Flt1
entrez
14254
canonical
uniprot
P35969
canonical
ensembl
ENSMUSG00000029648
resolver
ensp
ENSMUSP00000031653
resolver
ensp
ENSMUSP00000106158
resolver
ensp
ENSMUSP00000284247
resolver
ensp
ENSMUSP00000284248
resolver
ensp
ENSMUSP00000284249
resolver
enst
ENSMUST00000110529
resolver
genesymbol
Flt1
resolver
genesymbol_syn
Emrk2
resolver
genesymbol_syn
Flt
resolver
genesymbol_syn
Vegfr1
resolver
uniprot
A0A0R4J0A4
resolver
uniprot
F6VD03
resolver
uniprot
O55094
resolver
uniprot
O55095
resolver
uniprot
Q61517
resolver
uniprot_entry
F6VD03_MOUSE
resolver
uniprot_entry
O55095_MOUSE
resolver
uniprot_entry
VGFR1_MOUSE
resolver
uniprot_sec
A0A0R4J0A4
resolver
uniprot_sec
O55094
resolver
uniprot_sec
Q61517
resolver
activity_regulation
ACTIVITY REGULATION: Present in an inactive conformation in the absence of bound ligand. Binding of VEGFA, VEGFB or PGF leads to dimerization and activation by autophosphorylation on tyrosine residues (By similarity). {ECO:0000250}.
uniprot
proteins
amino_acid_sequence
MVSCWDTAVLPYALLGCLLLTGYGSGSKLKVPELSLKGTQHVMQAGQTLFLKCRGEAAHSWSLPTTVSQEDKRLSITPPSACGRDNRQFCSTLTLDTAQANHTGLYTCRYLPTSTSKKKKAESSIYIFVSDAGSPFIEMHTDIPKLVHMTEGRQLIIPCRVTSPNVTVTLKKFPFDTLTPDGQRITWDSRRGFIIANATYKEIGLLNCEATVNGHLYQTNYLTHRQTNTILDVQIRPPSPVRLLHGQTLVLNCTATTELNTRVQMSWNYPGKATKRASIRQRIDRSHSHNNVFHSVLKINNVESRDKGLYTCRVKSGSSFQSFNTSVHVYEKGFISVKHRKQPVQETTAGRRSYRLSMKVKAFPSPEIVWLKDGSPATLKSARYLVHGYSLIIKDVTTEDAGDYTILLGIKQSRLFKNLTATLIVNVKPQIYEKSVSSLPSPPLYPLGSRQVLTCTVYGIPRPTITWLWHPCHHNHSKERYDFCTENEESFILDPSSNLGNRIESISQRMTVIEGTNKTVSTLVVADSQTPGIYSCRAFNKIGTVERNIKFYVTDVPNGFHVSLEKMPAEGEDLKLSCVVNKFLYRDITWILLRTVNNRTMHHSISKQKMATTQDYSITLNLVIKNVSLEDSGTYACRARNIYTGEDILRKTEVLVRDSEAPHLLQNLSDYEVSISGSTTLDCQARGVPAPQITWFKNNHKIQQEPGIILGPGNSTLFIERVTEEDEGVYRCRATNQKGAVESAAYLTVQGTSDKSNLELITLTCTCVAATLFWLLLTLFIRKLKRSSSEVKTDYLSIIMDPDEVPLDEQCERLPYDASKWEFARERLKLGKSLGRGAFGKVVQASAFGIKKSPTCRTVAVKMLKEGATASEYKALMTELKILTHIGHHLNVVNLLGACTKQGGPLMVIVEYCKYGNLSNYLKSKRDLFCLNKDAALHMELKKESLEPGLEQGQKPRLDSVSSSSVTSSSFPEDRSVSDVEGDEDYSEISKQPLTMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIYKNPDYVRRGDTRLPLKWMAPESIFDKVYSTKSDVWSYGVLLWEIFSLGGSPYPGVQMDEDFCSRLKEGMRMRTPEYATPEIYQIMLDCWHKDPKERPRFAELVEKLGDLLQANVQQDGKDYIPLNAILTRNSGFTYSTPTFSEDLFKDGFADPHFHSGSSDDVRYVNAFKFMSLERIKTFEELSPNSTSMFEDYQLDTSTLLGSPLLKRFTWTETKPKASMKIDLRIASKSKEAGLSDLPRPSFCFSSCGHIRPVQDDESELGKESCCSPPPDYNSVVLYSSPPA
uniprot
proteins
ec_number
2.7.10.1
uniprot
proteins
function
FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFB and PGF, and plays an essential role in the development of embryonic vasculature, the regulation of angiogenesis, cell survival, cell migration, macrophage function, chemotaxis, and cancer cell invasion. Acts as a positive regulator of postnatal retinal hyaloid vessel regression (PubMed:30936473). May play an essential role as a negative regulator of embryonic angiogenesis by inhibiting excessive proliferation of endothelial cells. Can promote endothelial cell proliferation, survival and angiogenesis in adulthood. Its function in promoting cell proliferation seems to be cell-type specific. Promotes PGF-mediated proliferation of endothelial cells, and proliferation of some types of cancer cells, but does not promote proliferation of normal fibroblasts. Has very high affinity for VEGFA and relatively low protein kinase activity; may function as a negative regulator of VEGFA signaling by limiting the amount of free VEGFA and preventing its binding to KDR. Modulates KDR signaling by forming heterodimers with KDR. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leading to the activation of phosphatidylinositol kinase and the downstream signaling pathway. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Phosphorylates SRC, YES1 and PLCG, and may also phosphorylate CBL. Promotes phosphorylation of AKT1 and PTK2/FAK1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P17948, ECO:0000269|PubMed:11221852, ECO:0000269|PubMed:14982871, ECO:0000269|PubMed:18583712, ECO:0000269|PubMed:20924106, ECO:0000269|PubMed:30936473, ECO:0000269|PubMed:7596436, ECO:0000269|PubMed:9689083}.
uniprot
proteins
mass_dalton
149846
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000250}.; PTM: Ubiquitinated after VEGFA-mediated autophosphorylation, leading to proteolytic degradation. {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-1169 is important for interaction with PLCG. Phosphorylation at Tyr-1213 is important for interaction with PIK3R1, PTPN11, GRB2, and PLCG. Phosphorylation at Tyr-1328 is important for endocytosis and for interaction with CBL, NCK1 and CRK. Is probably dephosphorylated by PTPRB (By similarity). {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
11221852
uniprot
proteins
pubmed
14982871
uniprot
proteins
pubmed
18583712
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20924106
uniprot
proteins
pubmed
30936473
uniprot
proteins
pubmed
7596436
uniprot
proteins
pubmed
8134130
uniprot
proteins
pubmed
8393164
uniprot
proteins
pubmed
9524283
uniprot
proteins
pubmed
9689083
uniprot
proteins
sequence_length
1333
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Endosome {ECO:0000250}. Note=Autophosphorylation promotes ubiquitination and endocytosis. {ECO:0000250}.
uniprot
proteins
transmembrane_region
TRANSMEM 760..781; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins