ID   CXCR3_MOUSE             Reviewed;         367 AA.
AC   O88410; Q4V9Y6; Q9QWN6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 2.
DT   24-JAN-2024, entry version 171.
DE   RecName: Full=C-X-C chemokine receptor type 3;
DE            Short=CXC-R3;
DE            Short=CXCR-3;
DE   AltName: Full=Interferon-inducible protein 10 receptor;
DE            Short=IP-10 receptor;
DE   AltName: CD_antigen=CD183;
GN   Name=Cxcr3; Synonyms=Cmkar3;
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.
RX   PubMed=9653165; DOI=10.1073/pnas.95.14.8205;
RA   Soto H., Wang W., Strieter R.M., Copeland N.G., Gilbert D.J., Jenkins N.A.,
RA   Hedrick J., Zlotnik A.;
RT   "The CC chemokine 6Ckine binds the CXC chemokine receptor CXCR3.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:8205-8210(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND FUNCTION.
RC   TISSUE=Blood;
RX   PubMed=9790904; DOI=10.1006/bbrc.1998.9404;
RA   Tamaru M., Tominaga Y., Yatunami K., Narumi S.;
RT   "Cloning of the murine interferon-inducible protein 10 (IP-10) receptor and
RT   its specific expression in lymphoid organs.";
RL   Biochem. Biophys. Res. Commun. 251:41-48(1998).
RN   [3]
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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Receptor for the C-X-C chemokine CXCL9, CXCL10 and CXCL11 and
CC       mediates the proliferation, survival and angiogenic activity of
CC       mesangial cells through a heterotrimeric G-protein signaling pathway.
CC       Probably promotes cell chemotaxis response (By similarity). Binds to
CC       CCL21. {ECO:0000250, ECO:0000269|PubMed:9653165,
CC       ECO:0000269|PubMed:9790904}.
CC   -!- SUBUNIT: Homomer. Forms heteromers with ACKR4 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expresses in lymphoid organs and Th1 cells.
CC       {ECO:0000269|PubMed:9790904}.
CC   -!- PTM: Sulfation on Tyr-27 and Tyr-29 is essential for CXCL10 binding.
CC       {ECO:0000250}.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF045146; AAC40163.1; -; mRNA.
DR   EMBL; AB003174; BAA34045.1; -; mRNA.
DR   EMBL; BC096626; AAH96626.1; -; mRNA.
DR   CCDS; CCDS30319.1; -.
DR   PIR; JE0349; JE0349.
DR   RefSeq; NP_034040.1; NM_009910.3.
DR   AlphaFoldDB; O88410; -.
DR   SMR; O88410; -.
DR   STRING; 10090.ENSMUSP00000052444; -.
DR   BindingDB; O88410; -.
DR   ChEMBL; CHEMBL5200; -.
DR   GlyCosmos; O88410; 2 sites, No reported glycans.
DR   GlyGen; O88410; 2 sites.
DR   iPTMnet; O88410; -.
DR   PhosphoSitePlus; O88410; -.
DR   EPD; O88410; -.
DR   PaxDb; 10090-ENSMUSP00000052444; -.
DR   ProteomicsDB; 284075; -.
DR   Antibodypedia; 566; 1310 antibodies from 46 providers.
DR   DNASU; 12766; -.
DR   Ensembl; ENSMUST00000056614.7; ENSMUSP00000052444.7; ENSMUSG00000050232.7.
DR   GeneID; 12766; -.
DR   KEGG; mmu:12766; -.
DR   UCSC; uc009tye.1; mouse.
DR   AGR; MGI:1277207; -.
DR   CTD; 2833; -.
DR   MGI; MGI:1277207; Cxcr3.
DR   VEuPathDB; HostDB:ENSMUSG00000050232; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01050000244848; -.
DR   HOGENOM; CLU_009579_8_3_1; -.
DR   InParanoid; O88410; -.
DR   OMA; HAVHMYK; -.
DR   OrthoDB; 5356683at2759; -.
DR   PhylomeDB; O88410; -.
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; 12766; 2 hits in 77 CRISPR screens.
DR   PRO; PR:O88410; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; O88410; Protein.
DR   Bgee; ENSMUSG00000050232; Expressed in secondary oocyte and 57 other cell types or tissues.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISS: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; ISS:UniProtKB.
DR   GO; GO:0016494; F:C-X-C chemokine receptor activity; ISO:MGI.
DR   GO; GO:0019956; F:chemokine binding; ISO:MGI.
DR   GO; GO:0038023; F:signaling receptor activity; ISS:UniProtKB.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:MGI.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0019722; P:calcium-mediated signaling; ISO:MGI.
DR   GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:MGI.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS: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; ISO:MGI.
DR   GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISO:MGI.
DR   GO; GO:1900118; P:negative regulation of execution phase of apoptosis; ISS:UniProtKB.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0050921; P:positive regulation of chemotaxis; ISS:UniProtKB.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR   GO; GO:1900119; P:positive regulation of execution phase of apoptosis; ISO:MGI.
DR   GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0030155; P:regulation of cell adhesion; ISO:MGI.
DR   GO; GO:0002685; P:regulation of leukocyte migration; IEA:InterPro.
DR   GO; GO:0010818; P:T cell chemotaxis; ISO:MGI.
DR   CDD; cd15180; 7tmA_CXCR3; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR004070; Chemokine_CXCR3.
DR   InterPro; IPR000355; Chemokine_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR10489:SF671; C-X-C CHEMOKINE RECEPTOR TYPE 3; 1.
DR   PANTHER; PTHR10489; CELL ADHESION MOLECULE; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00657; CCCHEMOKINER.
DR   PRINTS; PR01532; CXCCHMKINER3.
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.
DR   Genevisible; O88410; MM.
PE   1: Evidence at protein level;
KW   Angiogenesis; Cell membrane; Chemotaxis; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW   Reference proteome; Sulfation; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..367
FT                   /note="C-X-C chemokine receptor type 3"
FT                   /id="PRO_0000069347"
FT   TOPO_DOM        1..52
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        53..79
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        80..88
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        89..109
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        110..124
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..146
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        147..168
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..188
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        189..211
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        212..232
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        233..254
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        255..276
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        277..297
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        298..320
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        321..367
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          338..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..367
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         27
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         29
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250"
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        123..202
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   CONFLICT        16
FT                   /note="F -> S (in Ref. 3; AAH96626)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        292
FT                   /note="E -> K (in Ref. 1; AAC40163)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        327
FT                   /note="Q -> K (in Ref. 1; AAC40163)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   367 AA;  41018 MW;  EF0348A8358AD951 CRC64;
     MYLEVSERQV LDASDFAFLL ENSTSPYDYG ENESDFSDSP PCPQDFSLNF DRTFLPALYS
     LLFLLGLLGN GAVAAVLLSQ RTALSSTDTF LLHLAVADVL LVLTLPLWAV DAAVQWVFGP
     GLCKVAGALF NINFYAGAFL LACISFDRYL SIVHATQIYR RDPRVRVALT CIVVWGLCLL
     FALPDFIYLS ANYDQRLNAT HCQYNFPQVG RTALRVLQLV AGFLLPLLVM AYCYAHILAV
     LLVSRGQRRF RAMRLVVVVV AAFAVCWTPY HLVVLVDILM DVGVLARNCG RESHVDVAKS
     VTSGMGYMHC CLNPLLYAFV GVKFREQMWM LFTRLGRSDQ RGPQRQPSSS RRESSWSETT
     EASYLGL
//