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0VGFR3_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameFLT4
DescriptionVascular endothelial growth factor receptor 3 precursor (ec 2.7.1.112) (vegfr-3) (tyrosine-protein kinase receptor flt4).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005887 integral to plasma membrane (TAS)
0005021 vascular endothelial growth factor receptor... (TAS)
0007169 transmembrane receptor protein tyrosine kin... (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Protein kinases comprise a large family of enzymes that mediate the response of eukaryotic cells to external stimuli by phosphorylation of hydroxyamino acids. The enzymes fall into two broad classes.haracterised with respect to substrate specificity: serine/threonine specific and tyrosine specific . Tyrosine phosphorylating activity was originally detected in two viral transforming proteins .ut many retroviral transforming proteins and their cellular counterparts have since been shown to possess such activity. The growth factor receptors.hich are activated by ligand binding.nd theinsulin-related peptide receptor.re also family members.
  IPR001245:Tyrosine protein kinase
The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda.ach composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha.elta.psilon.amma and mu.ll consisting of a variable domain (VH) and three (in alpha.elta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins.n which the variable and constant domains have clear.onserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; ).1-set (constant-1; ).2-set (constant-2; ) and I-set (intermediate; ) . Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure.ith the types differing in the number of strands in the beta-sheets as well as in their sequence patterns .Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. Ig-like domains are involved in a variety of functions.ncluding cell-cell recognition.ell-surface receptors.uscle structure and the immune system . This entry represents I-set domains.hich are found in several cell adhesion molecules.ncluding vascular (VCAM).ntercellular (ICAM).eural (NCAM) and mucosal addressin (MADCAM) cell adhesion molecules.s well as junction adhesion molecules (JAM). I-set domains are also present in several other diverse protein families.ncluding several tyrosine-protein kinase receptors.he hemolymph protein hemolin.he muscle proteins titin.elokin.nd twitchin.he neuronal adhesion molecule axonin-1 .nd the signalling molecule semaphorin 4D that is involved in axonal guidance.mmune function and angiogenesis .
  IPR013098:Immunoglobulin I-set
This entry is for immunoglobulin-like domains. Studies indicate that the interactions essential for defining the structure of these beta sandwich proteins are also important in nucleation of folding.nd that proteins containing this fold may share similar folding pathways even though the proteins may have low sequence homology. The fold consists of a beta-sandwich formed of 7 strands in 2 sheets with a Greek-key topology. Some members of the fold have additional strands. The Pfam alignments do not include the first and last strand of the immunoglobulin-like domain.
  IPR013151:Immunoglobulin
The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda.ach composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha.elta.psilon.amma and mu.ll consisting of a variable domain (VH) and three (in alpha.elta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins.n which the variable and constant domains have clear.onserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; ).1-set (constant-1; ).2-set (constant-2; ) and I-set (intermediate; ) . Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure.ith the types differing in the number of strands in the beta-sheets as well as in their sequence patterns .Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. Ig-like domains are involved in a variety of functions.ncluding cell-cell recognition.ell-surface receptors.uscle structure and the immune system . This entry represents a subtype of the immunoglobulin domain.nd is found in a diverse range of protein families that includes glycoproteins.ibroblast growth factor receptors.ascular endothelial growth factor receptors.nterleukin-6 receptor.nd neural cell adhesion molecules. It also includes proteins that are classified as unassigned proteinase inhibitors belonging to MEROPS inhibitor families I2.17 and I43 .
  IPR003598:Immunoglobulin subtype 2
The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda.ach composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha.elta.psilon.amma and mu.ll consisting of a variable domain (VH) and three (in alpha.elta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins.n which the variable and constant domains have clear.onserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; ).1-set (constant-1; ).2-set (constant-2; ) and I-set (intermediate; ) . Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure.ith the types differing in the number of strands in the beta-sheets as well as in their sequence patterns .Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. Ig-like domains are involved in a variety of functions.ncluding cell-cell recognition.ell-surface receptors.uscle structure and the immune system . This subfamily includes:Cell surface receptors containing an immunoglobin domain.Killer cell inhibitory receptors.Oprin a snake venom metalloproteinase inhibitor from Didelphis marsupialis (Southern opossum) .hich belongs to MEROPS inhibitor family I43.lan I- .Oprin homologues.
  IPR003599:Immunoglobulin subtype
Eukaryotic protein kinases are enzymesthat belong to a very extensive family of proteins which share a conserved catalytic core common withboth serine/threonine and tyrosine protein kinases. There are a number of conserved regions in thecatalytic domain of protein kinases. In the N-terminal extremity of the catalytic domain there is aglycine-rich stretch of residues in the vicinity of a lysine residue.hich has been shown to be involvedin ATP binding. In the central part of the catalytic domain there is a conserved aspartic acid residuewhich is important for the catalytic activity of the enzyme . This entry includes protein kinases from eukaryotes and viruses and may include some bacterial hits too.
  IPR000719:Protein kinase
Vascular endothelial growth factor (VEGF) is a potent and specificendothelial cell mitogen . Through binding with its receptor.EGFR.EGFhas critical roles in the growth and maintenance of vascular endothelialcells and in the development of new blood- and lymphatic-vessels inphysiological and pathological states . The vessel systems are important for the supply of oxygen and nutrients to all tissues of the body.s wellas for the drainage of excess fluids with waste metabolites from peripheraltissues. VEGF receptors have a characteristic structure.ith 7 Ig-likedomains in the extracellular domain and a cytoplasmic tyrosine kinase domainwith a long kinase insert region.The VEGF receptor family consists of three members.EGFR-1 (Flt-1).EGFR-2(KDR/Flk-1) and VEGFR-3 (Flt-4).ll of which belong to the receptor typetyrosine kinase superfamily . Among these receptors.EGFR-1 bindsstrongest to VEGF.EGF-2 binds more weakly.nd VEGFR-3 shows essentiallyno binding.lthough it does bind to other members of the VEGF family.This entry represents an N-terminal region of VEGFR proteins.ontainign several Ig domains.
  IPR009134:Vascular endothelial growth factor receptor, VEGFR, N-terminal
Vascular endothelial growth factor (VEGF) is a potent and specificendothelial cell mitogen . Through binding with its receptor.EGFR.EGFhas critical roles in the growth and maintenance of vascular endothelialcells and in the development of new blood- and lymphatic-vessels inphysiological and pathological states . The vessel systems are important for the supply of oxygen and nutrients to all tissues of the body.s wellas for the drainage of excess fluids with waste metabolites from peripheraltissues. VEGF receptors have a characteristic structure.ith 7 Ig-likedomains in the extracellular domain and a cytoplasmic tyrosine kinase domainwith a long kinase insert region.The VEGF receptor family consists of three members.EGFR-1 (Flt-1).EGFR-2(KDR/Flk-1) and VEGFR-3 (Flt-4).ll of which belong to the receptor typetyrosine kinase superfamily . Among these receptors.EGFR-1 bindsstrongest to VEGF.EGF-2 binds more weakly.nd VEGFR-3 shows essentiallyno binding.lthough it does bind to other members of the VEGF family.In humans.n A to G transition corresponding to a histidine to argininesubstitution in the catalytic loop of VEGFR3 has been linked to congenitalhereditary lymphoedema. In vitro expression studies show that this amino acidsubstitution causes loss of VEGFR3 tyrosine kinase activity. Thus.efectiveVEGFR3 signalling is responsible for 5q34-q35-linked congenital hereditarylymphedema.This entry represents the N-terminal region of VEGFR-3 proteins. This region contains the N-terminal signalling region and some of the Ig domains.
  IPR009137:Vascular endothelial growth factor receptor 3, VEGFR3, N-terminal
Protein kinases () catalyze the phosphotransfer reaction fundamental to most signalling and regulatory processes in the eukaryotic cell . The catalytic subunit contains a core that is common to both serine/threonine and tyrosine protein kinases. The catalytic domain contains the nucleotide-binding site and the catalytic apparatus in an inter-lobe cleft. Structurally it shares functional and structural similarities with the ATP-grasp fold.hich is found in enzymes that catalyse the formation of an amide bond.nd with PIPK (phosphoinositol phosphate kinase). The three-dimensional fold of the protein kinase catalytic domain is similar to domains found in several other proteins. These include the catalytic domain of actin-fragmin kinase.n atypical protein kinase that regulates the F-actin capping activity in plasmodia ; the catalytic domain of phosphoinositide-3-kinase (PI3K).hich phosphorylates phosphoinositides and as such is involved in a number of fundamental cellular processes such as apoptosis.roliferation.otility and adhesion ; the catalytic domain of the MHCK/EF2 kinase.n atypical protein kinase that includes the TRP (transient channel potential) calcium-channel kinase involved in the modulation of calcium channels in eukaryotic cells in response to external signals ; choline kinase.hich catalyses the ATP-dependent phosphorylation of choline during the biosynthesis of phosphatidylcholine ; and 3.-aminoglycoside phosphotransferase type IIIa. bacterial enzyme that confers resistance to a range of aminoglycoside antibiotics .
  IPR011009:Protein kinase-like
This entry represents domains with an immunoglobulin-like (Ig-like) fold.hich consists of a beta-sandwich of seven or more strands in two sheets with a Greek-key topology. Ig-like domains are one of the most common protein modules found in animals.ccurring in a variety of different proteins. These domains are often involved in interactions.ommonly with other Ig-like domains via their beta-sheets . Domains within this fold-family share the same structure.ut can diverge with respect to their sequence. Based on sequence.g-like domains can be classified as V-set domains (antibody variable domain-like).1-set domains (antibody constant domain-like).2-set domains.nd I-set domains (antibody intermediate domain-like). Proteins can contain more than one of these types of Ig-like domains. For example.n the human T-cell receptor antigen CD2.omain 1 (D1) is a V-set domain.hile domain 2 (D2) is a C2-set domain.oth domains having the same Ig-like fold .Domains with an Ig-like fold can be found in many.iverse proteins in addition to immunoglobulin molecules. For example.g-like domains occur in several different types of receptors (such as various T-cell antigen receptors).everal cell adhesion molecules.HC class I and II antigens.s well as the hemolymph protein hemolin.nd the muscle proteins titin.elokin and twitchin.
  IPR013783:Immunoglobulin-like fold
IPR001245:Pkinase_Tyr 
Evalue:-151 
Location:845-1169IPR003598:IGc2 
Evalue:-14.8538719643218 
Location:690-755IPR003599:IG 
Evalue:-8.79588001734407 
Location:237-328IPR003598:IGc2 
Evalue:-3.74472749489669 
Location:569-660IPR003599:IG 
Evalue:-0.1249387366083 
Location:36-133IPR013783:Ig-like_fold 
Evalue:0 
Location:425-556IPR013783:Ig-like_fold 
Evalue:0 
Location:336-424IPR009137:VEGFRECEPTR3 
Evalue:0 
Location:199-228IPR009137:VEGFRECEPTR3 
Evalue:0 
Location:2-29IPR009137:VEGFRECEPTR3 
Evalue:0 
Location:159-177IPR009134:VEGFRECEPTOR 
Evalue:0 
Location:183-193
SequencesProtein: VGFR3_HUMAN (1298 aa)
mRNA: NM_002020 NM_182925
Local Annotation
Synapse Ontology
the plasma membrane of the postsynaptic neuron. It apposes with presynaptic actiove zone.
sdb:0108 postsynaptic plasma membrane  (Evidence:keywords)
activation of protein kinase C
sdb:0206 activation of protein kinase C  (Evidence:keywords)
KO assignmentK05097
  Level 3 annotation:
    FMS-like tyrosine kinase 4
  Level 2 annotation:
    Cytokine receptors
    Cytokine-cytokine receptor interaction
    Focal adhesion
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 284 residues, 179962147-179962996Exon2: 30 residues, 179968573-179968659Exon3: 42 residues, 179969510-179969631Exon4: 51 residues, 179970936-179971085Exon5: 37 residues, 179972111-179972217Exon6: 35 residues, 179972616-179972716Exon7: 39 residues, 179973673-179973785Exon8: 43 residues, 179975972-179976095Exon9: 33 residues, 179976505-179976600Exon10: 52 residues, 179978375-179978526Exon11: 31 residues, 179978626-179978715Exon12: 40 residues, 179978858-179978972Exon13: 37 residues, 179979270-179979375Exon14: 47 residues, 179979778-179979914Exon15: 37 residues, 179980214-179980321Exon16: 46 residues, 179980481-179980613Exon17: 51 residues, 179980711-179980858Exon18: 123 residues, 179981147-179981510Exon19: 38 residues, 179982336-179982445Exon20: 44 residues, 179983540-179983667Exon21: 56 residues, 179985474-179985637Exon22: 53 residues, 179985716-179985871Exon23: 41 residues, 179988487-179988605Exon24: 58 residues, 179988864-179989033Exon25: 48 residues, 179989301-179989441Exon26: 56 residues, 179989548-179989711Exon27: 39 residues, 179989830-179989943Exon28: 83 residues, 179990160-179990405Exon29: 34 residues, 179991287-179991384Exon30: 28 residues, 180009093-180009171Exon31: 2 residues, -Jump to VGFR3_HUMANExon1: 178 residues, 179967359-179967890Exon2: 30 residues, 179968573-179968659Exon3: 42 residues, 179969510-179969631Exon4: 51 residues, 179970936-179971085Exon5: 37 residues, 179972111-179972217Exon6: 35 residues, 179972616-179972716Exon7: 39 residues, 179973673-179973785Exon8: 43 residues, 179975972-179976095Exon9: 33 residues, 179976505-179976600Exon10: 52 residues, 179978375-179978526Exon11: 31 residues, 179978626-179978715Exon12: 40 residues, 179978858-179978972Exon13: 37 residues, 179979270-179979375Exon14: 47 residues, 179979778-179979914Exon15: 37 residues, 179980214-179980321Exon16: 46 residues, 179980481-179980613Exon17: 51 residues, 179980711-179980858Exon18: 123 residues, 179981147-179981510Exon19: 38 residues, 179982336-179982445Exon20: 44 residues, 179983540-179983667Exon21: 56 residues, 179985474-179985637Exon22: 53 residues, 179985716-179985871Exon23: 41 residues, 179988487-179988605Exon24: 58 residues, 179988864-179989033Exon25: 48 residues, 179989301-179989441Exon26: 56 residues, 179989548-179989711Exon27: 39 residues, 179989830-179989943Exon28: 83 residues, 179990160-179990405Exon29: 34 residues, 179991287-179991384Exon30: 28 residues, 180009093-180009172Exon31: 2 residues, -Jump to VGFR3_HUMAN  
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