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P35917

- VGFR3_MOUSE

UniProt

P35917 - VGFR3_MOUSE

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Protein
Vascular endothelial growth factor receptor 3
Gene
Flt4, Flt-4, Vegfr3
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFC and VEGFD, and plays an essential role in adult lymphangiogenesis and in the development of the vascular network and the cardiovascular system during embryonic development. Promotes proliferation, survival and migration of endothelial cells, and regulates angiogenic sprouting. Signaling by activated FLT4 leads to enhanced production of VEGFC, and to a lesser degree VEGFA, thereby creating a positive feedback loop that enhances FLT4 signaling. Modulates KDR signaling by forming heterodimers. Mediates activation of the MAPK1/ERK2, MAPK3/ERK1 signaling pathway, of MAPK8 and the JUN signaling pathway, and of the AKT1 signaling pathway. Phosphorylates SHC1. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase. Promotes phosphorylation of MAPK8 at 'Thr-183' and 'Tyr-185', and of AKT1 at 'Ser-473'.6 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Enzyme regulationi

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 By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei879 – 8791ATP By similarity
Active sitei1037 – 10371Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi851 – 8599ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein binding Source: IntAct
  3. vascular endothelial growth factor-activated receptor activity Source: MGI

GO - Biological processi

  1. blood vessel morphogenesis Source: UniProtKB
  2. lymph vessel development Source: BHF-UCL
  3. lymphangiogenesis Source: UniProtKB
  4. negative regulation of apoptotic process Source: Ensembl
  5. positive regulation of ERK1 and ERK2 cascade Source: Ensembl
  6. positive regulation of JNK cascade Source: Ensembl
  7. positive regulation of cell proliferation Source: MGI
  8. positive regulation of endothelial cell migration Source: Ensembl
  9. positive regulation of endothelial cell proliferation Source: Ensembl
  10. positive regulation of protein kinase C signaling Source: Ensembl
  11. positive regulation of protein phosphorylation Source: Ensembl
  12. positive regulation vascular endothelial growth factor production Source: Ensembl
  13. protein autophosphorylation Source: Ensembl
  14. regulation of blood vessel remodeling Source: UniProtKB
  15. sprouting angiogenesis Source: UniProtKB
  16. vascular endothelial growth factor receptor signaling pathway Source: InterPro
  17. vascular endothelial growth factor signaling pathway Source: GOC
  18. vasculature development Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Angiogenesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.
ReactomeiREACT_205099. VEGF binds to VEGFR leading to receptor dimerization.

Names & Taxonomyi

Protein namesi
Recommended name:
Vascular endothelial growth factor receptor 3 (EC:2.7.10.1)
Short name:
VEGFR-3
Alternative name(s):
Fms-like tyrosine kinase 4
Short name:
FLT-4
Tyrosine-protein kinase receptor FLT4
Gene namesi
Name:Flt4
Synonyms:Flt-4, Vegfr3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:95561. Flt4.

Subcellular locationi

Cell membrane; Single-pass type I membrane protein. Cytoplasm. Nucleus By similarity
Note: Ligand-mediated autophosphorylation leads to rapid internalization.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 775751Extracellular Reviewed prediction
Add
BLAST
Transmembranei776 – 79621Helical; Reviewed prediction
Add
BLAST
Topological domaini797 – 1363567Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. integral component of plasma membrane Source: InterPro
  3. nucleus Source: UniProtKB-SubCell
  4. receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

Embryonic lethality at about 13 dpc, due to failure of remodeling of the yolk sac capillary network and defects in remodeling and maturation of primary vascular networks.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424 Reviewed prediction
Add
BLAST
Chaini25 – 13631339Vascular endothelial growth factor receptor 3
PRO_0000016777Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi33 – 331N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi51 ↔ 111 By similarity
Glycosylationi104 – 1041N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi158 ↔ 206 By similarity
Glycosylationi166 – 1661N-linked (GlcNAc...) Reviewed prediction
Glycosylationi251 – 2511N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi252 ↔ 310 By similarity
Glycosylationi299 – 2991N-linked (GlcNAc...) Reviewed prediction
Glycosylationi411 – 4111N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi445 ↔ 534 By similarity
Glycosylationi515 – 5151N-linked (GlcNAc...) Reviewed prediction
Glycosylationi527 – 5271N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi578 ↔ 653 By similarity
Glycosylationi582 – 5821N-linked (GlcNAc...)1 Publication
Glycosylationi594 – 5941N-linked (GlcNAc...) Reviewed prediction
Glycosylationi683 – 6831N-linked (GlcNAc...) Reviewed prediction
Glycosylationi690 – 6901N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi699 ↔ 751 By similarity
Glycosylationi758 – 7581N-linked (GlcNAc...) Reviewed prediction
Modified residuei830 – 8301Phosphotyrosine; by SRC By similarity
Modified residuei833 – 8331Phosphotyrosine; by SRC By similarity
Modified residuei1063 – 10631Phosphotyrosine; by autocatalysis and SRC By similarity
Modified residuei1068 – 10681Phosphotyrosine; by autocatalysis By similarity
Modified residuei1230 – 12301Phosphotyrosine; by autocatalysis By similarity
Modified residuei1231 – 12311Phosphotyrosine; by autocatalysis By similarity
Modified residuei1265 – 12651Phosphotyrosine; by autocatalysis By similarity
Modified residuei1333 – 13331Phosphotyrosine; by autocatalysis and SRC By similarity
Modified residuei1337 – 13371Phosphotyrosine; by autocatalysis and SRC By similarity
Modified residuei1363 – 13631Phosphotyrosine; by autocatalysis By similarity

Post-translational modificationi

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 H2O2 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 By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP35917.
PRIDEiP35917.

PTM databases

PhosphoSiteiP35917.

Expressioni

Tissue specificityi

Expressed in adult lung and liver, and in fetal liver, brain, intestine and placenta.1 Publication

Gene expression databases

ArrayExpressiP35917.
BgeeiP35917.
CleanExiMM_FLT4.
GenevestigatoriP35917.

Interactioni

Subunit structurei

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 By similarity.

Binary interactionsi

WithEntry#Exp.IntActNotes
KdrP359182EBI-7845747,EBI-1555005

Protein-protein interaction databases

BioGridi199709. 3 interactions.
DIPiDIP-60714N.
IntActiP35917. 1 interaction.
MINTiMINT-5313593.
STRINGi10090.ENSMUSP00000020617.

Structurei

3D structure databases

ProteinModelPortaliP35917.
SMRiP35917. Positions 27-765, 821-1223.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 11875Ig-like C2-type 1
Add
BLAST
Domaini151 – 21363Ig-like C2-type 2
Add
BLAST
Domaini230 – 32697Ig-like C2-type 3
Add
BLAST
Domaini331 – 41585Ig-like C2-type 4
Add
BLAST
Domaini422 – 552131Ig-like C2-type 5
Add
BLAST
Domaini555 – 671117Ig-like C2-type 6
Add
BLAST
Domaini678 – 76487Ig-like C2-type 7
Add
BLAST
Domaini845 – 1173329Protein kinase
Add
BLAST

Domaini

The first and second Ig-like C2-type (immunoglobulin-like) domains are sufficient for VEGFC binding By similarity.

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000037949.
HOVERGENiHBG053432.
InParanoidiP35917.
KOiK05097.
OMAiPAHADIK.
OrthoDBiEOG75F4CC.
PhylomeDBiP35917.
TreeFamiTF325768.

Family and domain databases

Gene3Di2.60.40.10. 9 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR001824. Tyr_kinase_rcpt_3_CS.
IPR009137. VEGFR3_rcpt.
[Graphical view]
PANTHERiPTHR24416:SF49. PTHR24416:SF49. 1 hit.
PfamiPF07679. I-set. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR01835. VEGFRECEPTR3.
SMARTiSM00409. IG. 4 hits.
SM00408. IGc2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS50835. IG_LIKE. 5 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P35917-1 [UniParc]FASTAAdd to Basket

« Hide

MQPGAALNLR LWLCLGLLQG LANGYSMTPP TLNITEDSYV IDTGDSLSIS     50
CRGQHPLEWT WPGAQEVLTT GGKDSEDTRV VHDCEGTEAR PYCKVLLLAQ 100
THANNTGSYH CYYKYIKARI EGTTAASTYV FVRDFKHPFI NKPDTLLVNR 150
KDSMWVPCLV SIPGLNITLR SQSSALHPDG QEVLWDDRRG MRVPTQLLRD 200
ALYLQCETTW GDQNFLSNLF VVHITGNELY DIQLYPKKSM ELLVGEKLVL 250
NCTVWAEFDS GVTFDWDYPG KQAERAKWVP ERRSQQTHTE LSSILTIHNV 300
SQNDLGPYVC EANNGIQRFR ESTEVIVHEK PFISVEWLKG PVLEATAGDE 350
LVKLPVKLAA YPPPEFQWYK DRKAVTGRHN PHALVLKEVT EASAGVYTLA 400
LWNSAAGLRQ NISLELVVNV PPHIHEKEAS SPSIYSRHSR QTLTCTAYGV 450
PQPLSVQWHW RPWTPCKTFA QRSLRRRQQR DGMPQCRDWK EVTTQDAVNP 500
IESLDSWTEF VEGKNKTVSK LVIQDANVSA MYKCVVVNKV GQDERLIYFY 550
VTTIPDGFSI ESEPSEDPLE GQSVRLSCRA DNYTYEHLRW YRLNLSTLHD 600
AQGNPLLLDC KNVHLFATPL EANLEEAEPG ARHATLSLNI PRVAPEDEGD 650
YVCEVQDRRS QDKHCHKKYL SVQALEAPRL TQNLTDLLVN VSDSLEMRCP 700
VAGAHVPSIV WYKDERLLEK ESGIDLADSN QRLSIQRVRE EDAGRYLCSV 750
CNAKGCVNSS ASVAVEGSED KGSMEIVILI GTGVIAVFFW VLLLLIFCNM 800
KRPAHADIKT GYLSIIMDPG EVPLEEQCEY LSYDASQWEF PRERLHLGRV 850
LGHGAFGKVV EASAFGINKG SSCDTVAVKM LKEGATASEH RALMSELKIL 900
IHIGNHLNVV NLLGACTKPN GPLMVIVEFC KYGNLSNFLR VKRDTFNPYA 950
EKSPEQRRRF RAMVEGAKAD RRRPGSSDRA LFTRFLMGKG SARRAPLVQE 1000
AEDLWLSPLT MEDLVCYSFQ VARGMEFLAS RKCIHRDLAA RNILLSESDI 1050
VKICDFGLAR DIYKDPDYVR KGSARLPLKW MAPESIFDKV YTTQSDVWSF 1100
GVLLWEIFSL GASPYPGVQI NEEFCQRLKD GTRMRAPELA TPAIRHIMQS 1150
CWSGDPKARP AFSDLVEILG DLLQGGGWQE EEEERMALHS SQSSEEDGFM 1200
QASTTALHIT EADADDSPPS MHCHSLAARY YNCVSFPGRL ARGTKTPGSS 1250
RMKTFEELPM TPTTYKASMD NQTDSGMVLA SEEFEELESR HRPEGSFSCK 1300
GPGQHMDIPR GHPDPQGRRR RPTQGAQGGK VFYNNEYGEV SQPCTEGDCC 1350
PSAGSTFFAD SSY 1363
Length:1,363
Mass (Da):153,016
Last modified:June 1, 1994 - v1
Checksum:iF1BF8A2BDEF99BE9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L07296 mRNA. Translation: AAA40077.1.
CCDSiCCDS24618.1.
PIRiI58375.
RefSeqiNP_032055.1. NM_008029.3.
UniGeneiMm.3291.

Genome annotation databases

EnsembliENSMUST00000020617; ENSMUSP00000020617; ENSMUSG00000020357.
GeneIDi14257.
KEGGimmu:14257.
UCSCiuc007iqu.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L07296 mRNA. Translation: AAA40077.1 .
CCDSi CCDS24618.1.
PIRi I58375.
RefSeqi NP_032055.1. NM_008029.3.
UniGenei Mm.3291.

3D structure databases

ProteinModelPortali P35917.
SMRi P35917. Positions 27-765, 821-1223.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199709. 3 interactions.
DIPi DIP-60714N.
IntActi P35917. 1 interaction.
MINTi MINT-5313593.
STRINGi 10090.ENSMUSP00000020617.

Chemistry

BindingDBi P35917.

PTM databases

PhosphoSitei P35917.

Proteomic databases

PaxDbi P35917.
PRIDEi P35917.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000020617 ; ENSMUSP00000020617 ; ENSMUSG00000020357 .
GeneIDi 14257.
KEGGi mmu:14257.
UCSCi uc007iqu.2. mouse.

Organism-specific databases

CTDi 2324.
MGIi MGI:95561. Flt4.

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000037949.
HOVERGENi HBG053432.
InParanoidi P35917.
KOi K05097.
OMAi PAHADIK.
OrthoDBi EOG75F4CC.
PhylomeDBi P35917.
TreeFami TF325768.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 3474.
Reactomei REACT_205099. VEGF binds to VEGFR leading to receptor dimerization.

Miscellaneous databases

NextBioi 285591.
PROi P35917.
SOURCEi Search...

Gene expression databases

ArrayExpressi P35917.
Bgeei P35917.
CleanExi MM_FLT4.
Genevestigatori P35917.

Family and domain databases

Gene3Di 2.60.40.10. 9 hits.
InterProi IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR001824. Tyr_kinase_rcpt_3_CS.
IPR009137. VEGFR3_rcpt.
[Graphical view ]
PANTHERi PTHR24416:SF49. PTHR24416:SF49. 1 hit.
Pfami PF07679. I-set. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view ]
PRINTSi PR01835. VEGFRECEPTR3.
SMARTi SM00409. IG. 4 hits.
SM00408. IGc2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 2 hits.
PROSITEi PS50835. IG_LIKE. 5 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of murine FLT and FLT4."
    Finnerty H., Kelleher K., Morris G.E., Bean K., Merberg D.M., Kriz R., Morris J.C., Sookdeo H., Turner K.J., Wood C.R.
    Oncogene 8:2293-2298(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
  2. "Chromosomal localization of FLT4, a novel receptor-type tyrosine kinase gene."
    Galland F., Karamysheva A., Mattei M.-G., Rosnet O., Marchetto S., Birnbaum D.
    Genomics 13:475-478(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1033-1072.
  3. "Cardiovascular failure in mouse embryos deficient in VEGF receptor-3."
    Dumont D.J., Jussila L., Taipale J., Lymboussaki A., Mustonen T., Pajusola K., Breitman M., Alitalo K.
    Science 282:946-949(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  4. "Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
    Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
    J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-582.
    Strain: C57BL/6.
    Tissue: Plasma.
  5. Cited for: FUNCTION, TISSUE SPECIFICITY.
  6. "VEGFR-3 ligand-binding and kinase activity are required for lymphangiogenesis but not for angiogenesis."
    Zhang L., Zhou F., Han W., Shen B., Luo J., Shibuya M., He Y.
    Cell Res. 20:1319-1331(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN LYMPHANGIOGENESIS.
  7. Cited for: FUNCTION IN ACTIVATION OF SIGNALING PATHWAYS, SUBCELLULAR LOCATION.
  8. "Soluble vascular endothelial growth factor receptor-3 suppresses lymphangiogenesis and lymphatic metastasis in bladder cancer."
    Yang H., Kim C., Kim M.J., Schwendener R.A., Alitalo K., Heston W., Kim I., Kim W.J., Koh G.Y.
    Mol. Cancer 10:36-36(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN LYMPHANGIOGENESIS, ROLE IN CANCER.
  9. Cited for: FUNCTION.

Entry informationi

Entry nameiVGFR3_MOUSE
AccessioniPrimary (citable) accession number: P35917
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: September 3, 2014
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi