CXCR3 is a seven-transmembrane chemokine receptor that recognizes CXCL9, CXCL10 and CXCL11 and coordinates lymphocyte recruitment through G-protein signaling. Mammalian alternative isoforms differ in ligand recognition and downstream growth responses; CXCR3-B also recognizes CXCL4 and mediates angiostatic responses.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0002685 regulation of leukocyte migration | IEA GO_REF:0000002 | ACCEPT | Summary: regulation of leukocyte migration: CXCR3 ligand binding and receptor signaling recruit immune cells. The human receptor/isoform experiments support this membrane chemokine-receptor function; calcium signaling and chemotaxis are mechanistic components rather than unrelated downstream associations. Reason: CXCR3 ligand binding and receptor signaling recruit immune cells. The human receptor/isoform experiments support this membrane chemokine-receptor function; calcium signaling and chemotaxis are mechanistic components rather than unrelated downstream associations. Supporting Evidence: PMID:12782716 Human microvascular endothelial cell line-1 (HMEC-1), transfected with either the known CXCR3 (renamed CXCR3-A) or CXCR3-B, bound CXCL9, CXCL10, and CXCL11, whereas CXCL4 showed high affinity only for CXCR3-B. file:HORSE/CXCR3/CXCR3-bioinformatics/RESULTS.md The downloaded human P49682 sequence (368 residues) and selected horse A0A9L0T1D1 sequence (369 residues) share 90.8% identity among 368 paired residues. Paired coverage is 100.0% of human and 99.7% of horse. |
| GO:0004930 G protein-coupled receptor activity | IEA GO_REF:0000120 | ACCEPT | Summary: G protein-coupled receptor activity: CXCR3 ligand binding and receptor signaling recruit immune cells. The human receptor/isoform experiments support this membrane chemokine-receptor function; calcium signaling and chemotaxis are mechanistic components rather than unrelated downstream associations. Reason: CXCR3 ligand binding and receptor signaling recruit immune cells. The human receptor/isoform experiments support this membrane chemokine-receptor function; calcium signaling and chemotaxis are mechanistic components rather than unrelated downstream associations. Supporting Evidence: PMID:12782716 Human microvascular endothelial cell line-1 (HMEC-1), transfected with either the known CXCR3 (renamed CXCR3-A) or CXCR3-B, bound CXCL9, CXCL10, and CXCL11, whereas CXCL4 showed high affinity only for CXCR3-B. file:HORSE/CXCR3/CXCR3-bioinformatics/RESULTS.md The downloaded human P49682 sequence (368 residues) and selected horse A0A9L0T1D1 sequence (369 residues) share 90.8% identity among 368 paired residues. Paired coverage is 100.0% of human and 99.7% of horse. |
| GO:0004950 chemokine receptor activity | IEA GO_REF:0000002 | ACCEPT | Summary: chemokine receptor activity: CXCR3 ligand binding and receptor signaling recruit immune cells. The human receptor/isoform experiments support this membrane chemokine-receptor function; calcium signaling and chemotaxis are mechanistic components rather than unrelated downstream associations. Reason: CXCR3 ligand binding and receptor signaling recruit immune cells. The human receptor/isoform experiments support this membrane chemokine-receptor function; calcium signaling and chemotaxis are mechanistic components rather than unrelated downstream associations. Supporting Evidence: PMID:12782716 Human microvascular endothelial cell line-1 (HMEC-1), transfected with either the known CXCR3 (renamed CXCR3-A) or CXCR3-B, bound CXCL9, CXCL10, and CXCL11, whereas CXCL4 showed high affinity only for CXCR3-B. file:HORSE/CXCR3/CXCR3-bioinformatics/RESULTS.md The downloaded human P49682 sequence (368 residues) and selected horse A0A9L0T1D1 sequence (369 residues) share 90.8% identity among 368 paired residues. Paired coverage is 100.0% of human and 99.7% of horse. |
| GO:0005886 plasma membrane | IEA GO_REF:0000120 | ACCEPT | Summary: plasma membrane: CXCR3 ligand binding and receptor signaling recruit immune cells. The human receptor/isoform experiments support this membrane chemokine-receptor function; calcium signaling and chemotaxis are mechanistic components rather than unrelated downstream associations. Reason: CXCR3 ligand binding and receptor signaling recruit immune cells. The human receptor/isoform experiments support this membrane chemokine-receptor function; calcium signaling and chemotaxis are mechanistic components rather than unrelated downstream associations. Supporting Evidence: PMID:12782716 Human microvascular endothelial cell line-1 (HMEC-1), transfected with either the known CXCR3 (renamed CXCR3-A) or CXCR3-B, bound CXCL9, CXCL10, and CXCL11, whereas CXCL4 showed high affinity only for CXCR3-B. file:HORSE/CXCR3/CXCR3-bioinformatics/RESULTS.md The downloaded human P49682 sequence (368 residues) and selected horse A0A9L0T1D1 sequence (369 residues) share 90.8% identity among 368 paired residues. Paired coverage is 100.0% of human and 99.7% of horse. |
| GO:0006935 chemotaxis | IEA GO_REF:0000002 | ACCEPT | Summary: chemotaxis: CXCR3 ligand binding and receptor signaling recruit immune cells. The human receptor/isoform experiments support this membrane chemokine-receptor function; calcium signaling and chemotaxis are mechanistic components rather than unrelated downstream associations. Reason: CXCR3 ligand binding and receptor signaling recruit immune cells. The human receptor/isoform experiments support this membrane chemokine-receptor function; calcium signaling and chemotaxis are mechanistic components rather than unrelated downstream associations. Supporting Evidence: PMID:12782716 Human microvascular endothelial cell line-1 (HMEC-1), transfected with either the known CXCR3 (renamed CXCR3-A) or CXCR3-B, bound CXCL9, CXCL10, and CXCL11, whereas CXCL4 showed high affinity only for CXCR3-B. file:HORSE/CXCR3/CXCR3-bioinformatics/RESULTS.md The downloaded human P49682 sequence (368 residues) and selected horse A0A9L0T1D1 sequence (369 residues) share 90.8% identity among 368 paired residues. Paired coverage is 100.0% of human and 99.7% of horse. |
| GO:0006954 inflammatory response | IEA GO_REF:0000002 | ACCEPT | Summary: inflammatory response: CXCR3 ligand binding and receptor signaling recruit immune cells. The human receptor/isoform experiments support this membrane chemokine-receptor function; calcium signaling and chemotaxis are mechanistic components rather than unrelated downstream associations. Reason: CXCR3 ligand binding and receptor signaling recruit immune cells. The human receptor/isoform experiments support this membrane chemokine-receptor function; calcium signaling and chemotaxis are mechanistic components rather than unrelated downstream associations. Supporting Evidence: PMID:12782716 Human microvascular endothelial cell line-1 (HMEC-1), transfected with either the known CXCR3 (renamed CXCR3-A) or CXCR3-B, bound CXCL9, CXCL10, and CXCL11, whereas CXCL4 showed high affinity only for CXCR3-B. file:HORSE/CXCR3/CXCR3-bioinformatics/RESULTS.md The downloaded human P49682 sequence (368 residues) and selected horse A0A9L0T1D1 sequence (369 residues) share 90.8% identity among 368 paired residues. Paired coverage is 100.0% of human and 99.7% of horse. |
| GO:0007165 signal transduction | IEA GO_REF:0000104 | UNDECIDED | Summary: signal transduction: The available evidence examined for CXCR3 does not resolve the exact claim of signal transduction. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000104 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper. Reason: The available evidence examined for CXCR3 does not resolve the exact claim of signal transduction. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000104 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper. |
| GO:0007186 G protein-coupled receptor signaling pathway | IEA GO_REF:0000120 | ACCEPT | Summary: G protein-coupled receptor signaling pathway: CXCR3 ligand binding and receptor signaling recruit immune cells. The human receptor/isoform experiments support this membrane chemokine-receptor function; calcium signaling and chemotaxis are mechanistic components rather than unrelated downstream associations. Reason: CXCR3 ligand binding and receptor signaling recruit immune cells. The human receptor/isoform experiments support this membrane chemokine-receptor function; calcium signaling and chemotaxis are mechanistic components rather than unrelated downstream associations. Supporting Evidence: PMID:12782716 Human microvascular endothelial cell line-1 (HMEC-1), transfected with either the known CXCR3 (renamed CXCR3-A) or CXCR3-B, bound CXCL9, CXCL10, and CXCL11, whereas CXCL4 showed high affinity only for CXCR3-B. file:HORSE/CXCR3/CXCR3-bioinformatics/RESULTS.md The downloaded human P49682 sequence (368 residues) and selected horse A0A9L0T1D1 sequence (369 residues) share 90.8% identity among 368 paired residues. Paired coverage is 100.0% of human and 99.7% of horse. |
| GO:0009986 cell surface | IEA GO_REF:0000117 | ACCEPT | Summary: cell surface: CXCR3 ligand binding and receptor signaling recruit immune cells. The human receptor/isoform experiments support this membrane chemokine-receptor function; calcium signaling and chemotaxis are mechanistic components rather than unrelated downstream associations. Reason: CXCR3 ligand binding and receptor signaling recruit immune cells. The human receptor/isoform experiments support this membrane chemokine-receptor function; calcium signaling and chemotaxis are mechanistic components rather than unrelated downstream associations. Supporting Evidence: PMID:12782716 Human microvascular endothelial cell line-1 (HMEC-1), transfected with either the known CXCR3 (renamed CXCR3-A) or CXCR3-B, bound CXCL9, CXCL10, and CXCL11, whereas CXCL4 showed high affinity only for CXCR3-B. file:HORSE/CXCR3/CXCR3-bioinformatics/RESULTS.md The downloaded human P49682 sequence (368 residues) and selected horse A0A9L0T1D1 sequence (369 residues) share 90.8% identity among 368 paired residues. Paired coverage is 100.0% of human and 99.7% of horse. |
| GO:0016020 membrane | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: membrane: A membrane location is correct but much less informative than plasma membrane for this seven-pass receptor. Reason: A membrane location is correct but much less informative than plasma membrane for this seven-pass receptor. Supporting Evidence: PMID:12782716 Human microvascular endothelial cell line-1 (HMEC-1), transfected with either the known CXCR3 (renamed CXCR3-A) or CXCR3-B, bound CXCL9, CXCL10, and CXCL11, whereas CXCL4 showed high affinity only for CXCR3-B. file:HORSE/CXCR3/CXCR3-bioinformatics/RESULTS.md The downloaded human P49682 sequence (368 residues) and selected horse A0A9L0T1D1 sequence (369 residues) share 90.8% identity among 368 paired residues. Paired coverage is 100.0% of human and 99.7% of horse. |
| GO:0016494 C-X-C chemokine receptor activity | IEA GO_REF:0000002 | ACCEPT | Summary: C-X-C chemokine receptor activity: CXCR3 ligand binding and receptor signaling recruit immune cells. The human receptor/isoform experiments support this membrane chemokine-receptor function; calcium signaling and chemotaxis are mechanistic components rather than unrelated downstream associations. Reason: CXCR3 ligand binding and receptor signaling recruit immune cells. The human receptor/isoform experiments support this membrane chemokine-receptor function; calcium signaling and chemotaxis are mechanistic components rather than unrelated downstream associations. Supporting Evidence: PMID:12782716 Human microvascular endothelial cell line-1 (HMEC-1), transfected with either the known CXCR3 (renamed CXCR3-A) or CXCR3-B, bound CXCL9, CXCL10, and CXCL11, whereas CXCL4 showed high affinity only for CXCR3-B. file:HORSE/CXCR3/CXCR3-bioinformatics/RESULTS.md The downloaded human P49682 sequence (368 residues) and selected horse A0A9L0T1D1 sequence (369 residues) share 90.8% identity among 368 paired residues. Paired coverage is 100.0% of human and 99.7% of horse. |
| GO:0070098 chemokine-mediated signaling pathway | IEA GO_REF:0000120 | ACCEPT | Summary: chemokine-mediated signaling pathway: CXCR3 ligand binding and receptor signaling recruit immune cells. The human receptor/isoform experiments support this membrane chemokine-receptor function; calcium signaling and chemotaxis are mechanistic components rather than unrelated downstream associations. Reason: CXCR3 ligand binding and receptor signaling recruit immune cells. The human receptor/isoform experiments support this membrane chemokine-receptor function; calcium signaling and chemotaxis are mechanistic components rather than unrelated downstream associations. Supporting Evidence: PMID:12782716 Human microvascular endothelial cell line-1 (HMEC-1), transfected with either the known CXCR3 (renamed CXCR3-A) or CXCR3-B, bound CXCL9, CXCL10, and CXCL11, whereas CXCL4 showed high affinity only for CXCR3-B. file:HORSE/CXCR3/CXCR3-bioinformatics/RESULTS.md The downloaded human P49682 sequence (368 residues) and selected horse A0A9L0T1D1 sequence (369 residues) share 90.8% identity among 368 paired residues. Paired coverage is 100.0% of human and 99.7% of horse. |
Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)The downloaded human P49682 sequence (368 residues) and selected horse A0A9L0T1D1 sequence (369 residues) share 90.8% identity among 368 paired residues. Paired coverage is 100.0% of human and 99.7% of horse.
Full alignment, hashes, parameters and reproducible script: CXCR3.json and compare.py.
Pairwise similarity supports homology but does not establish reciprocal orthology, intact gene models, conservation of targeting signals or every biological claim. Current UniProt sequences are compared; identity with the original ProtNLM input sequence is unverified.
Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)