ID CXCR3_BOVIN Reviewed; 366 AA.
AC Q5MD61; A7E3R9;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 24-JAN-2024, entry version 125.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Blumerman S.L., Baldwin C.L.;
RT "Molecular cloning and characterization of bovine chemokine receptors.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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-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; AY834254; AAV97931.1; -; mRNA.
DR EMBL; BT030690; ABS45006.1; -; mRNA.
DR RefSeq; NP_001011673.1; NM_001011673.1.
DR AlphaFoldDB; Q5MD61; -.
DR SMR; Q5MD61; -.
DR STRING; 9913.ENSBTAP00000019690; -.
DR GlyCosmos; Q5MD61; 3 sites, No reported glycans.
DR PaxDb; 9913-ENSBTAP00000019690; -.
DR Ensembl; ENSBTAT00000019690.5; ENSBTAP00000019690.4; ENSBTAG00000014798.5.
DR GeneID; 497018; -.
DR KEGG; bta:497018; -.
DR CTD; 2833; -.
DR VEuPathDB; HostDB:ENSBTAG00000014798; -.
DR VGNC; VGNC:27855; CXCR3.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244848; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; Q5MD61; -.
DR OMA; HAVHMYK; -.
DR OrthoDB; 5356683at2759; -.
DR TreeFam; TF330966; -.
DR Reactome; R-BTA-380108; Chemokine receptors bind chemokines.
DR Reactome; R-BTA-418594; G alpha (i) signalling events.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000014798; Expressed in mesenteric lymph node and 59 other cell types or tissues.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
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 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.
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_0000069343"
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 341..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; 40805 MW; 0889D2E73A1579E2 CRC64;
MVPEMSERQE FQASDFAYLL ENSSYDYGEN ETYFCCTSPP CPQDFSLNFD RTFLPVLYSL
LFVLGLLGNG IVAVVLLSQR AALSSTDTFL LHLAVADALL VLTLPLWAVD AAIQWVFGSG
LCKVAGALFN INFYAGALLL ACISFDRYLS IVHATQLYRR GPPTRVALTC VAVWGLCLLF
ALPDFIFLSS HHDNRLNATH CQYNFPQEGH TALRILQLVA GFLLPLLVMA YCYARILAVL
LVSRGQRRLR AMRLVVVVVV AFALCWTPYH LVVLVDTLMD LGALARNCGR ESSVDIAKSV
TSGMGYMHCC LNPLLYAFVG VKFRERMWVL LVRLGCPDQR CHQRQPSASR RESSWSETTE
ASYSGL
//
