CXCR3_MOUSE
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 03-AUG-2022, entry version 163.
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 GlyGen; O88410; 2 sites.
DR iPTMnet; O88410; -.
DR PhosphoSitePlus; O88410; -.
DR EPD; O88410; -.
DR PaxDb; O88410; -.
DR PRIDE; O88410; -.
DR ProteomicsDB; 284075; -.
DR Antibodypedia; 566; 1007 antibodies from 45 providers.
DR DNASU; 12766; -.
DR Ensembl; ENSMUST00000056614; ENSMUSP00000052444; ENSMUSG00000050232.
DR GeneID; 12766; -.
DR KEGG; mmu:12766; -.
DR UCSC; uc009tye.1; mouse.
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; VCISFDR; -.
DR OrthoDB; 794531at2759; -.
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 72 CRISPR screens.
DR PRO; PR:O88410; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; O88410; protein.
DR Bgee; ENSMUSG00000050232; Expressed in secondary oocyte and 56 other tissues.
DR Genevisible; O88410; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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 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
