding to CXCL10 and CXCL11 and
FT CXCL9-, CXCL10- and CXCL11-induced chemotaxis."
FT /evidence="ECO:0000269|PubMed:16847335"
FT CONFLICT 75
FT /note="A -> R (in Ref. 4; CAB02143)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="T -> I (in Ref. 6; BAG36429)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 368 AA; 40660 MW; F08A3B44B2BBAD04 CRC64;
MVLEVSDHQV LNDAEVAALL ENFSSSYDYG ENESDSCCTS PPCPQDFSLN FDRAFLPALY
SLLFLLGLLG NGAVAAVLLS RRTALSSTDT FLLHLAVADT LLVLTLPLWA VDAAVQWVFG
SGLCKVAGAL FNINFYAGAL LLACISFDRY LNIVHATQLY RRGPPARVTL TCLAVWGLCL
LFALPDFIFL SAHHDERLNA THCQYNFPQV GRTALRVLQL VAGFLLPLLV MAYCYAHILA
VLLVSRGQRR LRAMRLVVVV VVAFALCWTP YHLVVLVDIL MDLGALARNC GRESRVDVAK
SVTSGLGYMH CCLNPLLYAF VGVKFRERMW MLLLRLGCPN QRGLQRQPSS SRRDSSWSET
SEASYSGL
