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VEGFR3/FLT-4   Protein, Antibody, ELISA Kit, cDNA Clone

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Expression host: Human Cells  
10806-H08H-50
10806-H08H-100
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Expression host: Human Cells  
10806-H02H-50
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Expression host: E. coli  
10013-HNAE-500
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10013-HNAE-10
10013-HNAE-1
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Expression host: Human Cells  
50584-M02H-50
50584-M02H-100
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Expression host: Human Cells  
50584-M08H-50
50584-M08H-100
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VEGFR3/FLT-4  Related Area

VEGFR3/FLT-4  Related Pathways

VEGFR3/FLT-4  Related Protein, Antibody, cDNA Gene, and ELISA Kits

VEGFR3/FLT-4  Related Protein, Antibody, cDNA Gene, and ELISA Kits

VEGFR3/FLT-4  Summary & Protein Information

VEGFR3/FLT-4  Background

Gene Summary: FLT4 gene encodes a tyrosine kinase receptor for vascular endothelial growth factors C and D. The protein is thought to be involved in lymphangiogenesis and maintenance of the lymphatic endothelium. Mutations in FLT4 gene cause hereditary lymphedema type IA. [provided by RefSeq, Jul 2008]
General information above from NCBI
Catalytic activity: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:12881528, ECO:0000269|PubMed:7898938}.
Cofactor: 0
Enzyme regulation: Present in an inactive conformation in the absence of bound ligand. Binding of VEGFC or VEGFD leads to dimerization and activation by autophosphorylation on tyrosine residues. Inhibited by MAZ51. {ECO:0000269|PubMed:15102829, ECO:0000269|PubMed:19779139, ECO:0000269|PubMed:20431062}.
Subunit structure: Interacts with VEGFC and VEGFD. Monomer in the absence of bound VEGFC or VEGFD. Homodimer in the presence of bound VEGFC or VEGFD. Can also form a heterodimer with KDR. Interacts with PTPN14; the interaction is enhanced by stimulation with VEGFC. Interacts with CRK, GRB2, PTK2/FAK1, SHC1, PIK3R1 and PTPN11/SHP-2. Identified in a complex with SRC and ITGB1. {ECO:0000269|PubMed:12881528, ECO:0000269|PubMed:15102829, ECO:0000269|PubMed:15474514, ECO:0000269|PubMed:16076871, ECO:0000269|PubMed:16452200, ECO:0000269|PubMed:18593464, ECO:0000269|PubMed:19610651, ECO:0000269|PubMed:20224550, ECO:0000269|PubMed:20431062, ECO:0000269|PubMed:20826270, ECO:0000269|PubMed:7675451, ECO:0000269|PubMed:8700872, ECO:0000269|PubMed:9435229}.
Domain: The first and second Ig-like C2-type (immunoglobulin-like) domains are sufficient for VEGFC binding.
Subcellular location: Cell membrane; Single-pass type I membrane protein. Cytoplasm. Nucleus. Note=Ligand-mediated autophosphorylation leads to rapid internalization.; Isoform 1: Cell membrane; Single-pass type I membrane protein. Note=Ligand-mediated autophosphorylation leads to rapid internalization.; Isoform 2: Cell membrane; Single-pass type I membrane protein.; Isoform 3: Secreted. Cytoplasm.
Tissue specificity: Detected in endothelial cells (at protein level). Widely expressed. Detected in fetal spleen, lung and brain. Detected in adult liver, muscle, thymus, placenta, lung, testis, ovary, prostate, heart, and kidney. {ECO:0000269|PubMed:1327515, ECO:0000269|PubMed:20224550, ECO:0000269|PubMed:7675451}.
Developmental stage: 0
Induction: MUTAGEN 879 879 K->G: Abolishes enzyme activity. {ECO:0000269|PubMed:12881528}.; MUTAGEN 1063 1063 Y->F: Loss of phosphorylation site. No effect on stimulation of cell proliferation and cell migration. {ECO:0000269|PubMed:16076871, ECO:0000269|PubMed:20431062}.; MUTAGEN 1068 1068 Y->F: Global loss of autophosphorylation. Abolishes stimulation of cell proliferation and cell migration. {ECO:0000269|PubMed:16076871, ECO:0000269|PubMed:20431062}.; MUTAGEN 1230 1230 Y->F: Loss of phosphorylation site. Strongly reduces stimulation of cell proliferation and cell migration. {ECO:0000269|PubMed:12881528, ECO:0000269|PubMed:16076871}.; MUTAGEN 1231 1231 Y->F: Loss of phosphorylation site. Strongly reduces stimulation of cell proliferation and cell migration. {ECO:0000269|PubMed:12881528, ECO:0000269|PubMed:16076871}.; MUTAGEN 1265 1265 Y->F: Loss of phosphorylation site. No effect on stimulation of cell proliferation and cell migration. {ECO:0000269|PubMed:12881528}.; MUTAGEN 1333 1333 Y->F: Loss of phosphorylation site. Reduced autophosphorylation. {ECO:0000269|PubMed:12881528, ECO:0000269|PubMed:7675451}.; MUTAGEN 1337 1337 Y->F: Reduced autophosphorylation. Strongly reduces stimulation of cell proliferation and cell migration. {ECO:0000269|PubMed:12881528, ECO:0000269|PubMed:20431062, ECO:0000269|PubMed:7675451}.; MUTAGEN 1363 1363 Y->F: Loss of phosphorylation site. Slighly reduced autophosphorylation. {ECO:0000269|PubMed:12881528, ECO:0000269|PubMed:7675451}.
Post-translational: Autophosphorylated on tyrosine residues upon ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation in response to H(2)O(2) is mediated by a process that requires SRC and PRKCD activity. Phosphorylation at Tyr-1068 is required for autophosphorylation at additional tyrosine residues. Phosphorylation at Tyr-1063 and Tyr-1337 is important for interaction with CRK and subsequent activation of MAPK8. Phosphorylation at Tyr-1230, Tyr-1231 and Tyr-1337 is important for interaction with GRB2 and subsequent activation of the AKT1 and MAPK1/ERK2 and/or MAPK3/ERK1 signaling pathways. In response to endothelial cell adhesion onto collagen, can also be phosphorylated in the absence of FLT4 kinase activity by SRC at Tyr-830, Tyr-833, Tyr-853, Tyr-1063, Tyr-1333, and Tyr-1337. {ECO:0000269|PubMed:12881528, ECO:0000269|PubMed:15102829, ECO:0000269|PubMed:15474514, ECO:0000269|PubMed:16076871, ECO:0000269|PubMed:20431062, ECO:0000269|PubMed:8700872}.
Involvement in disease: Lymphedema, hereditary, 1A (LMPH1A) [MIM:153100]: A chronic disabling condition which results in swelling of the extremities due to altered lymphatic flow. Patients with lymphedema suffer from recurrent local infections and physical impairment. {ECO:0000269|PubMed:10835628, ECO:0000269|PubMed:10856194, ECO:0000269|PubMed:16924388, ECO:0000269|PubMed:16965327, ECO:0000269|PubMed:17458866, ECO:0000269|PubMed:19289394, ECO:0000269|PubMed:26091405, ECO:0000269|PubMed:9817924}. Note=The disease is caused by mutations affecting the gene represented in this entry.; Hemangioma, capillary infantile (HCI) [MIM:602089]: A condition characterized by dull red, firm, dome-shaped hemangiomas, sharply demarcated from surrounding skin, usually presenting at birth or occurring within the first two or three months of life. They result from highly proliferative, localized growth of capillary endothelium and generally undergo regression and involution without scarring. {ECO:0000269|PubMed:11807987}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; Note=Plays an important role in tumor lymphangiogenesis, in cancer cell survival, migration, and formation of metastases.
Sequence similarity: Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.; Contains 7 Ig-like C2-type (immunoglobulin-like) domains. {ECO:0000305}.; Contains 1 protein kinase domain. {ECO:0000255|PROSITE-ProRule:PRU00159}.
General information above from UniProt

Vascular endothelial growth factor receptor 3 (VEGFR3), also known as FLT-4, together with the other two members VEGFR1 (FLT-1) and VEGFR2 (KDR/Flk-1) are receptors for vascular endothelial growth factors (VEGF) and belong to the class III subfamily of receptor tyrosine kinases (RTKs). The VEGFR3 protein is expressed mainly on lymphatic vessels but it is also up-regulated in tumor angiogenesis. Mutations in VEGFR3 have been identified in patients with primary lymphoedema. The VEGF-C/VEGF-D/VEGFR3 signaling pathway may provide a target for antilymphangiogenic therapy in prostate cancer, breast cancer, gastric cancer, lung cancer, non-small cell lung cancer (NSCLC), and so on.

Immune Checkpoint   Immunotherapy   Cancer Immunotherapy   Targeted Therapy

VEGFR3/FLT-4  Alternative Name

VEGFR3/FLT-4  Related Studies

  • Shushanov S, et al. (2000)VEGFc and VEGFR3 expression in human thyroid pathologies. Int J Cancer.86(1): 47-52.
  • Iljin K, et al. (2001) VEGFR3 gene structure, regulatory region, and sequence polymorphisms. FASEB J. 15(6): 1028-36.
  • Liu XE, et al. (2004) Expression and significance of VEGF-C and FLT-4 in gastric cancer. World J Gastroenterol. 10(3): 352-5.
  • Stearns ME, et al. (2004) Expression of a flt-4 (VEGFR3) splicing variant in primary human prostate tumors. VEGF D and flt-4t(Delta773-1081) overexpression is diagnostic for sentinel lymph node metastasis. Lab Invest. 84(6): 785-95.
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