CXCR3_RAT
ID CXCR3_RAT Reviewed; 367 AA.
AC Q9JII9;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10825390;
RA Wang X., Li X., Schmidt D.B., Foley J.J., Barone F.C., Ames R.S.,
RA Sarau H.M.;
RT "Identification and molecular characterization of rat CXCR3: receptor
RT expression and interferon-inducible protein-10 binding are increased in
RT focal stroke.";
RL Mol. Pharmacol. 57:1190-1198(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
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).
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 Binds to CCL21. Probably promotes cell chemotaxis response (By
CC similarity). {ECO:0000250}.
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 -!- 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}.
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DR EMBL; AF223642; AAF76982.1; -; mRNA.
DR EMBL; BC091136; AAH91136.1; -; mRNA.
DR RefSeq; NP_445867.1; NM_053415.1.
DR AlphaFoldDB; Q9JII9; -.
DR SMR; Q9JII9; -.
DR STRING; 10116.ENSRNOP00000004406; -.
DR BindingDB; Q9JII9; -.
DR ChEMBL; CHEMBL1075172; -.
DR GlyGen; Q9JII9; 3 sites.
DR PhosphoSitePlus; Q9JII9; -.
DR PaxDb; Q9JII9; -.
DR Ensembl; ENSRNOT00000004406; ENSRNOP00000004406; ENSRNOG00000003305.
DR GeneID; 84475; -.
DR KEGG; rno:84475; -.
DR UCSC; RGD:621528; rat.
DR CTD; 2833; -.
DR RGD; 621528; Cxcr3.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244848; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; Q9JII9; -.
DR OMA; VCISFDR; -.
DR OrthoDB; 794531at2759; -.
DR PhylomeDB; Q9JII9; -.
DR TreeFam; TF330966; -.
DR Reactome; R-RNO-380108; Chemokine receptors bind chemokines.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:Q9JII9; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000003305; Expressed in spleen and 13 other tissues.
DR ExpressionAtlas; Q9JII9; baseline and differential.
DR Genevisible; Q9JII9; RN.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
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; IPI:RGD.
DR GO; GO:0019956; F:chemokine binding; ISO:RGD.
DR GO; GO:0038023; F:signaling receptor activity; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0019722; P:calcium-mediated signaling; IDA:RGD.
DR GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:RGD.
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: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; IDA:RGD.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISS:UniProtKB.
DR GO; GO:0030155; P:regulation of cell adhesion; ISO:RGD.
DR GO; GO:0002685; P:regulation of leukocyte migration; IEA:InterPro.
DR GO; GO:0010818; P:T cell chemotaxis; IMP:RGD.
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 2: Evidence at transcript 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_0000069348"
FT TOPO_DOM 1..56
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..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..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..189
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..222
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..255
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..300
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..367
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 339..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..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 CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 123..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 367 AA; 40935 MW; F67C0362EDDBFCB7 CRC64;
MYLEVSERQV LDASDIAFLL ENSTSPYDYG ENESDFSDSP PCPQDFSLNF DRTFLPVLYS
LLFLLGLLGN GAVAAVLLSQ RTALSSTDTF LLHLAVADVL LVLTLPLWAV DAAAQWVFGS
GLCKVAGALF NINFYAGAFL LACISFDRYL SIVHATQIYR RDPWVRVALT CIVVWGLCVL
FALPDFIFLS ASHDQRLNAT HCQYNFPQVG RTALRVLQLV AGFLMPLLVM AYCYAHILAV
LLVSRGQRRF RAMRLVVVVV VAFAVCWTPY HLVVLVDILM DVGVLARNCG RESHVDVAKS
VTSGMGYMHC CLNPLLYAFV GVKFKEQMWM LLMRLGRSDQ RGPQRQPSSS RRESSWSETT
EASYLGL
