CXCR3_CAPHI
ID CXCR3_CAPHI Reviewed; 366 AA.
AC Q867B2;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 87.
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 Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=12756249; DOI=10.1074/jbc.m300470200;
RA Nagaoka K., Nojima H., Watanabe F., Chang K.-T., Christenson R.K.,
RA Sakai S., Imakawa K.;
RT "Regulation of blastocyst migration, apposition, and initial adhesion by a
RT chemokine, interferon gamma-inducible protein 10 kDa (IP-10), during early
RT gestation.";
RL J. Biol. Chem. 278:29048-29056(2003).
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, ECO:0000269|PubMed:12756249}.
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-25 and Tyr-27 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; AB099893; BAC55184.1; -; mRNA.
DR RefSeq; NP_001272652.1; NM_001285723.1.
DR AlphaFoldDB; Q867B2; -.
DR SMR; Q867B2; -.
DR STRING; 9925.ENSCHIP00000013608; -.
DR Ensembl; ENSCHIT00000021389; ENSCHIP00000013597; ENSCHIG00000014964.
DR GeneID; 100860874; -.
DR KEGG; chx:100860874; -.
DR CTD; 2833; -.
DR GeneTree; ENSGT01050000244848; -.
DR OrthoDB; 794531at2759; -.
DR Proteomes; UP000291000; Unassembled WGS sequence.
DR Bgee; ENSCHIG00000014964; Expressed in spleen and 5 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
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: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..366
FT /note="C-X-C chemokine receptor type 3"
FT /id="PRO_0000069345"
FT TOPO_DOM 1..55
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..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..145
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..221
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..299
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..320
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 339..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 27
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 122..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 366 AA; 40871 MW; 222AE9D136E09C0F CRC64;
MVPEMSERQE FQASEFAYLL ENSSYDYGEN ETYFCCTSPP CPQDFSLNFD RTFLPVLYSL
LFVLGLLGNG VVAVVLLSQR AALSSTDTFL LHLAVADALL VLTLPLWAVD AAIQWVFGSG
LCKVAGALFN INFYAGALLL ACISFDRYLS IVHATQFYRR GPPARVALTC VAVWGLCLLF
ALPDFIFLSS HHDNRLNATH CQYNFPQEGR TALRVLQLVA GFLLPLLVMA YCYARILTVL
LVSRGQRRLR AMRLVVVVVV AFALCWTPYH LVVLVDTLMD LGALARNCGR ESRVDVAKSV
TSGMGYMHCC LNPLLYAFVG VKFRERMWVL LMRLGCPDQR GHQRQPSASR RDSSWSETTE
ASYSGL
