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Vascular endothelial growth factor receptor 1 (VEGFR-1) (EC 2.7.10.1) (Fms-like tyrosine kinase 1) (FLT-1) (Tyrosine-protein kinase FRT) (Tyrosine-protein kinase receptor FLT) (FLT) (Vascular permeability factor receptor)

 VGFR1_HUMAN             Reviewed;        1338 AA.
P17948; A3E342; A3E344; A8KA71; B0LPF1; B2BF46; B2BF47; B2BF48;
B3FR89; B5A923; F5H5L6; O60722; P16057; Q12954;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
03-APR-2007, sequence version 2.
25-OCT-2017, entry version 210.
RecName: Full=Vascular endothelial growth factor receptor 1;
Short=VEGFR-1;
EC=2.7.10.1;
AltName: Full=Fms-like tyrosine kinase 1;
Short=FLT-1;
AltName: Full=Tyrosine-protein kinase FRT;
AltName: Full=Tyrosine-protein kinase receptor FLT;
Short=FLT;
AltName: Full=Vascular permeability factor receptor;
Flags: Precursor;
Name=FLT1; Synonyms=FLT, FRT, VEGFR1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=2158038;
Shibuya M., Yamaguchi S., Yamane A., Ikeda T., Tojo A., Matsushime H.,
Sato M.;
"Nucleotide sequence and expression of a novel human receptor-type
tyrosine kinase gene (flt) closely related to the fms family.";
Oncogene 5:519-524(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF
N-TERMINUS, SUBCELLULAR LOCATION (ISOFORM 2), INTERACTION WITH VEGFA,
AND FUNCTION.
TISSUE=Umbilical vein;
PubMed=8248162; DOI=10.1073/pnas.90.22.10705;
Kendall R.L., Thomas K.A.;
"Inhibition of vascular endothelial cell growth factor activity by an
endogenously encoded soluble receptor.";
Proc. Natl. Acad. Sci. U.S.A. 90:10705-10709(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH VEGFA, AND
GLYCOSYLATION.
TISSUE=Umbilical vein;
PubMed=10471394; DOI=10.1006/bbrc.1999.1282;
Herley M.T., Yu Y., Whitney R.G., Sato J.D.;
"Characterization of the VEGF binding site on the Flt-1 receptor.";
Biochem. Biophys. Res. Commun. 262:731-738(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION IN LIGAND BINDING,
AND SUBCELLULAR LOCATION.
PubMed=18593464; DOI=10.1186/ar2447;
Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D.,
Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.;
"Novel splice variants derived from the receptor tyrosine kinase
superfamily are potential therapeutics for rheumatoid arthritis.";
Arthritis Res. Ther. 10:R73-R73(2008).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, ROLE IN PREECLAMPSIA, AND INDUCTION.
PubMed=18515749; DOI=10.1161/CIRCRESAHA.108.171504;
Sela S., Itin A., Natanson-Yaron S., Greenfield C., Goldman-Wohl D.,
Yagel S., Keshet E.;
"A novel human-specific soluble vascular endothelial growth factor
receptor 1: cell-type-specific splicing and implications to vascular
endothelial growth factor homeostasis and preeclampsia.";
Circ. Res. 102:1566-1574(2008).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5; 6; 7 AND 8), ALTERNATIVE
SPLICING, FUNCTION IN PHOSPHORYLATION OF SRC AND CANCER CELL
INVASIVENESS, AND TISSUE SPECIFICITY.
PubMed=20512933; DOI=10.1002/jcb.22584;
Mezquita B., Mezquita J., Pau M., Mezquita C.;
"A novel intracellular isoform of VEGFR-1 activates Src and promotes
cell invasion in MDA-MB-231 breast cancer cells.";
J. Cell. Biochem. 110:732-742(2010).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Mezquita J., Mezquita B., Pau M., Mezquita C.;
"A new VEGFR1 receptor transcript coding for the extracellular domains
of the protein followed by a C-terminal polyserine tail.";
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Placenta, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1018-1058, AND ALTERNATIVE
SPLICING (ISOFORM 1).
PubMed=3040650;
Matsushime H., Yoshida M.C., Sasaki M., Shibuya M.;
"A possible new member of tyrosine kinase family, human frt sequence,
is highly conserved in vertebrates and located on human chromosome
13.";
Jpn. J. Cancer Res. 78:655-661(1987).
[14]
PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY, PHOSPHORYLATION AT
TYR-914; TYR-1213; TYR-1242; TYR-1327 AND TYR-1333, MUTAGENESIS OF
TYR-914; TYR-1213; TYR-1242; TYR-1327 AND TYR-1333, AND INTERACTION
WITH PLCG; GRB2; CRK; NCK1 AND PTPN11.
PubMed=9722576; DOI=10.1074/jbc.273.36.23410;
Ito N., Wernstedt C., Engstrom U., Claesson-Welsh L.;
"Identification of vascular endothelial growth factor receptor-1
tyrosine phosphorylation sites and binding of SH2 domain-containing
molecules.";
J. Biol. Chem. 273:23410-23418(1998).
[15]
INTERACTION WITH VEGFA, AUTOPHOSPHORYLATION, CATALYTIC ACTIVITY,
FUNCTION IN PHOSPHORYLATION OF PLCG, AND ABSENCE OF MITOGENIC FUNCTION
IN CULTURED FIBROBLASTS.
PubMed=7824266;
Seetharam L., Gotoh N., Maru Y., Neufeld G., Yamaguchi S., Shibuya M.;
"A unique signal transduction from FLT tyrosine kinase, a receptor for
vascular endothelial growth factor VEGF.";
Oncogene 10:135-147(1995).
[16]
FUNCTION IN CELL MIGRATION, FUNCTION IN VEGFA AND PGF SIGNALING, AND
INDUCTION.
PubMed=8605350;
Barleon B., Sozzani S., Zhou D., Weich H.A., Mantovani A., Marme D.;
"Migration of human monocytes in response to vascular endothelial
growth factor (VEGF) is mediated via the VEGF receptor flt-1.";
Blood 87:3336-3343(1996).
[17]
FUNCTION IN PHOSPHORYLATION OF PLCG AND ACTIVATION OF MAP KINASES,
INTERACTION WITH PLCG, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-861 AND
TYR-1169, AND PHOSPHORYLATION AT TYR-1169 AND TYR-1213.
PubMed=9299537; DOI=10.1006/bbrc.1997.7327;
Sawano A., Takahashi T., Yamaguchi S., Shibuya M.;
"The phosphorylated 1169-tyrosine containing region of flt-1 kinase
(VEGFR-1) is a major binding site for PLCgamma.";
Biochem. Biophys. Res. Commun. 238:487-491(1997).
[18]
INTERACTION WITH PIK3R1; PTPN11 AND NCK1, AND PHOSPHORYLATION AT
TYR-1213.
PubMed=9600074; DOI=10.1006/bbrc.1998.8578;
Igarashi K., Isohara T., Kato T., Shigeta K., Yamano T., Uno I.;
"Tyrosine 1213 of Flt-1 is a major binding site of Nck and SHP-2.";
Biochem. Biophys. Res. Commun. 246:95-99(1998).
[19]
FUNCTION AS NEGATIVE REGULATOR OF KDR-MEDIATED CELL PROLIFERATION.
PubMed=11141500; DOI=10.1016/S0002-9440(10)63965-X;
Dunk C., Ahmed A.;
"Vascular endothelial growth factor receptor-2-mediated mitogenesis is
negatively regulated by vascular endothelial growth factor receptor-1
in tumor epithelial cells.";
Am. J. Pathol. 158:265-273(2001).
[20]
INTERACTION WITH PIK3R1 AND VEGFA, AUTOPHOSPHORYLATION,
PHOSPHORYLATION AT TYR-1213, SUBCELLULAR LOCATION, IDENTIFICATION BY
MASS SPECTROMETRY, AND GLYCOSYLATION.
PubMed=11513746; DOI=10.1042/0264-6021:3580465;
Yu Y., Hulmes J.D., Herley M.T., Whitney R.G., Crabb J.W., Sato J.D.;
"Direct identification of a major autophosphorylation site on vascular
endothelial growth factor receptor Flt-1 that mediates
phosphatidylinositol 3'-kinase binding.";
Biochem. J. 358:465-472(2001).
[21]
FUNCTION IN PGF-MEDIATED CHORIOCARCINOMA CELL PROLIFERATION.
PubMed=11811792; DOI=10.3109/08977190109001086;
Angelucci C., Lama G., Iacopino F., Maglione D., Sica G.;
"Effect of placenta growth factor-1 on proliferation and release of
nitric oxide, cyclic AMP and cyclic GMP in human epithelial cells
expressing the FLT-1 receptor.";
Growth Factors 19:193-206(2001).
[22]
INTERACTION WITH KDR, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, AND
FUNCTION IN VEGFA SIGNALING; PHOSPHORYLATION OF PLCG AND ACTIVATION OF
PHOSPHATIDYLINOSITOL KINASE AND PHOSPHOLIPASE C.
PubMed=11312102; DOI=10.1016/S1357-2725(01)00019-X;
Huang K., Andersson C., Roomans G.M., Ito N., Claesson-Welsh L.;
"Signaling properties of VEGF receptor-1 and -2 homo- and
heterodimers.";
Int. J. Biochem. Cell Biol. 33:315-324(2001).
[23]
FUNCTION IN SIGNALING VIA ACTIVATION OF THE PHOSPHATIDYLINOSITOL
KINASE PATHWAY AND POSITIVE REGULATION OF ANGIOGENESIS IN RESPONSE TO
PGF AND VEGFA.
PubMed=14633857; DOI=10.2337/diabetes.52.12.2959;
Cai J., Ahmad S., Jiang W.G., Huang J., Kontos C.D., Boulton M.,
Ahmed A.;
"Activation of vascular endothelial growth factor receptor-1 sustains
angiogenesis and Bcl-2 expression via the phosphatidylinositol 3-
kinase pathway in endothelial cells.";
Diabetes 52:2959-2968(2003).
[24]
INTERACTION WITH PGF AND KDR, FUNCTION IN PHOSPHORYLATION OF KDR;
VEGFA AND PGF SIGNALING, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS
SPECTROMETRY, AND PHOSPHORYLATION AT TYR-1213; TYR-1327 AND TYR-1309.
PubMed=12796773; DOI=10.1038/nm884;
Autiero M., Waltenberger J., Communi D., Kranz A., Moons L.,
Lambrechts D., Kroll J., Plaisance S., De Mol M., Bono F., Kliche S.,
Fellbrich G., Ballmer-Hofer K., Maglione D., Mayr-Beyrle U.,
Dewerchin M., Dombrowski S., Stanimirovic D., Van Hummelen P.,
Dehio C., Hicklin D.J., Persico G., Herbert J.M., Communi D.,
Shibuya M., Collen D., Conway E.M., Carmeliet P.;
"Role of PlGF in the intra- and intermolecular cross talk between the
VEGF receptors Flt1 and Flk1.";
Nat. Med. 9:936-943(2003).
[25]
INTERACTION WITH CBL AND CD2AP, UBIQUITINATION, AUTOPHOSPHORYLATION IN
RESPONSE TO VEGFA, MUTAGENESIS OF TYR-1333, AND SUBCELLULAR LOCATION.
PubMed=15001553; DOI=10.1096/fj.03-0767fje;
Kobayashi S., Sawano A., Nojima Y., Shibuya M., Maru Y.;
"The c-Cbl/CD2AP complex regulates VEGF-induced endocytosis and
degradation of Flt-1 (VEGFR-1).";
FASEB J. 18:929-931(2004).
[26]
FUNCTION IN VEGFA AND VEGFB SIGNALING; CANCER CELL MIGRATION;
INVASIVENESS AND ACTIVATION OF MAPK1/ERK2 AND MAPK3/ERK1.
PubMed=15735759; DOI=10.1038/sj.onc.1208246;
Fan F., Wey J.S., McCarty M.F., Belcheva A., Liu W., Bauer T.W.,
Somcio R.J., Wu Y., Hooper A., Hicklin D.J., Ellis L.M.;
"Expression and function of vascular endothelial growth factor
receptor-1 on human colorectal cancer cells.";
Oncogene 24:2647-2653(2005).
[27]
FUNCTION IN CELL MIGRATION AND PHOSPHORYLATION OF PTK2/FAK1; YES1 AND
SRC.
PubMed=16685275; DOI=10.1038/sj.bjc.6603143;
Lesslie D.P., Summy J.M., Parikh N.U., Fan F., Trevino J.G.,
Sawyer T.K., Metcalf C.A., Shakespeare W.C., Hicklin D.J., Ellis L.M.,
Gallick G.E.;
"Vascular endothelial growth factor receptor-1 mediates migration of
human colorectal carcinoma cells by activation of Src family
kinases.";
Br. J. Cancer 94:1710-1717(2006).
[28]
MUTAGENESIS OF ASN-1050.
PubMed=16286478; DOI=10.1074/jbc.M506454200;
Meyer R.D., Mohammadi M., Rahimi N.;
"A single amino acid substitution in the activation loop defines the
decoy characteristic of VEGFR-1/FLT-1.";
J. Biol. Chem. 281:867-875(2006).
[29]
FUNCTION IN PGF AND VEGFA SIGNALING; PHOSPHORYLATION OF AKT1;
MAPK3/ERK1 AND MAP KINASES; CHEMOTAXIS AND ACTIVATION OF
PHOSPHATIDYLINOSITOL 3-KINASE, AND AUTOPHOSPHORYLATION IN RESPONSE TO
PGF AND VEGFA.
PubMed=18079407; DOI=10.1161/ATVBAHA.107.158022;
Tchaikovski V., Fellbrich G., Waltenberger J.;
"The molecular basis of VEGFR-1 signal transduction pathways in
primary human monocytes.";
Arterioscler. Thromb. Vasc. Biol. 28:322-328(2008).
[30]
FUNCTION IN ENDOTHELIAL CELL SURVIVAL AND ANGIOGENESIS.
PubMed=18583712; DOI=10.1161/CIRCRESAHA.108.174128;
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.;
"Vascular endothelial growth factor receptor-1 regulates postnatal
angiogenesis through inhibition of the excessive activation of Akt.";
Circ. Res. 103:261-268(2008).
[31]
FUNCTION IN CANCER CELL MIGRATION AND ACTIVATION OF MAPK1/ERK2 AND/OR
MAPK3/ERK1.
PubMed=20551949; DOI=10.1038/sj.bjc.6605746;
Taylor A.P., Leon E., Goldenberg D.M.;
"Placental growth factor (PlGF) enhances breast cancer cell motility
by mobilising ERK1/2 phosphorylation and cytoskeletal rearrangement.";
Br. J. Cancer 103:82-89(2010).
[32]
INTERACTION WITH RACK1.
PubMed=21212275; DOI=10.1074/jbc.M110.165605;
Wang F., Yamauchi M., Muramatsu M., Osawa T., Tsuchida R., Shibuya M.;
"RACK1 regulates VEGF/Flt1-mediated cell migration via activation of a
PI3-K/Akt pathway.";
J. Biol. Chem. 286:9097-9106(2011).
[33]
INTERACTION WITH PSEN1 AND PTPRB, DEPHOSPHORYLATION BY PTPRB,
MUTAGENESIS OF VAL-767, AND PROTEOLYTIC CLEAVAGE BY PSEN1 AT VAL-767.
PubMed=22016384; DOI=10.1074/jbc.M111.296590;
Cai J., Chen Z., Ruan Q., Han S., Liu L., Qi X., Boye S.L.,
Hauswirth W.W., Grant M.B., Boulton M.E.;
"gamma-Secretase and presenilin mediate cleavage and phosphorylation
of vascular endothelial growth factor receptor-1.";
J. Biol. Chem. 286:42514-42523(2011).
[34]
FUNCTION AS DECOY RECEPTORS; REGULATION OF VEGFA SIGNALING AND
REGULATION OF KDR ACTIVITY (ISOFORMS 2/3/4), AND ROLE IN PREECLAMPSIA.
PubMed=21752276; DOI=10.1186/2045-824X-3-15;
Ahmad S., Hewett P.W., Al-Ani B., Sissaoui S., Fujisawa T.,
Cudmore M.J., Ahmed A.;
"Autocrine activity of soluble Flt-1 controls endothelial cell
function and angiogenesis.";
Vasc. Cell 3:15-15(2011).
[35]
REVIEW ON FUNCTION AS NEGATIVE REGULATOR OF ANGIOGENESIS DURING
EMBRYONIC DEVELOPMENT; POSITIVE REGULATION OF MACROPHAGE FUNCTION IN
ADULTHOOD; ROLE IN CARCINOGENESIS AND INFLAMMATION.
PubMed=17002866; DOI=10.5483/BMBRep.2006.39.5.469;
Shibuya M.;
"Differential roles of vascular endothelial growth factor receptor-1
and receptor-2 in angiogenesis.";
J. Biochem. Mol. Biol. 39:469-478(2006).
[36]
REVIEW ON STRUCTURE AND FUNCTION.
PubMed=18680722; DOI=10.1016/j.bbrc.2008.07.121;
Roskoski R. Jr.;
"VEGF receptor protein-tyrosine kinases: structure and regulation.";
Biochem. Biophys. Res. Commun. 375:287-291(2008).
[37]
REVIEW ON ROLE IN ANGIOGENESIS AND CANCER.
PubMed=19230644; DOI=10.1016/j.ceb.2008.12.012;
Lohela M., Bry M., Tammela T., Alitalo K.;
"VEGFs and receptors involved in angiogenesis versus
lymphangiogenesis.";
Curr. Opin. Cell Biol. 21:154-165(2009).
[38]
REVIEW ON LIGAND SPECIFICITY; FUNCTION; STRUCTURE; PHOSPHORYLATION AND
SIGNALING.
PubMed=19761875; DOI=10.1016/j.bbapap.2009.09.002;
Grunewald F.S., Prota A.E., Giese A., Ballmer-Hofer K.;
"Structure-function analysis of VEGF receptor activation and the role
of coreceptors in angiogenic signaling.";
Biochim. Biophys. Acta 1804:567-580(2010).
[39]
REVIEW ON ROLE IN CANCER.
PubMed=20127948; DOI=10.1002/cncr.24789;
Schwartz J.D., Rowinsky E.K., Youssoufian H., Pytowski B., Wu Y.;
"Vascular endothelial growth factor receptor-1 in human cancer:
concise review and rationale for development of IMC-18F1 (Human
antibody targeting vascular endothelial growth factor receptor-1).";
Cancer 116:1027-1032(2010).
[40]
REVIEW ON LIGAND SPECIFICITY; FUNCTION; STRUCTURE; PHOSPHORYLATION AND
SIGNALING.
PubMed=21711246; DOI=10.1042/BJ20110301;
Koch S., Tugues S., Li X., Gualandi L., Claesson-Welsh L.;
"Signal transduction by vascular endothelial growth factor
receptors.";
Biochem. J. 437:169-183(2011).
[41]
REVIEW ON ROLE IN CANCER AND PREECLAMPSIA.
PubMed=21558755; DOI=10.2183/pjab.87.167;
Shibuya M.;
"Involvement of Flt-1 (VEGF receptor-1) in cancer and preeclampsia.";
Proc. Jpn. Acad., B, Phys. Biol. Sci. 87:167-178(2011).
[42]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 132-226 IN COMPLEX WITH
VEGFA, AND DOMAIN.
PubMed=9393862; DOI=10.1016/S0092-8674(00)80456-0;
Wiesmann C., Fuh G., Christinger H.W., Eigenbrot C., Wells J.A.,
de Vos A.M.;
"Crystal structure at 1.7 A resolution of VEGF in complex with domain
2 of the Flt-1 receptor.";
Cell 91:695-704(1997).
[43]
STRUCTURE BY NMR OF 129-229, X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF
129-229 IN COMPLEX WITH VEGFA, SUBUNIT, AND INTERACTION WITH VEGFA.
PubMed=10543948; DOI=10.1006/jmbi.1999.3134;
Starovasnik M.A., Christinger H.W., Wiesmann C., Champe M.A.,
de Vos A.M., Skelton N.J.;
"Solution structure of the VEGF-binding domain of Flt-1: comparison of
its free and bound states.";
J. Mol. Biol. 293:531-544(1999).
[44]
X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 130-229 IN COMPLEX WITH PGF.
PubMed=14684734; DOI=10.1074/jbc.M313237200;
Christinger H.W., Fuh G., de Vos A.M., Wiesmann C.;
"The crystal structure of placental growth factor in complex with
domain 2 of vascular endothelial growth factor receptor-1.";
J. Biol. Chem. 279:10382-10388(2004).
[45]
X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 129-226 IN COMPLEX WITH
VEGFB, INTERACTION WITH VEGFB, SUBUNIT, AND DOMAIN.
PubMed=20501651; DOI=10.1074/jbc.M110.130658;
Iyer S., Darley P.I., Acharya K.R.;
"Structural insights into the binding of vascular endothelial growth
factor-B by VEGFR-1(D2): recognition and specificity.";
J. Biol. Chem. 285:23779-23789(2010).
[46]
VARIANTS [LARGE SCALE ANALYSIS] THR-60; LYS-144; GLN-281; ILE-422;
GLN-781; VAL-938; ALA-982 AND VAL-1061.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- 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. 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, proliferation of some types of cancer cells,
but does not promote proliferation of normal fibroblasts (in
vitro). 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. Likewise, isoforms lacking a
transmembrane domain, such as isoform 2, isoform 3 and isoform 4,
may function as decoy receptors for VEGFA. 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
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 and YES1, and may also
phosphorylate CBL. Isoform 1 phosphorylates PLCG. Promotes
phosphorylation of AKT1 at 'Ser-473'. Promotes phosphorylation of
PTK2/FAK1. Isoform 7 has a truncated kinase domain; it increases
phosphorylation of SRC at 'Tyr-418' by unknown means and promotes
tumor cell invasion. {ECO:0000269|PubMed:11141500,
ECO:0000269|PubMed:11312102, ECO:0000269|PubMed:11811792,
ECO:0000269|PubMed:12796773, ECO:0000269|PubMed:14633857,
ECO:0000269|PubMed:15735759, ECO:0000269|PubMed:16685275,
ECO:0000269|PubMed:18079407, ECO:0000269|PubMed:18515749,
ECO:0000269|PubMed:18583712, ECO:0000269|PubMed:18593464,
ECO:0000269|PubMed:20512933, ECO:0000269|PubMed:20551949,
ECO:0000269|PubMed:21752276, ECO:0000269|PubMed:7824266,
ECO:0000269|PubMed:8248162, ECO:0000269|PubMed:8605350,
ECO:0000269|PubMed:9299537}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:11312102,
ECO:0000269|PubMed:12796773, ECO:0000269|PubMed:7824266,
ECO:0000269|PubMed:9299537, ECO:0000269|PubMed:9722576}.
-!- ENZYME 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.
-!- SUBUNIT: 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 (when tyrosine phosphorylated) with CBL, CRK, GRB2,
NCK1, PIK3R1, PLCG, PSEN1 and PTPN11. Probably interacts also with
PTPRB. Interacts with RACK1. Identified in a complex with CBL and
CD2AP. {ECO:0000269|PubMed:10471394, ECO:0000269|PubMed:10543948,
ECO:0000269|PubMed:11312102, ECO:0000269|PubMed:11513746,
ECO:0000269|PubMed:12796773, ECO:0000269|PubMed:14684734,
ECO:0000269|PubMed:15001553, ECO:0000269|PubMed:20501651,
ECO:0000269|PubMed:21212275, ECO:0000269|PubMed:22016384,
ECO:0000269|PubMed:7824266, ECO:0000269|PubMed:8248162,
ECO:0000269|PubMed:9299537, ECO:0000269|PubMed:9393862,
ECO:0000269|PubMed:9600074, ECO:0000269|PubMed:9722576}.
-!- INTERACTION:
P22681:CBL; NbExp=2; IntAct=EBI-1026718, EBI-518228;
P46109:CRKL; NbExp=9; IntAct=EBI-1026718, EBI-910;
P35222:CTNNB1; NbExp=2; IntAct=EBI-1026718, EBI-491549;
P08631:HCK; NbExp=2; IntAct=EBI-1026718, EBI-346340;
P98160:HSPG2; NbExp=2; IntAct=EBI-6530464, EBI-6896259;
P49763:PGF; NbExp=2; IntAct=EBI-1026718, EBI-1037633;
P27986:PIK3R1; NbExp=2; IntAct=EBI-1026718, EBI-79464;
P19174:PLCG1; NbExp=2; IntAct=EBI-1026718, EBI-79387;
Q05397:PTK2; NbExp=2; IntAct=EBI-1026718, EBI-702142;
Q06124:PTPN11; NbExp=2; IntAct=EBI-1026718, EBI-297779;
Q12913:PTPRJ; NbExp=2; IntAct=EBI-1026718, EBI-2264500;
P15692:VEGFA; NbExp=4; IntAct=EBI-1026718, EBI-1026643;
P15692-4:VEGFA; NbExp=3; IntAct=EBI-1026718, EBI-1026691;
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
membrane protein. Endosome. Note=Autophosphorylation promotes
ubiquitination and endocytosis.
-!- SUBCELLULAR LOCATION: Isoform 2: Secreted
{ECO:0000269|PubMed:8248162}.
-!- SUBCELLULAR LOCATION: Isoform 3: Secreted.
-!- SUBCELLULAR LOCATION: Isoform 4: Secreted.
-!- SUBCELLULAR LOCATION: Isoform 5: Cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 6: Cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 7: Cytoplasm {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=Flt1;
IsoId=P17948-1; Sequence=Displayed;
Name=2; Synonyms=sFlt1;
IsoId=P17948-2; Sequence=VSP_002955, VSP_002956;
Name=3; Synonyms=sFlt1-14;
IsoId=P17948-3; Sequence=VSP_041927, VSP_041928;
Name=4;
IsoId=P17948-4; Sequence=VSP_041929, VSP_041930;
Name=5; Synonyms=i15;
IsoId=P17948-5; Sequence=VSP_041985;
Name=6; Synonyms=i18;
IsoId=P17948-6; Sequence=VSP_041984;
Name=7; Synonyms=i21;
IsoId=P17948-7; Sequence=VSP_041983;
Name=8;
IsoId=P17948-8; Sequence=VSP_047759, VSP_047760;
-!- TISSUE SPECIFICITY: Detected in normal lung, but also in placenta,
liver, kidney, heart and brain tissues. Specifically expressed in
most of the vascular endothelial cells, and also expressed in
peripheral blood monocytes. Isoform 2 is strongly expressed in
placenta. Isoform 3 is expressed in corneal epithelial cells (at
protein level). Isoform 3 is expressed in vascular smooth muscle
cells (VSMC). {ECO:0000269|PubMed:18515749,
ECO:0000269|PubMed:20512933}.
-!- INDUCTION: Up-regulated in coculture of VSMC/endothelial cell (EC)
or by direct exposure to VEGF of VSMC monoculture. Up-regulated
from the second trimester of pregnancy to the term and in the
placenta of women with preeclampsia (PE). Up-regulated in
monocytes exposed to bacterial lipopolysaccharide (LPS).
{ECO:0000269|PubMed:18515749, ECO:0000269|PubMed:8605350}.
-!- DOMAIN: The second and third Ig-like C2-type (immunoglobulin-like)
domains are sufficient for VEGFA binding.
{ECO:0000269|PubMed:20501651, ECO:0000269|PubMed:9393862}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:10471394,
ECO:0000269|PubMed:11513746}.
-!- PTM: Ubiquitinated after VEGFA-mediated autophosphorylation,
leading to proteolytic degradation. {ECO:0000269|PubMed:15001553}.
-!- 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-1333 is important for endocytosis and for interaction with
CBL, NCK1 and CRK. Is probably dephosphorylated by PTPRB.
{ECO:0000269|PubMed:11513746, ECO:0000269|PubMed:12796773,
ECO:0000269|PubMed:9299537, ECO:0000269|PubMed:9600074,
ECO:0000269|PubMed:9722576}.
-!- DISEASE: Note=Can contribute to cancer cell survival,
proliferation, migration, and invasion, and tumor angiogenesis and
metastasis. May contribute to cancer pathogenesis by promoting
inflammatory responses and recruitment of tumor-infiltrating
macrophages.
-!- DISEASE: Note=Abnormally high expression of soluble isoforms
(isoform 2, isoform 3 or isoform 4) may be a cause of
preeclampsia.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. CSF-1/PDGF receptor subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
-----------------------------------------------------------------------
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EMBL; X51602; CAA35946.1; -; mRNA.
EMBL; U01134; AAC50060.1; -; mRNA.
EMBL; AF063657; AAC16449.2; -; mRNA.
EMBL; EU826561; ACF47597.1; -; mRNA.
EMBL; EU368830; ACA62948.1; -; mRNA.
EMBL; DQ836394; ABI53803.1; -; mRNA.
EMBL; DQ836395; ABI53804.1; -; mRNA.
EMBL; DQ836396; ABI53805.1; -; mRNA.
EMBL; EF491868; ABS32268.1; -; mRNA.
EMBL; EF491869; ABS32269.1; -; mRNA.
EMBL; EF491870; ABS32270.1; -; mRNA.
EMBL; EU360600; ACB05747.1; -; mRNA.
EMBL; EU332841; ABY87530.1; -; Genomic_DNA.
EMBL; AK292936; BAF85625.1; -; mRNA.
EMBL; AK300392; BAG62125.1; -; mRNA.
EMBL; AL138712; CAI14846.1; -; Genomic_DNA.
EMBL; AL139005; CAI14846.1; JOINED; Genomic_DNA.
EMBL; AL139005; CAI17096.1; -; Genomic_DNA.
EMBL; AL138712; CAI17096.1; JOINED; Genomic_DNA.
EMBL; CH471075; EAX08431.1; -; Genomic_DNA.
EMBL; CH471075; EAX08432.1; -; Genomic_DNA.
EMBL; BC039007; AAH39007.1; -; mRNA.
EMBL; D00133; BAA00080.1; -; Genomic_DNA.
CCDS; CCDS53860.1; -. [P17948-3]
CCDS; CCDS53861.1; -. [P17948-4]
CCDS; CCDS73556.1; -. [P17948-2]
CCDS; CCDS9330.1; -. [P17948-1]
PIR; A49636; A49636.
PIR; S09982; S09982.
RefSeq; NP_001153392.1; NM_001159920.1. [P17948-2]
RefSeq; NP_001153502.1; NM_001160030.1. [P17948-3]
RefSeq; NP_001153503.1; NM_001160031.1. [P17948-4]
RefSeq; NP_002010.2; NM_002019.4. [P17948-1]
UniGene; Hs.594454; -.
PDB; 1FLT; X-ray; 1.70 A; X/Y=132-226.
PDB; 1QSV; NMR; -; A=129-229.
PDB; 1QSZ; NMR; -; A=129-229.
PDB; 1QTY; X-ray; 2.70 A; T/U/X/Y=129-229.
PDB; 1RV6; X-ray; 2.45 A; X/Y=130-229.
PDB; 2XAC; X-ray; 2.71 A; C/X=129-226.
PDB; 3HNG; X-ray; 2.70 A; A=801-1158.
PDB; 4CKV; X-ray; 2.06 A; X=132-225.
PDB; 4CL7; X-ray; 2.00 A; A/B/C/D=132-225.
PDB; 5ABD; X-ray; 2.00 A; E/I/X=132-226.
PDB; 5EX3; X-ray; 2.41 A; D=827-835.
PDB; 5T89; X-ray; 4.00 A; X/Y=27-656.
PDBsum; 1FLT; -.
PDBsum; 1QSV; -.
PDBsum; 1QSZ; -.
PDBsum; 1QTY; -.
PDBsum; 1RV6; -.
PDBsum; 2XAC; -.
PDBsum; 3HNG; -.
PDBsum; 4CKV; -.
PDBsum; 4CL7; -.
PDBsum; 5ABD; -.
PDBsum; 5EX3; -.
PDBsum; 5T89; -.
ProteinModelPortal; P17948; -.
SMR; P17948; -.
BioGrid; 108609; 14.
DIP; DIP-643N; -.
IntAct; P17948; 30.
MINT; MINT-127610; -.
STRING; 9606.ENSP00000282397; -.
BindingDB; P17948; -.
ChEMBL; CHEMBL1868; -.
DrugBank; DB06080; ABT-869.
DrugBank; DB06626; Axitinib.
DrugBank; DB06101; IMC-1C11.
DrugBank; DB09078; Lenvatinib.
DrugBank; DB07288; N-(4-chlorophenyl)-2-[(pyridin-4-ylmethyl)amino]benzamide.
DrugBank; DB09079; Nintedanib.
DrugBank; DB05913; OSI-930.
DrugBank; DB06589; Pazopanib.
DrugBank; DB08896; Regorafenib.
DrugBank; DB00398; Sorafenib.
DrugBank; DB01268; Sunitinib.
DrugBank; DB05075; TG100801.
DrugBank; DB04879; Vatalanib.
GuidetoPHARMACOLOGY; 1812; -.
iPTMnet; P17948; -.
PhosphoSitePlus; P17948; -.
UniCarbKB; P17948; -.
BioMuta; FLT1; -.
DMDM; 143811474; -.
EPD; P17948; -.
MaxQB; P17948; -.
PaxDb; P17948; -.
PeptideAtlas; P17948; -.
PRIDE; P17948; -.
DNASU; 2321; -.
Ensembl; ENST00000282397; ENSP00000282397; ENSG00000102755. [P17948-1]
Ensembl; ENST00000539099; ENSP00000442630; ENSG00000102755. [P17948-4]
Ensembl; ENST00000541932; ENSP00000437631; ENSG00000102755. [P17948-3]
Ensembl; ENST00000543394; ENSP00000437841; ENSG00000102755. [P17948-8]
Ensembl; ENST00000615840; ENSP00000484039; ENSG00000102755. [P17948-2]
GeneID; 2321; -.
KEGG; hsa:2321; -.
UCSC; uc001usb.4; human. [P17948-1]
CTD; 2321; -.
DisGeNET; 2321; -.
EuPathDB; HostDB:ENSG00000102755.10; -.
GeneCards; FLT1; -.
H-InvDB; HIX0130593; -.
HGNC; HGNC:3763; FLT1.
HPA; CAB068189; -.
HPA; CAB068190; -.
HPA; HPA011740; -.
HPA; HPA014290; -.
MIM; 165070; gene.
neXtProt; NX_P17948; -.
OpenTargets; ENSG00000102755; -.
PharmGKB; PA28180; -.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118923; -.
HOGENOM; HOG000037949; -.
HOVERGEN; HBG053432; -.
InParanoid; P17948; -.
KO; K05096; -.
OMA; CTCVAAT; -.
OrthoDB; EOG091G01TL; -.
PhylomeDB; P17948; -.
TreeFam; TF325768; -.
BRENDA; 2.7.10.1; 2681.
Reactome; R-HSA-194306; Neurophilin interactions with VEGF and VEGFR.
Reactome; R-HSA-195399; VEGF binds to VEGFR leading to receptor dimerization.
SignaLink; P17948; -.
SIGNOR; P17948; -.
ChiTaRS; FLT1; human.
EvolutionaryTrace; P17948; -.
GeneWiki; FLT1; -.
GenomeRNAi; 2321; -.
PRO; PR:P17948; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000102755; -.
CleanEx; HS_FLT1; -.
ExpressionAtlas; P17948; baseline and differential.
Genevisible; P17948; HS.
GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
GO; GO:0005615; C:extracellular space; TAS:ProtInc.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019838; F:growth factor binding; IPI:UniProtKB.
GO; GO:0036332; F:placental growth factor-activated receptor activity; IDA:UniProtKB.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; TAS:ProtInc.
GO; GO:0005021; F:vascular endothelial growth factor-activated receptor activity; IDA:UniProtKB.
GO; GO:0036326; F:VEGF-A-activated receptor activity; IDA:UniProtKB.
GO; GO:0036327; F:VEGF-B-activated receptor activity; IDA:UniProtKB.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0048514; P:blood vessel morphogenesis; ISS:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0016477; P:cell migration; IMP:UniProtKB.
GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IDA:UniProtKB.
GO; GO:0048598; P:embryonic morphogenesis; ISS:UniProtKB.
GO; GO:0002548; P:monocyte chemotaxis; IDA:UniProtKB.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB.
GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:UniProtKB.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IMP:UniProtKB.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IMP:UniProtKB.
GO; GO:0010863; P:positive regulation of phospholipase C activity; IMP:UniProtKB.
GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; TAS:ProtInc.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IDA:UniProtKB.
GO; GO:0036323; P:vascular endothelial growth factor receptor-1 signaling pathway; IDA:UniProtKB.
Gene3D; 2.60.40.10; -; 8.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013106; Ig_V-set.
InterPro; IPR013151; Immunoglobulin.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
InterPro; IPR009135; VEGFR1_rcpt.
Pfam; PF07679; I-set; 2.
Pfam; PF00047; ig; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
PRINTS; PR01833; VEGFRECEPTR1.
SMART; SM00409; IG; 7.
SMART; SM00408; IGc2; 5.
SMART; SM00406; IGv; 2.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF48726; SSF48726; 8.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS50835; IG_LIKE; 6.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Angiogenesis; ATP-binding;
Cell membrane; Chemotaxis; Complete proteome; Cytoplasm;
Developmental protein; Differentiation; Direct protein sequencing;
Disulfide bond; Endosome; Glycoprotein; Immunoglobulin domain; Kinase;
Membrane; Nucleotide-binding; Phosphoprotein; Polymorphism; Receptor;
Reference proteome; Repeat; Secreted; Signal; Transferase;
Transmembrane; Transmembrane helix; Tyrosine-protein kinase;
Ubl conjugation.
SIGNAL 1 26 {ECO:0000269|PubMed:8248162}.
CHAIN 27 1338 Vascular endothelial growth factor
receptor 1.
/FTId=PRO_0000016768.
TOPO_DOM 27 758 Extracellular. {ECO:0000255}.
TRANSMEM 759 780 Helical. {ECO:0000255}.
TOPO_DOM 781 1338 Cytoplasmic. {ECO:0000255}.
DOMAIN 32 123 Ig-like C2-type 1.
DOMAIN 151 214 Ig-like C2-type 2.
DOMAIN 230 327 Ig-like C2-type 3.
DOMAIN 335 421 Ig-like C2-type 4.
DOMAIN 428 553 Ig-like C2-type 5.
DOMAIN 556 654 Ig-like C2-type 6.
DOMAIN 661 747 Ig-like C2-type 7.
DOMAIN 827 1158 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 833 841 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 1022 1022 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 861 861 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 767 768 Cleavage; by PSEN1. {ECO:0000305}.
MOD_RES 914 914 Phosphotyrosine; by autocatalysis.
{ECO:0000305|PubMed:9722576}.
MOD_RES 1053 1053 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
MOD_RES 1169 1169 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:9299537}.
MOD_RES 1213 1213 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:11513746,
ECO:0000269|PubMed:12796773,
ECO:0000269|PubMed:9299537,
ECO:0000269|PubMed:9600074,
ECO:0000269|PubMed:9722576}.
MOD_RES 1242 1242 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:9722576}.
MOD_RES 1309 1309 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:12796773}.
MOD_RES 1327 1327 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:12796773,
ECO:0000269|PubMed:9722576}.
MOD_RES 1333 1333 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:9722576}.
CARBOHYD 100 100 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 164 164 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 196 196 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 251 251 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 323 323 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 402 402 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 417 417 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 474 474 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 547 547 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 597 597 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 620 620 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 625 625 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 666 666 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 53 107 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 158 207
DISULFID 252 311 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 454 535 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 577 636 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 682 731 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 1 995 Missing (in isoform 7).
{ECO:0000303|PubMed:20512933}.
/FTId=VSP_041983.
VAR_SEQ 1 875 Missing (in isoform 6).
{ECO:0000303|PubMed:20512933}.
/FTId=VSP_041984.
VAR_SEQ 1 782 Missing (in isoform 5).
{ECO:0000303|PubMed:20512933}.
/FTId=VSP_041985.
VAR_SEQ 1 7 MVSYWDT -> MNSDLLV (in isoform 8).
{ECO:0000303|PubMed:20512933}.
/FTId=VSP_047759.
VAR_SEQ 8 984 Missing (in isoform 8).
{ECO:0000303|PubMed:20512933}.
/FTId=VSP_047760.
VAR_SEQ 518 541 MASTLVVADSRISGIYICIASNKV -> LPPANSSFMLPPT
SFSSNYFHFLP (in isoform 4).
{ECO:0000303|PubMed:18593464}.
/FTId=VSP_041929.
VAR_SEQ 542 1338 Missing (in isoform 4).
{ECO:0000303|PubMed:18593464}.
/FTId=VSP_041930.
VAR_SEQ 657 687 DQEAPYLLRNLSDHTVAISSSTTLDCHANGV -> GEHCNK
KAVFSRISKFKSTRNDCTTQSNVKH (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8248162}.
/FTId=VSP_002955.
VAR_SEQ 688 1338 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8248162}.
/FTId=VSP_002956.
VAR_SEQ 706 733 GIILGPGSSTLFIERVTEEDEGVYHCKA -> ELYTSTSPS
SSSSSPLSSSSSSSSSSSS (in isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:18515749,
ECO:0000303|Ref.7}.
/FTId=VSP_041927.
VAR_SEQ 734 1338 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:18515749,
ECO:0000303|Ref.7}.
/FTId=VSP_041928.
VARIANT 60 60 K -> T (in dbSNP:rs56409818).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042045.
VARIANT 128 128 I -> L (in dbSNP:rs35073261).
/FTId=VAR_049719.
VARIANT 144 144 E -> K (in dbSNP:rs55974987).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042046.
VARIANT 281 281 R -> Q (in dbSNP:rs55687105).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042047.
VARIANT 422 422 L -> I (in a lung adenocarcinoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042048.
VARIANT 781 781 R -> Q (in a glioma low grade
oligodendroglioma sample; somatic
mutation; dbSNP:rs553261958).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042049.
VARIANT 938 938 M -> V (in dbSNP:rs35549791).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042050.
VARIANT 982 982 E -> A (in dbSNP:rs35832528).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042051.
VARIANT 1061 1061 L -> V (in a bladder transitional cell
carcinoma sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042052.
MUTAGEN 767 767 V->A: Abolishes proteolytic cleavage by
PSEN1. {ECO:0000269|PubMed:22016384}.
MUTAGEN 861 861 K->M: Abolishes enzyme activity.
Abolishes interaction with PLCG.
{ECO:0000269|PubMed:9299537}.
MUTAGEN 914 914 Y->F: Reduces phosphorylation at other
tyrosine residues.
{ECO:0000269|PubMed:9722576}.
MUTAGEN 1050 1050 N->D: Strongly increases kinase activity.
Increases activity in promoting
proliferation of endothelial cells.
{ECO:0000269|PubMed:16286478}.
MUTAGEN 1169 1169 Y->F: Loss of phosphorylation site.
Abolishes interaction with PLCG.
{ECO:0000269|PubMed:9299537}.
MUTAGEN 1213 1213 Y->F: Loss of phosphorylation site.
Abolishes interaction with PIK3R1.
{ECO:0000269|PubMed:9722576}.
MUTAGEN 1242 1242 Y->F: Loss of phosphorylation site.
{ECO:0000269|PubMed:9722576}.
MUTAGEN 1327 1327 Y->F: Loss of phosphorylation site.
{ECO:0000269|PubMed:9722576}.
MUTAGEN 1333 1333 Y->F: Loss of phosphorylation site.
Abolishes interaction with CBL.
{ECO:0000269|PubMed:15001553,
ECO:0000269|PubMed:9722576}.
CONFLICT 490 490 F -> S (in Ref. 3; AAC16449).
{ECO:0000305}.
CONFLICT 779 779 F -> L (in Ref. 1; CAA35946).
{ECO:0000305}.
CONFLICT 1029 1029 L -> F (in Ref. 6; ABI53803/ABI53804).
{ECO:0000305}.
TURN 130 132 {ECO:0000244|PDB:1QSV}.
STRAND 135 137 {ECO:0000244|PDB:1FLT}.
STRAND 140 142 {ECO:0000244|PDB:4CL7}.
STRAND 144 148 {ECO:0000244|PDB:1FLT}.
STRAND 150 152 {ECO:0000244|PDB:1QSZ}.
STRAND 154 156 {ECO:0000244|PDB:1FLT}.
STRAND 160 162 {ECO:0000244|PDB:5ABD}.
HELIX 163 165 {ECO:0000244|PDB:1QSV}.
STRAND 168 171 {ECO:0000244|PDB:1FLT}.
TURN 172 174 {ECO:0000244|PDB:1FLT}.
STRAND 175 177 {ECO:0000244|PDB:1FLT}.
STRAND 181 187 {ECO:0000244|PDB:1FLT}.
TURN 188 190 {ECO:0000244|PDB:1FLT}.
STRAND 191 196 {ECO:0000244|PDB:1FLT}.
HELIX 199 201 {ECO:0000244|PDB:1FLT}.
STRAND 203 211 {ECO:0000244|PDB:1FLT}.
STRAND 214 224 {ECO:0000244|PDB:1FLT}.
HELIX 806 809 {ECO:0000244|PDB:3HNG}.
HELIX 817 820 {ECO:0000244|PDB:3HNG}.
HELIX 824 826 {ECO:0000244|PDB:3HNG}.
STRAND 827 835 {ECO:0000244|PDB:3HNG}.
STRAND 837 848 {ECO:0000244|PDB:3HNG}.
HELIX 849 851 {ECO:0000244|PDB:3HNG}.
STRAND 854 863 {ECO:0000244|PDB:3HNG}.
HELIX 869 883 {ECO:0000244|PDB:3HNG}.
STRAND 894 898 {ECO:0000244|PDB:3HNG}.
STRAND 906 910 {ECO:0000244|PDB:3HNG}.
HELIX 917 922 {ECO:0000244|PDB:3HNG}.
HELIX 996 1014 {ECO:0000244|PDB:3HNG}.
TURN 1015 1017 {ECO:0000244|PDB:3HNG}.
HELIX 1025 1027 {ECO:0000244|PDB:3HNG}.
STRAND 1028 1030 {ECO:0000244|PDB:3HNG}.
HELIX 1032 1034 {ECO:0000244|PDB:3HNG}.
STRAND 1036 1038 {ECO:0000244|PDB:3HNG}.
HELIX 1042 1044 {ECO:0000244|PDB:3HNG}.
TURN 1047 1049 {ECO:0000244|PDB:3HNG}.
STRAND 1053 1055 {ECO:0000244|PDB:3HNG}.
HELIX 1063 1065 {ECO:0000244|PDB:3HNG}.
HELIX 1068 1073 {ECO:0000244|PDB:3HNG}.
HELIX 1078 1093 {ECO:0000244|PDB:3HNG}.
HELIX 1107 1113 {ECO:0000244|PDB:3HNG}.
TURN 1114 1116 {ECO:0000244|PDB:3HNG}.
HELIX 1127 1136 {ECO:0000244|PDB:3HNG}.
HELIX 1141 1143 {ECO:0000244|PDB:3HNG}.
HELIX 1147 1157 {ECO:0000244|PDB:3HNG}.
SEQUENCE 1338 AA; 150769 MW; FF3381EEFAF0787C CRC64;
MVSYWDTGVL LCALLSCLLL TGSSSGSKLK DPELSLKGTQ HIMQAGQTLH LQCRGEAAHK
WSLPEMVSKE SERLSITKSA CGRNGKQFCS TLTLNTAQAN HTGFYSCKYL AVPTSKKKET
ESAIYIFISD TGRPFVEMYS EIPEIIHMTE GRELVIPCRV TSPNITVTLK KFPLDTLIPD
GKRIIWDSRK GFIISNATYK EIGLLTCEAT VNGHLYKTNY LTHRQTNTII DVQISTPRPV
KLLRGHTLVL NCTATTPLNT RVQMTWSYPD EKNKRASVRR RIDQSNSHAN IFYSVLTIDK
MQNKDKGLYT CRVRSGPSFK SVNTSVHIYD KAFITVKHRK QQVLETVAGK RSYRLSMKVK
AFPSPEVVWL KDGLPATEKS ARYLTRGYSL IIKDVTEEDA GNYTILLSIK QSNVFKNLTA
TLIVNVKPQI YEKAVSSFPD PALYPLGSRQ ILTCTAYGIP QPTIKWFWHP CNHNHSEARC
DFCSNNEESF ILDADSNMGN RIESITQRMA IIEGKNKMAS TLVVADSRIS GIYICIASNK
VGTVGRNISF YITDVPNGFH VNLEKMPTEG EDLKLSCTVN KFLYRDVTWI LLRTVNNRTM
HYSISKQKMA ITKEHSITLN LTIMNVSLQD SGTYACRARN VYTGEEILQK KEITIRDQEA
PYLLRNLSDH TVAISSSTTL DCHANGVPEP QITWFKNNHK IQQEPGIILG PGSSTLFIER
VTEEDEGVYH CKATNQKGSV ESSAYLTVQG TSDKSNLELI TLTCTCVAAT LFWLLLTLFI
RKMKRSSSEI KTDYLSIIMD PDEVPLDEQC ERLPYDASKW EFARERLKLG KSLGRGAFGK
VVQASAFGIK KSPTCRTVAV KMLKEGATAS EYKALMTELK ILTHIGHHLN VVNLLGACTK
QGGPLMVIVE YCKYGNLSNY LKSKRDLFFL NKDAALHMEP KKEKMEPGLE QGKKPRLDSV
TSSESFASSG FQEDKSLSDV EEEEDSDGFY KEPITMEDLI SYSFQVARGM EFLSSRKCIH
RDLAARNILL SENNVVKICD FGLARDIYKN PDYVRKGDTR LPLKWMAPES IFDKIYSTKS
DVWSYGVLLW EIFSLGGSPY PGVQMDEDFC SRLREGMRMR APEYSTPEIY QIMLDCWHRD
PKERPRFAEL VEKLGDLLQA NVQQDGKDYI PINAILTGNS GFTYSTPAFS EDFFKESISA
PKFNSGSSDD VRYVNAFKFM SLERIKTFEE LLPNATSMFD DYQGDSSTLL ASPMLKRFTW
TDSKPKASLK IDLRVTSKSK ESGLSDVSRP SFCHSSCGHV SEGKRRFTYD HAELERKIAC
CSPPPDYNSV VLYSTPPI


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