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CXCR3_CANLF
ID   CXCR3_CANLF             Reviewed;         365 AA.
AC   Q5KSK8;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 98.
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   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Tsukui T., Maeda S., Koyanagi M., Hashimoto R., Masuda K., Ohno K.,
RA   Sakaguchi M., Tsujimoto H., Iwabuchi S.;
RT   "Expression analysis of CXCR3 gene in canine atopic dermatitis.";
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
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; AB185149; BAD86855.1; -; mRNA.
DR   AlphaFoldDB; Q5KSK8; -.
DR   SMR; Q5KSK8; -.
DR   STRING; 9612.ENSCAFP00000025254; -.
DR   BindingDB; Q5KSK8; -.
DR   ChEMBL; CHEMBL1075194; -.
DR   PaxDb; Q5KSK8; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   InParanoid; Q5KSK8; -.
DR   PRO; PR:Q5KSK8; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
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; IEA:InterPro.
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; IBA:GO_Central.
DR   GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISS: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   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..365
FT                   /note="C-X-C chemokine receptor type 3"
FT                   /id="PRO_0000069344"
FT   TOPO_DOM        1..57
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        58..78
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        79..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..126
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        127..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..190
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        191..223
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        224..244
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        245..256
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        257..277
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        278..301
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        302..322
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        323..365
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          342..365
FT                   /note="Disordered"
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        124..203
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   365 AA;  40884 MW;  03B09F8E1D50216D CRC64;
     MVPEMSERQV FQASELTYLL ENCSSSYDYA ENESDSCCAS PPCPQDISLN FDRAFLPALY
     GLLFLLGLLG NGAVAAVLCS QRAARTSTDT FLLHLAVADM LLVLTLPLWR VDTAVQWVFG
     SGLCKVAGAL FNINFYAGAL LLACISFDRY LSIVHATQPY RRGPPARVTL TCVVVWGLCL
     FFAIPDFIFL SANRDERLNA MHCRYNFPQV GRTALRGLQL VAGFLLPLLV MAYCYARILA
     VLLVSRGQRR QRRMRLVVVV VVAFALCWTP YHLVVLVDTL MDLGALDRNC GRESRVDVAK
     SVTSGLGYMH CCLNPLLYAF VGVKFRERMW MLLLRLGCPD HRGHQRHPTL SRRESSWSET
     PSTPR
 
 
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