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Protein

Vascular endothelial growth factor receptor 1

Gene

Flt1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. 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).By similarity

Catalytic activityi

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

Enzyme regulationi

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei768 – 7692Cleavage; by PSEN1By similarity
Binding sitei862 – 8621ATPPROSITE-ProRule annotation
Active sitei1022 – 10221Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi834 – 8429ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • angiogenesis Source: UniProtKB
  • blood vessel morphogenesis Source: UniProtKB
  • cell differentiation Source: UniProtKB-KW
  • cell migration Source: UniProtKB
  • cellular response to vascular endothelial growth factor stimulus Source: MGI
  • embryonic morphogenesis Source: UniProtKB
  • monocyte chemotaxis Source: MGI
  • patterning of blood vessels Source: MGI
  • peptidyl-tyrosine phosphorylation Source: UniProtKB
  • positive regulation of angiogenesis Source: MGI
  • positive regulation of cell migration Source: MGI
  • positive regulation of hematopoietic progenitor cell differentiation Source: MGI
  • positive regulation of MAPK cascade Source: MGI
  • positive regulation of MAP kinase activity Source: MGI
  • positive regulation of phosphatidylinositol 3-kinase activity Source: MGI
  • positive regulation of phosphatidylinositol 3-kinase signaling Source: MGI
  • positive regulation of phospholipase C activity Source: MGI
  • positive regulation of vascular endothelial growth factor receptor signaling pathway Source: MGI
  • protein autophosphorylation Source: UniProtKB
  • response to hypoxia Source: MGI
  • sprouting angiogenesis Source: MGI
  • vascular endothelial growth factor receptor-1 signaling pathway Source: MGI
  • vascular endothelial growth factor receptor signaling pathway Source: MGI
  • vascular endothelial growth factor signaling pathway Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Angiogenesis, Chemotaxis, Differentiation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.
ReactomeiREACT_293283. VEGF binds to VEGFR leading to receptor dimerization.
REACT_336251. Neurophilin interactions with VEGF and VEGFR.

Names & Taxonomyi

Protein namesi
Recommended name:
Vascular endothelial growth factor receptor 1 (EC:2.7.10.1)
Short name:
VEGFR-1
Alternative name(s):
Embryonic receptor kinase 2
Fms-like tyrosine kinase 1
Short name:
FLT-1
Tyrosine-protein kinase receptor FLT
Gene namesi
Name:Flt1
Synonyms:Emrk2, Flt, Vegfr1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:95558. Flt1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 759737ExtracellularSequence AnalysisAdd
BLAST
Transmembranei760 – 78122HelicalSequence AnalysisAdd
BLAST
Topological domaini782 – 1333552CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Disruption phenotypei

Embryonic lethality at about 9 dpc, due to defects in the formation and organization of the vascular network. Mice display abnormal blood island structures in the yolk sac, leading to defects in the organization of the vascular endothelium, excess growth and disorganization of embryonic and extraembryonic vasculature, including the endocardium and the microvasculature. Mice expressing a mutant protein that lacks the kinase domain survive and have no apparent phenotype.3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 13331311Vascular endothelial growth factor receptor 1PRO_0000016769Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi53 ↔ 108PROSITE-ProRule annotation
Glycosylationi101 – 1011N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi159 ↔ 208PROSITE-ProRule annotation
Glycosylationi165 – 1651N-linked (GlcNAc...)Sequence Analysis
Glycosylationi197 – 1971N-linked (GlcNAc...)Sequence Analysis
Glycosylationi252 – 2521N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi253 ↔ 312PROSITE-ProRule annotation
Glycosylationi324 – 3241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi418 – 4181N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi455 ↔ 536PROSITE-ProRule annotation
Glycosylationi475 – 4751N-linked (GlcNAc...)Sequence Analysis
Glycosylationi517 – 5171N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi578 ↔ 637PROSITE-ProRule annotation
Glycosylationi598 – 5981N-linked (GlcNAc...)Sequence Analysis
Glycosylationi626 – 6261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi667 – 6671N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi683 ↔ 732PROSITE-ProRule annotation
Glycosylationi714 – 7141N-linked (GlcNAc...)Sequence Analysis
Modified residuei915 – 9151Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1053 – 10531Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1169 – 11691Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1213 – 12131Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1242 – 12421Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1322 – 13221Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1328 – 13281Phosphotyrosine; by autocatalysisBy similarity

Post-translational modificationi

N-glycosylated.By similarity
Ubiquitinated after VEGFA-mediated autophosphorylation, leading to proteolytic degradation.By similarity
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).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP35969.
PaxDbiP35969.
PRIDEiP35969.

PTM databases

PhosphoSiteiP35969.

Expressioni

Gene expression databases

BgeeiP35969.
CleanExiMM_FLT1.
ExpressionAtlasiP35969. baseline and differential.
GenevisibleiP35969. MM.

Interactioni

Subunit structurei

Interacts with VEGFA, VEGFB and PGF. Monomer in the absence of bound VEGFA, VEGFB or PGF. Homodimer in the presence of bound VEGFA, VEGFB and PGF. Can also form a heterodimer with KDR. Interacts (tyrosine phosphorylated) with CBL, CRK, GRB2, NCK1, PIK3R1, PLCG, PSEN1 and PTPN11. Probably interacts with PTPRB. Interacts with GNB2L1/RACK1. Identified in a complex with CBL and CD2AP (By similarity).By similarity

Protein-protein interaction databases

BioGridi199706. 5 interactions.
DIPiDIP-39359N.
IntActiP35969. 8 interactions.
MINTiMINT-4139959.
STRINGi10090.ENSMUSP00000031653.

Structurei

3D structure databases

ProteinModelPortaliP35969.
SMRiP35969. Positions 135-226, 804-1165.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 12493Ig-like C2-type 1Add
BLAST
Domaini152 – 21564Ig-like C2-type 2Add
BLAST
Domaini231 – 32898Ig-like C2-type 3Add
BLAST
Domaini334 – 42996Ig-like C2-type 4Add
BLAST
Domaini430 – 550121Ig-like C2-type 5Add
BLAST
Domaini557 – 656100Ig-like C2-type 6Add
BLAST
Domaini662 – 74887Ig-like C2-type 7Add
BLAST
Domaini828 – 1158331Protein kinasePROSITE-ProRule annotationAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000037949.
HOVERGENiHBG053432.
InParanoidiP35969.
KOiK05096.
OrthoDBiEOG75F4CC.
PhylomeDBiP35969.
TreeFamiTF325768.

Family and domain databases

Gene3Di2.60.40.10. 7 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
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.
IPR009135. VEGFR1_rcpt.
[Graphical view]
PANTHERiPTHR24416:SF126. PTHR24416:SF126. 1 hit.
PfamiPF07679. I-set. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
PRINTSiPR01833. VEGFRECEPTR1.
SMARTiSM00409. IG. 5 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.

P35969-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSCWDTAVL PYALLGCLLL TGYGSGSKLK VPELSLKGTQ HVMQAGQTLF
60 70 80 90 100
LKCRGEAAHS WSLPTTVSQE DKRLSITPPS ACGRDNRQFC STLTLDTAQA
110 120 130 140 150
NHTGLYTCRY LPTSTSKKKK AESSIYIFVS DAGSPFIEMH TDIPKLVHMT
160 170 180 190 200
EGRQLIIPCR VTSPNVTVTL KKFPFDTLTP DGQRITWDSR RGFIIANATY
210 220 230 240 250
KEIGLLNCEA TVNGHLYQTN YLTHRQTNTI LDVQIRPPSP VRLLHGQTLV
260 270 280 290 300
LNCTATTELN TRVQMSWNYP GKATKRASIR QRIDRSHSHN NVFHSVLKIN
310 320 330 340 350
NVESRDKGLY TCRVKSGSSF QSFNTSVHVY EKGFISVKHR KQPVQETTAG
360 370 380 390 400
RRSYRLSMKV KAFPSPEIVW LKDGSPATLK SARYLVHGYS LIIKDVTTED
410 420 430 440 450
AGDYTILLGI KQSRLFKNLT ATLIVNVKPQ IYEKSVSSLP SPPLYPLGSR
460 470 480 490 500
QVLTCTVYGI PRPTITWLWH PCHHNHSKER YDFCTENEES FILDPSSNLG
510 520 530 540 550
NRIESISQRM TVIEGTNKTV STLVVADSQT PGIYSCRAFN KIGTVERNIK
560 570 580 590 600
FYVTDVPNGF HVSLEKMPAE GEDLKLSCVV NKFLYRDITW ILLRTVNNRT
610 620 630 640 650
MHHSISKQKM ATTQDYSITL NLVIKNVSLE DSGTYACRAR NIYTGEDILR
660 670 680 690 700
KTEVLVRDSE APHLLQNLSD YEVSISGSTT LDCQARGVPA PQITWFKNNH
710 720 730 740 750
KIQQEPGIIL GPGNSTLFIE RVTEEDEGVY RCRATNQKGA VESAAYLTVQ
760 770 780 790 800
GTSDKSNLEL ITLTCTCVAA TLFWLLLTLF IRKLKRSSSE VKTDYLSIIM
810 820 830 840 850
DPDEVPLDEQ CERLPYDASK WEFARERLKL GKSLGRGAFG KVVQASAFGI
860 870 880 890 900
KKSPTCRTVA VKMLKEGATA SEYKALMTEL KILTHIGHHL NVVNLLGACT
910 920 930 940 950
KQGGPLMVIV EYCKYGNLSN YLKSKRDLFC LNKDAALHME LKKESLEPGL
960 970 980 990 1000
EQGQKPRLDS VSSSSVTSSS FPEDRSVSDV EGDEDYSEIS KQPLTMEDLI
1010 1020 1030 1040 1050
SYSFQVARGM EFLSSRKCIH RDLAARNILL SENNVVKICD FGLARDIYKN
1060 1070 1080 1090 1100
PDYVRRGDTR LPLKWMAPES IFDKVYSTKS DVWSYGVLLW EIFSLGGSPY
1110 1120 1130 1140 1150
PGVQMDEDFC SRLKEGMRMR TPEYATPEIY QIMLDCWHKD PKERPRFAEL
1160 1170 1180 1190 1200
VEKLGDLLQA NVQQDGKDYI PLNAILTRNS SFTYSTPTFS EDLFKDGFAD
1210 1220 1230 1240 1250
PHFHSGSSDD VRYVNAFKFM SLERIKTFEE LSPNSTSMFE DYQLDTSTLL
1260 1270 1280 1290 1300
GSPLLKRFTW TETKPKASMK IDLRIASKSK EAGLSDLPRP SFCFSSCGHI
1310 1320 1330
RPVQDDESEL GKESCCSPPP DYNSVVLYSS PPA
Length:1,333
Mass (Da):149,876
Last modified:June 1, 1994 - v1
Checksum:iC06533B7ECBC404C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti158 – 1581Missing in CAA55311 (PubMed:8134130).Curated
Sequence conflicti211 – 2111Missing in CAA55311 (PubMed:8134130).Curated
Sequence conflicti245 – 2451H → L in CAA55311 (PubMed:8134130).Curated
Sequence conflicti603 – 6031H → N in CAA55311 (PubMed:8134130).Curated
Sequence conflicti609 – 6157KMATTQD → NGHHSS in CAA55311 (PubMed:8134130).Curated
Sequence conflicti696 – 6961F → L in CAA55311 (PubMed:8134130).Curated
Sequence conflicti734 – 7341A → S in CAA55311 (PubMed:8134130).Curated
Sequence conflicti765 – 7651C → Y in CAA55311 (PubMed:8134130).Curated
Sequence conflicti820 – 8201K → N in CAA55311 (PubMed:8134130).Curated
Sequence conflicti1009 – 10091G → R in CAA55311 (PubMed:8134130).Curated
Sequence conflicti1181 – 11811S → G in BAA24498 (PubMed:9524283).Curated
Sequence conflicti1181 – 11811S → N in CAA55311 (PubMed:8134130).Curated
Sequence conflicti1193 – 11942LF → RG in CAA55311 (PubMed:8134130).Curated
Sequence conflicti1278 – 12792KS → PR in CAA55311 (PubMed:8134130).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07297 mRNA. Translation: AAA40078.1.
X78568 mRNA. Translation: CAA55311.1.
D88689 mRNA. Translation: BAA24498.1.
CCDSiCCDS19879.1.
PIRiI78875.
S49010.
RefSeqiNP_034358.2. NM_010228.3.
UniGeneiMm.389712.

Genome annotation databases

GeneIDi14254.
KEGGimmu:14254.
UCSCiuc009aoh.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07297 mRNA. Translation: AAA40078.1.
X78568 mRNA. Translation: CAA55311.1.
D88689 mRNA. Translation: BAA24498.1.
CCDSiCCDS19879.1.
PIRiI78875.
S49010.
RefSeqiNP_034358.2. NM_010228.3.
UniGeneiMm.389712.

3D structure databases

ProteinModelPortaliP35969.
SMRiP35969. Positions 135-226, 804-1165.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199706. 5 interactions.
DIPiDIP-39359N.
IntActiP35969. 8 interactions.
MINTiMINT-4139959.
STRINGi10090.ENSMUSP00000031653.

Chemistry

BindingDBiP35969.
ChEMBLiCHEMBL3516.

PTM databases

PhosphoSiteiP35969.

Proteomic databases

MaxQBiP35969.
PaxDbiP35969.
PRIDEiP35969.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi14254.
KEGGimmu:14254.
UCSCiuc009aoh.1. mouse.

Organism-specific databases

CTDi2321.
MGIiMGI:95558. Flt1.

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000037949.
HOVERGENiHBG053432.
InParanoidiP35969.
KOiK05096.
OrthoDBiEOG75F4CC.
PhylomeDBiP35969.
TreeFamiTF325768.

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.
ReactomeiREACT_293283. VEGF binds to VEGFR leading to receptor dimerization.
REACT_336251. Neurophilin interactions with VEGF and VEGFR.

Miscellaneous databases

ChiTaRSiFlt1. mouse.
NextBioi285579.
PROiP35969.
SOURCEiSearch...

Gene expression databases

BgeeiP35969.
CleanExiMM_FLT1.
ExpressionAtlasiP35969. baseline and differential.
GenevisibleiP35969. MM.

Family and domain databases

Gene3Di2.60.40.10. 7 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
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.
IPR009135. VEGFR1_rcpt.
[Graphical view]
PANTHERiPTHR24416:SF126. PTHR24416:SF126. 1 hit.
PfamiPF07679. I-set. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
PRINTSiPR01833. VEGFRECEPTR1.
SMARTiSM00409. IG. 5 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]
ProtoNetiSearch...

Publicationsi

  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: BALB/c.
    Tissue: Neonatal brain and Placenta.
  2. "Isolation of a gene encoding a novel receptor tyrosine kinase from differentiated embryonic stem cells."
    Choi K., Wall C., Hanratty R., Keller G.
    Oncogene 9:1261-1266(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. "Genomic organization of the flt-1 gene encoding for vascular endothelial growth factor (VEGF) receptor-1 suggests an intimate evolutionary relationship between the 7-Ig and the 5-Ig tyrosine kinase receptors."
    Kondo K., Hiratsuka S., Subbalakshmi E., Matsushime H., Shibuya M.
    Gene 208:297-305(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6.
    Tissue: Lung.
  4. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 110-119 AND 185-191, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  5. "Role of the Flt-1 receptor tyrosine kinase in regulating the assembly of vascular endothelium."
    Fong G.H., Rossant J., Gertsenstein M., Breitman M.L.
    Nature 376:66-70(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION IN BLOOD VESSEL DEVELOPMENT DURING EMBRYOGENESIS.
  6. "Flt-1 lacking the tyrosine kinase domain is sufficient for normal development and angiogenesis in mice."
    Hiratsuka S., Minowa O., Kuno J., Noda T., Shibuya M.
    Proc. Natl. Acad. Sci. U.S.A. 95:9349-9354(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION IN MACROPHAGE MIGRATION.
  7. "Involvement of Flt-1 tyrosine kinase (vascular endothelial growth factor receptor-1) in pathological angiogenesis."
    Hiratsuka S., Maru Y., Okada A., Seiki M., Noda T., Shibuya M.
    Cancer Res. 61:1207-1213(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ANGIOGENESIS.
  8. "The VEGF receptor flt-1 (VEGFR-1) is a positive modulator of vascular sprout formation and branching morphogenesis."
    Kearney J.B., Kappas N.C., Ellerstrom C., DiPaola F.W., Bautch V.L.
    Blood 103:4527-4535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  9. "Vascular endothelial growth factor receptor-1 regulates postnatal angiogenesis through inhibition of the excessive activation of Akt."
    Nishi J., Minamino T., Miyauchi H., Nojima A., Tateno K., Okada S., Orimo M., Moriya J., Fong G.H., Sunagawa K., Shibuya M., Komuro I.
    Circ. Res. 103:261-268(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ANGIOGENESIS.
  10. "Vascular endothelial growth factor receptor-1 signaling promotes mobilization of macrophage lineage cells from bone marrow and stimulates solid tumor growth."
    Muramatsu M., Yamamoto S., Osawa T., Shibuya M.
    Cancer Res. 70:8211-8221(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiVGFR1_MOUSE
AccessioniPrimary (citable) accession number: P35969
Secondary accession number(s): O55094, Q61517
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: June 24, 2015
This is version 163 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, Direct protein sequencing, 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.