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P49682

- CXCR3_HUMAN

UniProt

P49682 - CXCR3_HUMAN

Protein

C-X-C chemokine receptor type 3

Gene

CXCR3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Isoform 1: Receptor for the C-X-C chemokine CXCL9, CXCL10 and CXCL11 and mediates the proliferation, survival and angiogenic activity of human mesangial cells (HMC) through a heterotrimeric G-protein signaling pathway (PubMed:12782716). Binds to CCL21. Probably promotes cell chemotaxis response.1 Publication
    Isoform 2: Receptor for the C-X-C chemokine CXCL4 and also mediates the inhibitory activities of CXCL9, CXCL10 and CXCL11 on the proliferation, survival and angiogenic activity of human microvascular endothelial cells (HMVEC) through a cAMP-mediated signaling pathway (PubMed:12782716). Does not promote cell chemotaxis respons. Interaction with CXCL4 or CXCL10 leads to activation of the p38MAPK pathway and contributes to inhibition of angiogenesis. Overexpression in renal cancer cells down-regulates expression of the anti-apoptotic protein HMOX1 and promotes apoptosis.1 Publication
    Isoform 3: Mediates the activity of CXCL11.

    GO - Molecular functioni

    1. chemokine binding Source: BHF-UCL
    2. chemokine receptor activity Source: ProtInc
    3. C-X-C chemokine binding Source: UniProtKB
    4. C-X-C chemokine receptor activity Source: Ensembl
    5. receptor activity Source: UniProtKB

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. apoptotic process Source: UniProtKB-KW
    3. calcium-mediated signaling Source: Ensembl
    4. cell adhesion Source: ProtInc
    5. cell surface receptor signaling pathway Source: BHF-UCL
    6. cellular component movement Source: ProtInc
    7. chemokine (C-C motif) ligand 11 production Source: UniProtKB
    8. chemotaxis Source: ProtInc
    9. G-protein coupled receptor signaling pathway Source: UniProtKB
    10. inflammatory response Source: InterPro
    11. negative regulation of angiogenesis Source: UniProtKB
    12. negative regulation of endothelial cell proliferation Source: UniProtKB
    13. negative regulation of execution phase of apoptosis Source: UniProtKB
    14. positive regulation of angiogenesis Source: UniProtKB
    15. positive regulation of cAMP-mediated signaling Source: UniProtKB
    16. positive regulation of cAMP metabolic process Source: UniProtKB
    17. positive regulation of cell proliferation Source: UniProtKB
    18. positive regulation of chemotaxis Source: UniProtKB
    19. positive regulation of cytosolic calcium ion concentration Source: ProtInc
    20. positive regulation of execution phase of apoptosis Source: UniProtKB
    21. positive regulation of release of sequestered calcium ion into cytosol Source: UniProtKB
    22. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    23. regulation of leukocyte migration Source: InterPro
    24. T cell chemotaxis Source: Ensembl

    Keywords - Molecular functioni

    G-protein coupled receptor, Receptor, Transducer

    Keywords - Biological processi

    Angiogenesis, Apoptosis, Chemotaxis

    Enzyme and pathway databases

    ReactomeiREACT_15344. Chemokine receptors bind chemokines.
    REACT_19231. G alpha (i) signalling events.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    C-X-C chemokine receptor type 3
    Short name:
    CXC-R3
    Short name:
    CXCR-3
    Alternative name(s):
    CKR-L2
    G protein-coupled receptor 9
    Interferon-inducible protein 10 receptor
    Short name:
    IP-10 receptor
    CD_antigen: CD183
    Gene namesi
    Name:CXCR3
    Synonyms:GPR9
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:4540. CXCR3.

    Subcellular locationi

    Isoform 1 : Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication
    Isoform 2 : Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. external side of plasma membrane Source: Ensembl
    3. integral component of plasma membrane Source: ProtInc
    4. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1 – 1616Missing: Reduces binding to CXCL10 and CXCL11, and reduces CXCL10- and CXCL11-induced chemotaxis and activation. Does not affect CXCL9-induced chemotaxis and activation. Add
    BLAST
    Mutagenesisi4 – 41E → K: Does not affect binding to CXCL9, CXCL10 and CXCL11 or activation. 1 Publication
    Mutagenesisi21 – 211E → K: Reduces slightly CXCL9-, CXCL10- and CXCL11-induced chemotaxis. 1 Publication
    Mutagenesisi27 – 293YDY → ADA: Abolishes binding to CXCL10 and CXCL11 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis. 2 Publications
    Mutagenesisi27 – 271Y → F: Reduces sulfation and CXCL9-, CXCL10- and CXCL11-induced chemotaxis. Abolishes binding to CXCL10. Abolishes sulfation, binding to CXCL11, ligand-induced receptor internalization and CXCL9-, CXCL10- and CXCL11-induced chemotaxis; when associated with F-29. 2 Publications
    Mutagenesisi29 – 291Y → F: Reduces sulfation, binding to CXCL10 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis. Abolishes sulfation, binding to CXCL10 and CXCL11 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis; when associated with F-27. 2 Publications
    Mutagenesisi112 – 1121D → A: Abolishes binding to CXCL10 and CXCL11. Reduces CXCL9-, CXCL10- and CXCL11-induced chemotaxis. 1 Publication
    Mutagenesisi112 – 1121D → K: Abolishes binding to CXCL10 and CXCL11 and CXCL10- and CXCL11-induced chemotaxis. Reduces CXCL9-induced chemotaxis. 1 Publication
    Mutagenesisi197 – 1971R → A: Abolishes binding to CXCL10 and CXCL11 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis. Reduces ligand-induced receptor internalization. 1 Publication
    Mutagenesisi212 – 2121R → A: Abolishes CXCL10-induced chemotaxis. Reduces CXCL9- and CXCL11-induced chemotaxis. Does not affect binding to CXCL10 and CXCL11. 1 Publication
    Mutagenesisi216 – 2161R → A: Reduces CXCL9-, CXCL10- and CXCL11-induced chemotaxis. Does not affect binding to CXCL10 and CXCL11 or receptor internalization. 1 Publication
    Mutagenesisi278 – 2781D → A: Abolishes binding to CXCL10 and CXCL11 and CXCL11-induced chemotaxis. Reduces CXCL9 and CXCL10-induced chemotaxis. 1 Publication
    Mutagenesisi278 – 2781D → K: Abolishes binding to CXCL10 and CXCL11 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis. 1 Publication
    Mutagenesisi282 – 2821D → A: Reduces binding to CXCL10 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis. Abolishes binding to CXCL11. 1 Publication
    Mutagenesisi282 – 2821D → K: Reduces binding to CXCL10 and CXCL11 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis. 1 Publication
    Mutagenesisi293 – 2931E → A: Reduces binding to CXCL10 and CXCL9- and CXCL11-induced chemotaxis. Abolishes binding to CXCL11 and CXCL10-induced chemotaxis. 1 Publication
    Mutagenesisi293 – 2931E → K: Abolishes binding to CXCL10 and CXCL11 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis. 1 Publication

    Organism-specific databases

    PharmGKBiPA35049.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 368368C-X-C chemokine receptor type 3PRO_0000069346Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi22 – 221N-linked (GlcNAc...)Sequence Analysis
    Modified residuei27 – 271Sulfotyrosine2 Publications
    Modified residuei29 – 291Sulfotyrosine1 Publication
    Glycosylationi32 – 321N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi124 ↔ 203PROSITE-ProRule annotation

    Post-translational modificationi

    Sulfation on Tyr-27 and Tyr-29 is essential for CXCL10 binding and subsequent signal transduction induction.2 Publications
    N-glycosylated.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Sulfation

    Proteomic databases

    PaxDbiP49682.
    PRIDEiP49682.

    PTM databases

    PhosphoSiteiP49682.

    Expressioni

    Tissue specificityi

    Isoform 1 and isoform 2 are mainly expressed in heart, kidney, liver and skeletal muscle. Isoform 1 is also expressed in placenta. Isoform 2 is expressed in endothelial cells. Expressed in T-cells (at protein level).2 Publications

    Gene expression databases

    BgeeiP49682.
    CleanExiHS_CXCR3.
    GenevestigatoriP49682.

    Organism-specific databases

    HPAiCAB017820.

    Interactioni

    Subunit structurei

    Homomer. Forms heteromers with ACKR4.1 Publication

    Protein-protein interaction databases

    BioGridi109094. 6 interactions.
    DIPiDIP-5891N.
    MINTiMINT-91399.
    STRINGi9606.ENSP00000362795.

    Structurei

    3D structure databases

    ProteinModelPortaliP49682.
    SMRiP49682. Positions 60-326.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 5353ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini81 – 899CytoplasmicSequence Analysis
    Topological domaini111 – 12515ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini148 – 16922CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini190 – 21223ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini234 – 25522CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini278 – 29821ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini322 – 36847CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei54 – 8027Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei90 – 11021Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei126 – 14722Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei170 – 18920Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei213 – 23321Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei256 – 27722Helical; Name=6Sequence AnalysisAdd
    BLAST
    Transmembranei299 – 32123Helical; Name=7Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG150428.
    HOGENOMiHOG000234122.
    HOVERGENiHBG106917.
    KOiK04188.
    OMAiAYCYARI.
    OrthoDBiEOG7F5126.
    PhylomeDBiP49682.
    TreeFamiTF330966.

    Family and domain databases

    Gene3Di1.20.1070.10. 1 hit.
    InterProiIPR004070. Chemokine_CXCR3.
    IPR000355. Chemokine_rcpt.
    IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    [Graphical view]
    PANTHERiPTHR24227. PTHR24227. 1 hit.
    PTHR24227:SF27. PTHR24227:SF27. 1 hit.
    PfamiPF00001. 7tm_1. 1 hit.
    [Graphical view]
    PRINTSiPR00657. CCCHEMOKINER.
    PR01532. CXCCHMKINER3.
    PR00237. GPCRRHODOPSN.
    PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P49682-1) [UniParc]FASTAAdd to Basket

    Also known as: CXCR3-A

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MVLEVSDHQV LNDAEVAALL ENFSSSYDYG ENESDSCCTS PPCPQDFSLN    50
    FDRAFLPALY SLLFLLGLLG NGAVAAVLLS RRTALSSTDT FLLHLAVADT 100
    LLVLTLPLWA VDAAVQWVFG SGLCKVAGAL FNINFYAGAL LLACISFDRY 150
    LNIVHATQLY RRGPPARVTL TCLAVWGLCL LFALPDFIFL SAHHDERLNA 200
    THCQYNFPQV GRTALRVLQL VAGFLLPLLV MAYCYAHILA VLLVSRGQRR 250
    LRAMRLVVVV VVAFALCWTP YHLVVLVDIL MDLGALARNC GRESRVDVAK 300
    SVTSGLGYMH CCLNPLLYAF VGVKFRERMW MLLLRLGCPN QRGLQRQPSS 350
    SRRDSSWSET SEASYSGL 368
    Length:368
    Mass (Da):40,660
    Last modified:November 1, 1997 - v2
    Checksum:iF08A3B44B2BBAD04
    GO
    Isoform 2 (identifier: P49682-2) [UniParc]FASTAAdd to Basket

    Also known as: CXCR3-B

    The sequence of this isoform differs from the canonical sequence as follows:
         1-4: MVLE → MELRKYGPGRLAGTVIGGAAQSKSQTKSDSITKEFLPGLYTAPSSPFPPSQ

    Show »
    Length:415
    Mass (Da):45,523
    Checksum:i325C8A65982A43C4
    GO
    Isoform 3 (identifier: P49682-3) [UniParc]FASTAAdd to Basket

    Also known as: CXCR3-alt

    The sequence of this isoform differs from the canonical sequence as follows:
         210-368: VGRTALRVLQ...ETSEASYSGL → GSSSGSGCGC...AGIRAPLSPI

    Note: Due to exon skipping.

    Show »
    Length:267
    Mass (Da):28,715
    Checksum:i8E5C6052A5A3E518
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti75 – 751A → R in CAB02143. 1 PublicationCurated
    Sequence conflicti157 – 1571T → I in BAG36429. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti292 – 2921R → Q.1 Publication
    Corresponds to variant rs139226823 [ dbSNP | Ensembl ].
    VAR_016240
    Natural varianti363 – 3631A → T.1 Publication
    VAR_016241

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 44MVLE → MELRKYGPGRLAGTVIGGAA QSKSQTKSDSITKEFLPGLY TAPSSPFPPSQ in isoform 2. 2 PublicationsVSP_015684
    Alternative sequencei210 – 368159VGRTA…SYSGL → GSSSGSGCGCCSCAWAAPTR EGSRGSHRLPAGIHPGLRPQ RPPTRACEAGIRAPLSPI in isoform 3. CuratedVSP_015685Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X95876 mRNA. Translation: CAA65126.1.
    AF469635 mRNA. Translation: AAP55851.1.
    Z79783 Genomic DNA. Translation: CAB02143.1.
    AY242128 mRNA. Translation: AAO92295.1.
    AK313679 mRNA. Translation: BAG36429.1.
    BC034403 mRNA. Translation: AAH34403.1.
    U32674 Genomic DNA. Translation: AAC50505.1.
    AB032735 Genomic DNA. Translation: BAA92297.1.
    AB032736 Genomic DNA. Translation: BAA92298.1.
    CCDSiCCDS14416.1. [P49682-1]
    CCDS48135.1. [P49682-2]
    RefSeqiNP_001136269.1. NM_001142797.1. [P49682-2]
    NP_001495.1. NM_001504.1. [P49682-1]
    UniGeneiHs.198252.

    Genome annotation databases

    EnsembliENST00000373691; ENSP00000362795; ENSG00000186810. [P49682-2]
    ENST00000373693; ENSP00000362797; ENSG00000186810. [P49682-1]
    GeneIDi2833.
    KEGGihsa:2833.
    UCSCiuc004eaf.3. human. [P49682-1]
    uc011mpx.2. human. [P49682-2]

    Polymorphism databases

    DMDMi2829400.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    Wikipedia

    CXC chemokine receptors entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X95876 mRNA. Translation: CAA65126.1 .
    AF469635 mRNA. Translation: AAP55851.1 .
    Z79783 Genomic DNA. Translation: CAB02143.1 .
    AY242128 mRNA. Translation: AAO92295.1 .
    AK313679 mRNA. Translation: BAG36429.1 .
    BC034403 mRNA. Translation: AAH34403.1 .
    U32674 Genomic DNA. Translation: AAC50505.1 .
    AB032735 Genomic DNA. Translation: BAA92297.1 .
    AB032736 Genomic DNA. Translation: BAA92298.1 .
    CCDSi CCDS14416.1. [P49682-1 ]
    CCDS48135.1. [P49682-2 ]
    RefSeqi NP_001136269.1. NM_001142797.1. [P49682-2 ]
    NP_001495.1. NM_001504.1. [P49682-1 ]
    UniGenei Hs.198252.

    3D structure databases

    ProteinModelPortali P49682.
    SMRi P49682. Positions 60-326.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109094. 6 interactions.
    DIPi DIP-5891N.
    MINTi MINT-91399.
    STRINGi 9606.ENSP00000362795.

    Chemistry

    BindingDBi P49682.
    ChEMBLi CHEMBL4441.
    GuidetoPHARMACOLOGYi 70.

    Protein family/group databases

    GPCRDBi Search...

    PTM databases

    PhosphoSitei P49682.

    Polymorphism databases

    DMDMi 2829400.

    Proteomic databases

    PaxDbi P49682.
    PRIDEi P49682.

    Protocols and materials databases

    DNASUi 2833.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373691 ; ENSP00000362795 ; ENSG00000186810 . [P49682-2 ]
    ENST00000373693 ; ENSP00000362797 ; ENSG00000186810 . [P49682-1 ]
    GeneIDi 2833.
    KEGGi hsa:2833.
    UCSCi uc004eaf.3. human. [P49682-1 ]
    uc011mpx.2. human. [P49682-2 ]

    Organism-specific databases

    CTDi 2833.
    GeneCardsi GC0XM070835.
    HGNCi HGNC:4540. CXCR3.
    HPAi CAB017820.
    MIMi 300574. gene.
    neXtProti NX_P49682.
    PharmGKBi PA35049.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG150428.
    HOGENOMi HOG000234122.
    HOVERGENi HBG106917.
    KOi K04188.
    OMAi AYCYARI.
    OrthoDBi EOG7F5126.
    PhylomeDBi P49682.
    TreeFami TF330966.

    Enzyme and pathway databases

    Reactomei REACT_15344. Chemokine receptors bind chemokines.
    REACT_19231. G alpha (i) signalling events.

    Miscellaneous databases

    GeneWikii CXCR3.
    GenomeRNAii 2833.
    NextBioi 11181.
    PROi P49682.
    SOURCEi Search...

    Gene expression databases

    Bgeei P49682.
    CleanExi HS_CXCR3.
    Genevestigatori P49682.

    Family and domain databases

    Gene3Di 1.20.1070.10. 1 hit.
    InterProi IPR004070. Chemokine_CXCR3.
    IPR000355. Chemokine_rcpt.
    IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    [Graphical view ]
    PANTHERi PTHR24227. PTHR24227. 1 hit.
    PTHR24227:SF27. PTHR24227:SF27. 1 hit.
    Pfami PF00001. 7tm_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00657. CCCHEMOKINER.
    PR01532. CXCCHMKINER3.
    PR00237. GPCRRHODOPSN.
    PROSITEi PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Chemokine receptor specific for IP10 and mig: structure, function, and expression in activated T-lymphocytes."
      Loetscher M., Gerber B., Loetscher P., Jones S.A., Piali L., Clark-Lewis I., Baggiolini M., Moser B.
      J. Exp. Med. 184:963-969(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Blood.
    2. "An alternatively spliced variant of CXCR3 mediates the inhibition of endothelial cell growth induced by IP-10, Mig, and I-TAC, and acts as functional receptor for platelet factor 4."
      Lasagni L., Francalanci M., Annunziato F., Lazzeri E., Giannini S., Cosmi L., Sagrinati C., Mazzinghi B., Orlando C., Maggi E., Marra F., Romagnani S., Serio M., Romagnani P.
      J. Exp. Med. 197:1537-1549(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION.
      Tissue: Endothelial cell and Thymus.
    4. Gutierrez J., Varona R., Zaballos A., Lind P., Marquez G.
      Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
    5. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
      Warren C.N., Aronstam R.S., Sharma S.V.
      Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Leukocyte.
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Colon.
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain, Lung and Testis.
    8. "Cloning and chromosomal mapping of three novel genes, GPR9, GPR10, and GPR14, encoding receptors related to interleukin 8, neuropeptide Y, and somatostatin receptors."
      Marchese A., Heiber M., Nguyen T., Heng H.H.Q., Saldivia V.R., Cheng R., Murphy P.M., Tsui L.-C., Shi X., Gregor P., George S.R., O'Dowd B.F., Docherty J.M.
      Genomics 29:335-344(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-368.
    9. "Single nucleotide polymorphisms in the coding regions of human CXC-chemokine receptors CXCR1, CXCR2 and CXCR3."
      Kato H., Tsuchiya N., Tokunaga K.
      Genes Immun. 1:330-337(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 278-368, VARIANTS GLN-292 AND THR-363.
    10. "Identification and partial characterization of a variant of human CXCR3 generated by posttranscriptional exon skipping."
      Ehlert J.E., Addison C.A., Burdick M.D., Kunkel S.L., Strieter R.M.
      J. Immunol. 173:6234-6240(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM 3), FUNCTION.
    11. "Interferon-inducible T cell alpha chemoattractant (I-TAC): a novel non-ELR CXC chemokine with potent activity on activated T cells through selective high affinity binding to CXCR3."
      Cole K.E., Strick C.A., Paradis T.J., Ogborne K.T., Loetscher M., Gladue R.P., Lin W., Boyd J.G., Moser B., Wood D.E., Sahagan B.G., Neote K.
      J. Exp. Med. 187:2009-2021(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: LIGAND-BINDING.
      Tissue: Fetal astrocyte.
    12. "CXCR3 requires tyrosine sulfation for ligand binding and a second extracellular loop arginine residue for ligand-induced chemotaxis."
      Colvin R.A., Campanella G.S., Manice L.A., Luster A.D.
      Mol. Cell. Biol. 26:5838-5849(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SULFATION AT TYR-27, MUTAGENESIS OF 1-MET--VAL-16; GLU-4; GLU-21; TYR-27; 27-TYR--TYR-29; TYR-29; ASP-112; ARG-197; ARG-212; ARG-216; ASP-278; ASP-282 AND GLU-293.
    13. "Sulfated tyrosines 27 and 29 in the N-terminus of human CXCR3 participate in binding native IP-10."
      Gao J.M., Xiang R.L., Jiang L., Li W.H., Feng Q.P., Guo Z.J., Sun Q., Zeng Z.P., Fang F.D.
      Acta Pharmacol. Sin. 30:193-201(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SULFATION AT TYR-27 AND TYR-29, MUTAGENESIS OF TYR-27 AND TYR-29.
    14. "CXCR3-B can mediate growth-inhibitory signals in human renal cancer cells by down-regulating the expression of heme oxygenase-1."
      Datta D., Banerjee P., Gasser M., Waaga-Gasser A.M., Pal S.
      J. Biol. Chem. 285:36842-36848(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. Cited for: SUBUNIT, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiCXCR3_HUMAN
    AccessioniPrimary (citable) accession number: P49682
    Secondary accession number(s): B2R982
    , O15185, Q7Z710, Q9P2T4, Q9P2T5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 149 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. 7-transmembrane G-linked receptors
      List of 7-transmembrane G-linked receptor entries
    2. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    3. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    4. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    5. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    6. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

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