Kdr
entrez
16542
canonical
uniprot
P35918
canonical
ensembl
ENSMUSG00000062960
resolver
ensp
ENSMUSP00000109144
resolver
ensp
ENSMUSP00000322898
resolver
ensp
ENSMUSP00000322900
resolver
genesymbol
Kdr
resolver
genesymbol_syn
Flk-1
resolver
genesymbol_syn
Flk1
resolver
uniprot
C5H7S5
resolver
uniprot
Q8VCD0
resolver
uniprot_entry
VGFR2_MOUSE
resolver
uniprot_sec
C5H7S5
resolver
uniprot_sec
Q8VCD0
resolver
activity_regulation
ACTIVITY REGULATION: Present in an inactive conformation in the absence of bound ligand. Binding of VEGFA, VEGFC or VEGFD leads to dimerization and activation by autophosphorylation on tyrosine residues. May be regulated by hydrogen sulfide (H(2)S) levels via a sensitive intracellular disulfide bond (By similarity). {ECO:0000250}.
uniprot
proteins
amino_acid_sequence
MESKALLAVALWFCVETRAASVGLPGDFLHPPKLSTQKDILTILANTTLQITCRGQRDLDWLWPNAQRDSEERVLVTECGGGDSIFCKTLTIPRVVGNDTGAYKCSYRDVDIASTVYVYVRDYRSPFIASVSDQHGIVYITENKNKTVVIPCRGSISNLNVSLCARYPEKRFVPDGNRISWDSEIGFTLPSYMISYAGMVFCEAKINDETYQSIMYIVVVVGYRIYDVILSPPHEIELSAGEKLVLNCTARTELNVGLDFTWHSPPSKSHHKKIVNRDVKPFPGTVAKMFLSTLTIESVTKSDQGEYTCVASSGRMIKRNRTFVRVHTKPFIAFGSGMKSLVEATVGSQVRIPVKYLSYPAPDIKWYRNGRPIESNYTMIVGDELTIMEVTERDAGNYTVILTNPISMEKQSHMVSLVVNVPPQIGEKALISPMDSYQYGTMQTLTCTVYANPPLHHIQWYWQLEEACSYRPGQTSPYACKEWRHVEDFQGGNKIEVTKNQYALIEGKNKTVSTLVIQAANVSALYKCEAINKAGRGERVISFHVIRGPEITVQPAAQPTEQESVSLLCTADRNTFENLTWYKLGSQATSVHMGESLTPVCKNLDALWKLNGTMFSNSTNDILIVAFQNASLQDQGDYVCSAQDKKTKKRHCLVKQLIILERMAPMITGNLENQTTTIGETIEVTCPASGNPTPHITWFKDNETLVEDSGIVLRDGNRNLTIRRVRKEDGGLYTCQACNVLGCARAETLFIIEGAQEKTNLEVIILVGTAVIAMFFWLLLVIVLRTVKRANEGELKTGYLSIVMDPDELPLDERCERLPYDASKWEFPRDRLKLGKPLGRGAFGQVIEADAFGIDKTATCKTVAVKMLKEGATHSEHRALMSELKILIHIGHHLNVVNLLGACTKPGGPLMVIVEFCKFGNLSTYLRGKRNEFVPYKSKGARFRQGKDYVGELSVDLKRRLDSITSSQSSASSGFVEEKSLSDVEEEEASEELYKDFLTLEHLICYSFQVAKGMEFLASRKCIHRDLAARNILLSEKNVVKICDFGLARDIYKDPDYVRKGDARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGVKIDEEFCRRLKEGTRMRAPDYTTPEMYQTMLDCWHEDPNQRPSFSELVEHLGNLLQANAQQDGKDYIVLPMSETLSMEEDSGLSLPTSPVSCMEEEEVCDPKFHYDNTAGISHYLQNSKRKSRPVSVKTFEDIPLEEPEVKVIPDDSQTDSGMVLASEELKTLEDRNKLSPSFGGMMPSKSRESVASEGSNQTSGYQSGYHSDDTDTTVYSSDEAGLLKMVDAAVHADSGTTLRSPPV
uniprot
proteins
ec_number
2.7.10.1
uniprot
proteins
function
FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFC and VEGFD. Plays an essential role in the regulation of angiogenesis, vascular development, vascular permeability, and embryonic hematopoiesis. Promotes proliferation, survival, migration and differentiation of endothelial cells. Promotes reorganization of the actin cytoskeleton. Isoforms lacking a transmembrane domain, such as isoform 2, may function as decoy receptors for VEGFA, VEGFC and/or VEGFD. Isoform 2 plays an important role as a negative regulator of VEGFA- and VEGFC-mediated lymphangiogenesis by limiting the amount of free VEGFA and/or VEGFC and by preventing their binding to FLT4. Modulates FLT1 and FLT4 signaling by forming heterodimers. Binding of vascular growth factors to isoform 1 leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, reorganization of the actin cytoskeleton and activation of PTK2/FAK1. Required for VEGFA-mediated induction of NOS2 and NOS3, leading to the production of the signaling molecule nitric oxide (NO) by endothelial cells. Phosphorylates PLCG1. Promotes phosphorylation of FYN, NCK1, NOS3, PIK3R1, PTK2/FAK1 and SRC. {ECO:0000269|PubMed:12023952, ECO:0000269|PubMed:15673613, ECO:0000269|PubMed:19635461, ECO:0000269|PubMed:19652084, ECO:0000269|PubMed:19668192, ECO:0000269|PubMed:20705758, ECO:0000269|PubMed:7596435, ECO:0000269|PubMed:8356051}.
uniprot
proteins
mass_dalton
150462
uniprot
proteins
mutagenesis
MUTAGEN 866; /note="K->R: Loss of enzyme activity. Abolishes ubiquitination in response to VEGFA binding."; /evidence="ECO:0000269|PubMed:15673613"; MUTAGEN 1173; /note="Y->F: Loss of interaction with SHB."; /evidence="ECO:0000269|PubMed:15026417"; MUTAGEN 1188; /note="S->A: Strongly reduces internalization and down-regulation of the activated receptor; when associated with A-1191."; /evidence="ECO:0000269|PubMed:15673613"; MUTAGEN 1191; /note="S->A: Strongly reduces internalization and down-regulation of the activated receptor; when associated with A-1188."; /evidence="ECO:0000269|PubMed:15673613"; MUTAGEN 1212; /note="Y->F: Strongly reduced autophosphorylation."; /evidence="ECO:0000269|PubMed:12023952
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000250}.; PTM: Ubiquitinated. Tyrosine phosphorylation of the receptor promotes its poly-ubiquitination, leading to its degradation via the proteasome or lysosomal proteases (By similarity). {ECO:0000250}.; PTM: 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 at Tyr-949 is important for interaction with SH2D2A/TSAD and VEGFA-mediated reorganization of the actin cytoskeleton. Phosphorylation at Tyr-1173 is important for interaction with PLCG1 and SHB. Phosphorylation at Tyr-1212 is important for interaction with NCK1 and FYN. Dephosphorylated by PTPRJ at Tyr-799, Tyr-949, Tyr-994, Tyr-1052, Tyr-1057, Tyr-1173 and Tyr-1212 (By similarity). {ECO:0000250|UniProtKB:P35968}.; PTM: The inhibitory disulfide bond between Cys-1022 and Cys-1043 may serve as a specific molecular switch for H(2)S-induced modification that regulates KDR/VEGFR2 function. {ECO:0000250}.
uniprot
proteins
protein_family
CSF-1/PDGF receptor subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
10878616
uniprot
proteins
pubmed
12023952
uniprot
proteins
pubmed
12796773
uniprot
proteins
pubmed
12881528
uniprot
proteins
pubmed
15026417
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15673613
uniprot
proteins
pubmed
1717995
uniprot
proteins
pubmed
17702744
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19635461
uniprot
proteins
pubmed
19652084
uniprot
proteins
pubmed
19668192
uniprot
proteins
pubmed
20705758
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
7559454
uniprot
proteins
pubmed
7596435
uniprot
proteins
pubmed
7681362
uniprot
proteins
pubmed
8356051
uniprot
proteins
pubmed
8423988
uniprot
proteins
sequence_length
1345
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:15673613, ECO:0000269|PubMed:19635461, ECO:0000269|PubMed:19668192}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P35968}. Cell membrane {ECO:0000250|UniProtKB:P35968}. Note=Colocalizes with ERN1 and XBP1 in the endoplasmic reticulum in endothelial cells in a vascular endothelial growth factor (VEGF)-dependent manner (By similarity). Localized with RAP1A at cell-cell junctions. {ECO:0000250|UniProtKB:P35968}.; SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I membrane protein. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Early endosome {ECO:0000250}. Note=Detected on caveolae-enriched lipid rafts at the cell surface. Is recycled from the plasma membrane to endosomes and back again. Phosphorylation triggered by VEGFA binding promotes internalization and subsequent degradation. VEGFA binding triggers internalization and translocation to the nucleus (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
uniprot
proteins
transmembrane_region
TRANSMEM 763..783; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins