VGFR1_HUMAN
ID VGFR1_HUMAN Reviewed; 1338 AA.
AC P17948; A3E342; A3E344; A8KA71; B0LPF1; B2BF46; B2BF47; B2BF48; B3FR89;
AC B5A923; F5H5L6; O60722; P16057; Q12954;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 243.
DE RecName: Full=Vascular endothelial growth factor receptor 1;
DE Short=VEGFR-1;
DE EC=2.7.10.1;
DE AltName: Full=Fms-like tyrosine kinase 1;
DE Short=FLT-1;
DE AltName: Full=Tyrosine-protein kinase FRT;
DE AltName: Full=Tyrosine-protein kinase receptor FLT;
DE Short=FLT;
DE AltName: Full=Vascular permeability factor receptor;
DE Flags: Precursor;
GN Name=FLT1; Synonyms=FLT, FRT, VEGFR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=2158038;
RA Shibuya M., Yamaguchi S., Yamane A., Ikeda T., Tojo A., Matsushime H.,
RA Sato M.;
RT "Nucleotide sequence and expression of a novel human receptor-type tyrosine
RT kinase gene (flt) closely related to the fms family.";
RL Oncogene 5:519-524(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF N-TERMINUS,
RP SUBCELLULAR LOCATION (ISOFORM 2), INTERACTION WITH VEGFA, AND FUNCTION.
RC TISSUE=Umbilical vein;
RX PubMed=8248162; DOI=10.1073/pnas.90.22.10705;
RA Kendall R.L., Thomas K.A.;
RT "Inhibition of vascular endothelial cell growth factor activity by an
RT endogenously encoded soluble receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:10705-10709(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH VEGFA, AND
RP GLYCOSYLATION.
RC TISSUE=Umbilical vein;
RX PubMed=10471394; DOI=10.1006/bbrc.1999.1282;
RA Herley M.T., Yu Y., Whitney R.G., Sato J.D.;
RT "Characterization of the VEGF binding site on the Flt-1 receptor.";
RL Biochem. Biophys. Res. Commun. 262:731-738(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION IN LIGAND BINDING, AND
RP SUBCELLULAR LOCATION.
RX PubMed=18593464; DOI=10.1186/ar2447;
RA Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D.,
RA Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.;
RT "Novel splice variants derived from the receptor tyrosine kinase
RT superfamily are potential therapeutics for rheumatoid arthritis.";
RL Arthritis Res. Ther. 10:R73-R73(2008).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, ROLE IN PREECLAMPSIA, AND INDUCTION.
RX PubMed=18515749; DOI=10.1161/circresaha.108.171504;
RA Sela S., Itin A., Natanson-Yaron S., Greenfield C., Goldman-Wohl D.,
RA Yagel S., Keshet E.;
RT "A novel human-specific soluble vascular endothelial growth factor receptor
RT 1: cell-type-specific splicing and implications to vascular endothelial
RT growth factor homeostasis and preeclampsia.";
RL Circ. Res. 102:1566-1574(2008).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5; 6; 7 AND 8), ALTERNATIVE SPLICING,
RP FUNCTION IN PHOSPHORYLATION OF SRC AND CANCER CELL INVASIVENESS, AND TISSUE
RP SPECIFICITY.
RX PubMed=20512933; DOI=10.1002/jcb.22584;
RA Mezquita B., Mezquita J., Pau M., Mezquita C.;
RT "A novel intracellular isoform of VEGFR-1 activates Src and promotes cell
RT invasion in MDA-MB-231 breast cancer cells.";
RL J. Cell. Biochem. 110:732-742(2010).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Mezquita J., Mezquita B., Pau M., Mezquita C.;
RT "A new VEGFR1 receptor transcript coding for the extracellular domains of
RT the protein followed by a C-terminal polyserine tail.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Placenta, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1018-1058, AND ALTERNATIVE SPLICING
RP (ISOFORM 1).
RX PubMed=3040650;
RA Matsushime H., Yoshida M.C., Sasaki M., Shibuya M.;
RT "A possible new member of tyrosine kinase family, human frt sequence, is
RT highly conserved in vertebrates and located on human chromosome 13.";
RL Jpn. J. Cancer Res. 78:655-661(1987).
RN [14]
RP PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY, PHOSPHORYLATION AT TYR-914;
RP TYR-1213; TYR-1242; TYR-1327 AND TYR-1333, MUTAGENESIS OF TYR-914;
RP TYR-1213; TYR-1242; TYR-1327 AND TYR-1333, AND INTERACTION WITH PLCG; GRB2;
RP CRK; NCK1 AND PTPN11.
RX PubMed=9722576; DOI=10.1074/jbc.273.36.23410;
RA Ito N., Wernstedt C., Engstrom U., Claesson-Welsh L.;
RT "Identification of vascular endothelial growth factor receptor-1 tyrosine
RT phosphorylation sites and binding of SH2 domain-containing molecules.";
RL J. Biol. Chem. 273:23410-23418(1998).
RN [15]
RP INTERACTION WITH VEGFA, AUTOPHOSPHORYLATION, CATALYTIC ACTIVITY, FUNCTION
RP IN PHOSPHORYLATION OF PLCG, AND ABSENCE OF MITOGENIC FUNCTION IN CULTURED
RP FIBROBLASTS.
RX PubMed=7824266;
RA Seetharam L., Gotoh N., Maru Y., Neufeld G., Yamaguchi S., Shibuya M.;
RT "A unique signal transduction from FLT tyrosine kinase, a receptor for
RT vascular endothelial growth factor VEGF.";
RL Oncogene 10:135-147(1995).
RN [16]
RP FUNCTION IN CELL MIGRATION, FUNCTION IN VEGFA AND PGF SIGNALING, AND
RP INDUCTION.
RX PubMed=8605350;
RA Barleon B., Sozzani S., Zhou D., Weich H.A., Mantovani A., Marme D.;
RT "Migration of human monocytes in response to vascular endothelial growth
RT factor (VEGF) is mediated via the VEGF receptor flt-1.";
RL Blood 87:3336-3343(1996).
RN [17]
RP FUNCTION IN PHOSPHORYLATION OF PLCG AND ACTIVATION OF MAP KINASES,
RP INTERACTION WITH PLCG, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-861 AND
RP TYR-1169, AND PHOSPHORYLATION AT TYR-1169 AND TYR-1213.
RX PubMed=9299537; DOI=10.1006/bbrc.1997.7327;
RA Sawano A., Takahashi T., Yamaguchi S., Shibuya M.;
RT "The phosphorylated 1169-tyrosine containing region of flt-1 kinase (VEGFR-
RT 1) is a major binding site for PLCgamma.";
RL Biochem. Biophys. Res. Commun. 238:487-491(1997).
RN [18]
RP INTERACTION WITH PIK3R1; PTPN11 AND NCK1, AND PHOSPHORYLATION AT TYR-1213.
RX PubMed=9600074; DOI=10.1006/bbrc.1998.8578;
RA Igarashi K., Isohara T., Kato T., Shigeta K., Yamano T., Uno I.;
RT "Tyrosine 1213 of Flt-1 is a major binding site of Nck and SHP-2.";
RL Biochem. Biophys. Res. Commun. 246:95-99(1998).
RN [19]
RP FUNCTION AS NEGATIVE REGULATOR OF KDR-MEDIATED CELL PROLIFERATION.
RX PubMed=11141500; DOI=10.1016/s0002-9440(10)63965-x;
RA Dunk C., Ahmed A.;
RT "Vascular endothelial growth factor receptor-2-mediated mitogenesis is
RT negatively regulated by vascular endothelial growth factor receptor-1 in
RT tumor epithelial cells.";
RL Am. J. Pathol. 158:265-273(2001).
RN [20]
RP INTERACTION WITH PIK3R1 AND VEGFA, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT
RP TYR-1213, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP GLYCOSYLATION.
RX PubMed=11513746; DOI=10.1042/0264-6021:3580465;
RA Yu Y., Hulmes J.D., Herley M.T., Whitney R.G., Crabb J.W., Sato J.D.;
RT "Direct identification of a major autophosphorylation site on vascular
RT endothelial growth factor receptor Flt-1 that mediates phosphatidylinositol
RT 3'-kinase binding.";
RL Biochem. J. 358:465-472(2001).
RN [21]
RP FUNCTION IN PGF-MEDIATED CHORIOCARCINOMA CELL PROLIFERATION.
RX PubMed=11811792; DOI=10.3109/08977190109001086;
RA Angelucci C., Lama G., Iacopino F., Maglione D., Sica G.;
RT "Effect of placenta growth factor-1 on proliferation and release of nitric
RT oxide, cyclic AMP and cyclic GMP in human epithelial cells expressing the
RT FLT-1 receptor.";
RL Growth Factors 19:193-206(2001).
RN [22]
RP INTERACTION WITH KDR, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, AND FUNCTION
RP IN VEGFA SIGNALING; PHOSPHORYLATION OF PLCG AND ACTIVATION OF
RP PHOSPHATIDYLINOSITOL KINASE AND PHOSPHOLIPASE C.
RX PubMed=11312102; DOI=10.1016/s1357-2725(01)00019-x;
RA Huang K., Andersson C., Roomans G.M., Ito N., Claesson-Welsh L.;
RT "Signaling properties of VEGF receptor-1 and -2 homo- and heterodimers.";
RL Int. J. Biochem. Cell Biol. 33:315-324(2001).
RN [23]
RP FUNCTION IN SIGNALING VIA ACTIVATION OF THE PHOSPHATIDYLINOSITOL KINASE
RP PATHWAY AND POSITIVE REGULATION OF ANGIOGENESIS IN RESPONSE TO PGF AND
RP VEGFA.
RX PubMed=14633857; DOI=10.2337/diabetes.52.12.2959;
RA Cai J., Ahmad S., Jiang W.G., Huang J., Kontos C.D., Boulton M., Ahmed A.;
RT "Activation of vascular endothelial growth factor receptor-1 sustains
RT angiogenesis and Bcl-2 expression via the phosphatidylinositol 3-kinase
RT pathway in endothelial cells.";
RL Diabetes 52:2959-2968(2003).
RN [24]
RP INTERACTION WITH PGF AND KDR, FUNCTION IN PHOSPHORYLATION OF KDR; VEGFA AND
RP PGF SIGNALING, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP PHOSPHORYLATION AT TYR-1213; TYR-1327 AND TYR-1309.
RX PubMed=12796773; DOI=10.1038/nm884;
RA Autiero M., Waltenberger J., Communi D., Kranz A., Moons L., Lambrechts D.,
RA Kroll J., Plaisance S., De Mol M., Bono F., Kliche S., Fellbrich G.,
RA Ballmer-Hofer K., Maglione D., Mayr-Beyrle U., Dewerchin M., Dombrowski S.,
RA Stanimirovic D., Van Hummelen P., Dehio C., Hicklin D.J., Persico G.,
RA Herbert J.M., Communi D., Shibuya M., Collen D., Conway E.M., Carmeliet P.;
RT "Role of PlGF in the intra- and intermolecular cross talk between the VEGF
RT receptors Flt1 and Flk1.";
RL Nat. Med. 9:936-943(2003).
RN [25]
RP INTERACTION WITH CBL AND CD2AP, UBIQUITINATION, AUTOPHOSPHORYLATION IN
RP RESPONSE TO VEGFA, MUTAGENESIS OF TYR-1333, AND SUBCELLULAR LOCATION.
RX PubMed=15001553; DOI=10.1096/fj.03-0767fje;
RA Kobayashi S., Sawano A., Nojima Y., Shibuya M., Maru Y.;
RT "The c-Cbl/CD2AP complex regulates VEGF-induced endocytosis and degradation
RT of Flt-1 (VEGFR-1).";
RL FASEB J. 18:929-931(2004).
RN [26]
RP FUNCTION IN VEGFA AND VEGFB SIGNALING; CANCER CELL MIGRATION; INVASIVENESS
RP AND ACTIVATION OF MAPK1/ERK2 AND MAPK3/ERK1.
RX PubMed=15735759; DOI=10.1038/sj.onc.1208246;
RA Fan F., Wey J.S., McCarty M.F., Belcheva A., Liu W., Bauer T.W.,
RA Somcio R.J., Wu Y., Hooper A., Hicklin D.J., Ellis L.M.;
RT "Expression and function of vascular endothelial growth factor receptor-1
RT on human colorectal cancer cells.";
RL Oncogene 24:2647-2653(2005).
RN [27]
RP FUNCTION IN CELL MIGRATION AND PHOSPHORYLATION OF PTK2/FAK1; YES1 AND SRC.
RX PubMed=16685275; DOI=10.1038/sj.bjc.6603143;
RA Lesslie D.P., Summy J.M., Parikh N.U., Fan F., Trevino J.G., Sawyer T.K.,
RA Metcalf C.A., Shakespeare W.C., Hicklin D.J., Ellis L.M., Gallick G.E.;
RT "Vascular endothelial growth factor receptor-1 mediates migration of human
RT colorectal carcinoma cells by activation of Src family kinases.";
RL Br. J. Cancer 94:1710-1717(2006).
RN [28]
RP MUTAGENESIS OF ASN-1050.
RX PubMed=16286478; DOI=10.1074/jbc.m506454200;
RA Meyer R.D., Mohammadi M., Rahimi N.;
RT "A single amino acid substitution in the activation loop defines the decoy
RT characteristic of VEGFR-1/FLT-1.";
RL J. Biol. Chem. 281:867-875(2006).
RN [29]
RP FUNCTION IN PGF AND VEGFA SIGNALING; PHOSPHORYLATION OF AKT1; MAPK3/ERK1
RP AND MAP KINASES; CHEMOTAXIS AND ACTIVATION OF PHOSPHATIDYLINOSITOL
RP 3-KINASE, AND AUTOPHOSPHORYLATION IN RESPONSE TO PGF AND VEGFA.
RX PubMed=18079407; DOI=10.1161/atvbaha.107.158022;
RA Tchaikovski V., Fellbrich G., Waltenberger J.;
RT "The molecular basis of VEGFR-1 signal transduction pathways in primary
RT human monocytes.";
RL Arterioscler. Thromb. Vasc. Biol. 28:322-328(2008).
RN [30]
RP FUNCTION IN ENDOTHELIAL CELL SURVIVAL AND ANGIOGENESIS.
RX PubMed=18583712; DOI=10.1161/circresaha.108.174128;
RA Nishi J., Minamino T., Miyauchi H., Nojima A., Tateno K., Okada S.,
RA Orimo M., Moriya J., Fong G.H., Sunagawa K., Shibuya M., Komuro I.;
RT "Vascular endothelial growth factor receptor-1 regulates postnatal
RT angiogenesis through inhibition of the excessive activation of Akt.";
RL Circ. Res. 103:261-268(2008).
RN [31]
RP FUNCTION IN CANCER CELL MIGRATION AND ACTIVATION OF MAPK1/ERK2 AND/OR
RP MAPK3/ERK1.
RX PubMed=20551949; DOI=10.1038/sj.bjc.6605746;
RA Taylor A.P., Leon E., Goldenberg D.M.;
RT "Placental growth factor (PlGF) enhances breast cancer cell motility by
RT mobilising ERK1/2 phosphorylation and cytoskeletal rearrangement.";
RL Br. J. Cancer 103:82-89(2010).
RN [32]
RP INTERACTION WITH RACK1.
RX PubMed=21212275; DOI=10.1074/jbc.m110.165605;
RA Wang F., Yamauchi M., Muramatsu M., Osawa T., Tsuchida R., Shibuya M.;
RT "RACK1 regulates VEGF/Flt1-mediated cell migration via activation of a PI3-
RT K/Akt pathway.";
RL J. Biol. Chem. 286:9097-9106(2011).
RN [33]
RP INTERACTION WITH PSEN1 AND PTPRB, DEPHOSPHORYLATION BY PTPRB, MUTAGENESIS
RP OF VAL-767, AND PROTEOLYTIC CLEAVAGE BY PSEN1 AT VAL-767.
RX PubMed=22016384; DOI=10.1074/jbc.m111.296590;
RA Cai J., Chen Z., Ruan Q., Han S., Liu L., Qi X., Boye S.L., Hauswirth W.W.,
RA Grant M.B., Boulton M.E.;
RT "gamma-Secretase and presenilin mediate cleavage and phosphorylation of
RT vascular endothelial growth factor receptor-1.";
RL J. Biol. Chem. 286:42514-42523(2011).
RN [34]
RP FUNCTION AS DECOY RECEPTORS; REGULATION OF VEGFA SIGNALING AND REGULATION
RP OF KDR ACTIVITY (ISOFORMS 2/3/4), AND ROLE IN PREECLAMPSIA.
RX PubMed=21752276; DOI=10.1186/2045-824x-3-15;
RA Ahmad S., Hewett P.W., Al-Ani B., Sissaoui S., Fujisawa T., Cudmore M.J.,
RA Ahmed A.;
RT "Autocrine activity of soluble Flt-1 controls endothelial cell function and
RT angiogenesis.";
RL Vasc. Cell 3:15-15(2011).
RN [35]
RP REVIEW ON FUNCTION AS NEGATIVE REGULATOR OF ANGIOGENESIS DURING EMBRYONIC
RP DEVELOPMENT; POSITIVE REGULATION OF MACROPHAGE FUNCTION IN ADULTHOOD; ROLE
RP IN CARCINOGENESIS AND INFLAMMATION.
RX PubMed=17002866; DOI=10.5483/bmbrep.2006.39.5.469;
RA Shibuya M.;
RT "Differential roles of vascular endothelial growth factor receptor-1 and
RT receptor-2 in angiogenesis.";
RL J. Biochem. Mol. Biol. 39:469-478(2006).
RN [36]
RP REVIEW ON STRUCTURE AND FUNCTION.
RX PubMed=18680722; DOI=10.1016/j.bbrc.2008.07.121;
RA Roskoski R. Jr.;
RT "VEGF receptor protein-tyrosine kinases: structure and regulation.";
RL Biochem. Biophys. Res. Commun. 375:287-291(2008).
RN [37]
RP REVIEW ON ROLE IN ANGIOGENESIS AND CANCER.
RX PubMed=19230644; DOI=10.1016/j.ceb.2008.12.012;
RA Lohela M., Bry M., Tammela T., Alitalo K.;
RT "VEGFs and receptors involved in angiogenesis versus lymphangiogenesis.";
RL Curr. Opin. Cell Biol. 21:154-165(2009).
RN [38]
RP REVIEW ON LIGAND SPECIFICITY; FUNCTION; STRUCTURE; PHOSPHORYLATION AND
RP SIGNALING.
RX PubMed=19761875; DOI=10.1016/j.bbapap.2009.09.002;
RA Grunewald F.S., Prota A.E., Giese A., Ballmer-Hofer K.;
RT "Structure-function analysis of VEGF receptor activation and the role of
RT coreceptors in angiogenic signaling.";
RL Biochim. Biophys. Acta 1804:567-580(2010).
RN [39]
RP REVIEW ON ROLE IN CANCER.
RX PubMed=20127948; DOI=10.1002/cncr.24789;
RA Schwartz J.D., Rowinsky E.K., Youssoufian H., Pytowski B., Wu Y.;
RT "Vascular endothelial growth factor receptor-1 in human cancer: concise
RT review and rationale for development of IMC-18F1 (Human antibody targeting
RT vascular endothelial growth factor receptor-1).";
RL Cancer 116:1027-1032(2010).
RN [40]
RP REVIEW ON LIGAND SPECIFICITY; FUNCTION; STRUCTURE; PHOSPHORYLATION AND
RP SIGNALING.
RX PubMed=21711246; DOI=10.1042/bj20110301;
RA Koch S., Tugues S., Li X., Gualandi L., Claesson-Welsh L.;
RT "Signal transduction by vascular endothelial growth factor receptors.";
RL Biochem. J. 437:169-183(2011).
RN [41]
RP REVIEW ON ROLE IN CANCER AND PREECLAMPSIA.
RX PubMed=21558755; DOI=10.2183/pjab.87.167;
RA Shibuya M.;
RT "Involvement of Flt-1 (VEGF receptor-1) in cancer and preeclampsia.";
RL Proc. Jpn. Acad., B, Phys. Biol. Sci. 87:167-178(2011).
RN [42]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 132-226 IN COMPLEX WITH VEGFA, AND
RP DOMAIN.
RX PubMed=9393862; DOI=10.1016/s0092-8674(00)80456-0;
RA Wiesmann C., Fuh G., Christinger H.W., Eigenbrot C., Wells J.A.,
RA de Vos A.M.;
RT "Crystal structure at 1.7 A resolution of VEGF in complex with domain 2 of
RT the Flt-1 receptor.";
RL Cell 91:695-704(1997).
RN [43]
RP STRUCTURE BY NMR OF 129-229, X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF
RP 129-229 IN COMPLEX WITH VEGFA, SUBUNIT, AND INTERACTION WITH VEGFA.
RX PubMed=10543948; DOI=10.1006/jmbi.1999.3134;
RA Starovasnik M.A., Christinger H.W., Wiesmann C., Champe M.A., de Vos A.M.,
RA Skelton N.J.;
RT "Solution structure of the VEGF-binding domain of Flt-1: comparison of its
RT free and bound states.";
RL J. Mol. Biol. 293:531-544(1999).
RN [44]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 130-229 IN COMPLEX WITH PGF.
RX PubMed=14684734; DOI=10.1074/jbc.m313237200;
RA Christinger H.W., Fuh G., de Vos A.M., Wiesmann C.;
RT "The crystal structure of placental growth factor in complex with domain 2
RT of vascular endothelial growth factor receptor-1.";
RL J. Biol. Chem. 279:10382-10388(2004).
RN [45]
RP X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 129-226 IN COMPLEX WITH VEGFB,
RP INTERACTION WITH VEGFB, SUBUNIT, AND DOMAIN.
RX PubMed=20501651; DOI=10.1074/jbc.m110.130658;
RA Iyer S., Darley P.I., Acharya K.R.;
RT "Structural insights into the binding of vascular endothelial growth
RT factor-B by VEGFR-1(D2): recognition and specificity.";
RL J. Biol. Chem. 285:23779-23789(2010).
RN [46]
RP VARIANTS [LARGE SCALE ANALYSIS] THR-60; LYS-144; GLN-281; ILE-422; GLN-781;
RP VAL-938; ALA-982 AND VAL-1061.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor
CC for VEGFA, VEGFB and PGF, and plays an essential role in the
CC development of embryonic vasculature, the regulation of angiogenesis,
CC cell survival, cell migration, macrophage function, chemotaxis, and
CC cancer cell invasion. Acts as a positive regulator of postnatal retinal
CC hyaloid vessel regression (Ref.11). May play an essential role as a
CC negative regulator of embryonic angiogenesis by inhibiting excessive
CC proliferation of endothelial cells. Can promote endothelial cell
CC proliferation, survival and angiogenesis in adulthood. Its function in
CC promoting cell proliferation seems to be cell-type specific. Promotes
CC PGF-mediated proliferation of endothelial cells, proliferation of some
CC types of cancer cells, but does not promote proliferation of normal
CC fibroblasts (in vitro). Has very high affinity for VEGFA and relatively
CC low protein kinase activity; may function as a negative regulator of
CC VEGFA signaling by limiting the amount of free VEGFA and preventing its
CC binding to KDR. Modulates KDR signaling by forming heterodimers with
CC KDR. Ligand binding leads to the activation of several signaling
CC cascades. Activation of PLCG leads to the production of the cellular
CC signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and
CC the activation of protein kinase C. Mediates phosphorylation of PIK3R1,
CC the regulatory subunit of phosphatidylinositol 3-kinase, leading to
CC activation of phosphatidylinositol kinase and the downstream signaling
CC pathway. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP
CC kinase signaling pathway, as well as of the AKT1 signaling pathway.
CC Phosphorylates SRC and YES1, and may also phosphorylate CBL. Promotes
CC phosphorylation of AKT1 at 'Ser-473'. Promotes phosphorylation of
CC PTK2/FAK1 (PubMed:16685275). {ECO:0000269|PubMed:11141500,
CC ECO:0000269|PubMed:11312102, ECO:0000269|PubMed:11811792,
CC ECO:0000269|PubMed:12796773, ECO:0000269|PubMed:14633857,
CC ECO:0000269|PubMed:15735759, ECO:0000269|PubMed:16685275,
CC ECO:0000269|PubMed:18079407, ECO:0000269|PubMed:18515749,
CC ECO:0000269|PubMed:18583712, ECO:0000269|PubMed:18593464,
CC ECO:0000269|PubMed:20512933, ECO:0000269|PubMed:20551949,
CC ECO:0000269|PubMed:21752276, ECO:0000269|PubMed:7824266,
CC ECO:0000269|PubMed:8248162, ECO:0000269|PubMed:8605350,
CC ECO:0000269|PubMed:9299537, ECO:0000269|Ref.11}.
CC -!- FUNCTION: [Isoform 1]: Phosphorylates PLCG.
CC {ECO:0000269|PubMed:9299537}.
CC -!- FUNCTION: [Isoform 2]: May function as decoy receptor for VEGFA.
CC {ECO:0000269|PubMed:21752276}.
CC -!- FUNCTION: [Isoform 3]: May function as decoy receptor for VEGFA.
CC {ECO:0000269|PubMed:21752276}.
CC -!- FUNCTION: [Isoform 4]: May function as decoy receptor for VEGFA.
CC {ECO:0000269|PubMed:21752276}.
CC -!- FUNCTION: [Isoform 7]: Has a truncated kinase domain; it increases
CC phosphorylation of SRC at 'Tyr-418' by unknown means and promotes tumor
CC cell invasion. {ECO:0000269|PubMed:20512933}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028,
CC ECO:0000269|PubMed:11312102, ECO:0000269|PubMed:12796773,
CC ECO:0000269|PubMed:7824266, ECO:0000269|PubMed:9299537,
CC ECO:0000269|PubMed:9722576};
CC -!- ACTIVITY REGULATION: Present in an inactive conformation in the absence
CC of bound ligand. Binding of VEGFA, VEGFB or PGF leads to dimerization
CC and activation by autophosphorylation on tyrosine residues.
CC -!- SUBUNIT: Interacts with VEGFA, VEGFB and PGF. Monomer in the absence of
CC bound VEGFA, VEGFB or PGF. Homodimer in the presence of bound VEGFA,
CC VEGFB and PGF. Can also form a heterodimer with KDR. Interacts (when
CC tyrosine phosphorylated) with CBL, CRK, GRB2, NCK1, PIK3R1, PLCG, PSEN1
CC and PTPN11. Probably interacts also with PTPRB. Interacts with RACK1.
CC Identified in a complex with CBL and CD2AP.
CC {ECO:0000269|PubMed:10471394, ECO:0000269|PubMed:10543948,
CC ECO:0000269|PubMed:11312102, ECO:0000269|PubMed:11513746,
CC ECO:0000269|PubMed:12796773, ECO:0000269|PubMed:14684734,
CC ECO:0000269|PubMed:15001553, ECO:0000269|PubMed:20501651,
CC ECO:0000269|PubMed:21212275, ECO:0000269|PubMed:22016384,
CC ECO:0000269|PubMed:7824266, ECO:0000269|PubMed:8248162,
CC ECO:0000269|PubMed:9299537, ECO:0000269|PubMed:9393862,
CC ECO:0000269|PubMed:9600074, ECO:0000269|PubMed:9722576}.
CC -!- INTERACTION:
CC P17948; P22681: CBL; NbExp=2; IntAct=EBI-1026718, EBI-518228;
CC P17948; P46109: CRKL; NbExp=9; IntAct=EBI-1026718, EBI-910;
CC P17948; P49763: PGF; NbExp=2; IntAct=EBI-1026718, EBI-1037633;
CC P17948; P27986: PIK3R1; NbExp=3; IntAct=EBI-1026718, EBI-79464;
CC P17948; Q12913: PTPRJ; NbExp=2; IntAct=EBI-1026718, EBI-2264500;
CC P17948; P15692: VEGFA; NbExp=4; IntAct=EBI-1026718, EBI-1026643;
CC P17948; P15692-4: VEGFA; NbExp=3; IntAct=EBI-1026718, EBI-1026691;
CC P17948-2; PRO_0000391621 [P98160]: HSPG2; NbExp=2; IntAct=EBI-6530464, EBI-6896259;
CC P17948-2; PRO_0000391622 [P98160]: HSPG2; NbExp=2; IntAct=EBI-6530464, EBI-6896607;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I
CC membrane protein. Endosome. Note=Autophosphorylation promotes
CC ubiquitination and endocytosis.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted
CC {ECO:0000269|PubMed:8248162}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 7]: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=Flt1;
CC IsoId=P17948-1; Sequence=Displayed;
CC Name=2; Synonyms=sFlt1;
CC IsoId=P17948-2; Sequence=VSP_002955, VSP_002956;
CC Name=3; Synonyms=sFlt1-14;
CC IsoId=P17948-3; Sequence=VSP_041927, VSP_041928;
CC Name=4;
CC IsoId=P17948-4; Sequence=VSP_041929, VSP_041930;
CC Name=5; Synonyms=i15;
CC IsoId=P17948-5; Sequence=VSP_041985;
CC Name=6; Synonyms=i18;
CC IsoId=P17948-6; Sequence=VSP_041984;
CC Name=7; Synonyms=i21;
CC IsoId=P17948-7; Sequence=VSP_041983;
CC Name=8;
CC IsoId=P17948-8; Sequence=VSP_047759, VSP_047760;
CC -!- TISSUE SPECIFICITY: Detected in normal lung, but also in placenta,
CC liver, kidney, heart and brain tissues. Specifically expressed in most
CC of the vascular endothelial cells, and also expressed in peripheral
CC blood monocytes. Isoform 2 is strongly expressed in placenta. Isoform 3
CC is expressed in corneal epithelial cells (at protein level). Isoform 3
CC is expressed in vascular smooth muscle cells (VSMC).
CC {ECO:0000269|PubMed:18515749, ECO:0000269|PubMed:20512933}.
CC -!- INDUCTION: Up-regulated in coculture of VSMC/endothelial cell (EC) or
CC by direct exposure to VEGF of VSMC monoculture. Up-regulated from the
CC second trimester of pregnancy to the term and in the placenta of women
CC with preeclampsia (PE). Up-regulated in monocytes exposed to bacterial
CC lipopolysaccharide (LPS). {ECO:0000269|PubMed:18515749,
CC ECO:0000269|PubMed:8605350}.
CC -!- DOMAIN: The second and third Ig-like C2-type (immunoglobulin-like)
CC domains are sufficient for VEGFA binding. {ECO:0000269|PubMed:20501651,
CC ECO:0000269|PubMed:9393862}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:10471394,
CC ECO:0000269|PubMed:11513746}.
CC -!- PTM: Ubiquitinated after VEGFA-mediated autophosphorylation, leading to
CC proteolytic degradation. {ECO:0000269|PubMed:15001553}.
CC -!- PTM: Autophosphorylated on tyrosine residues upon ligand binding.
CC Autophosphorylation occurs in trans, i.e. one subunit of the dimeric
CC receptor phosphorylates tyrosine residues on the other subunit.
CC Phosphorylation at Tyr-1169 is important for interaction with PLCG.
CC Phosphorylation at Tyr-1213 is important for interaction with PIK3R1,
CC PTPN11, GRB2, and PLCG. Phosphorylation at Tyr-1333 is important for
CC endocytosis and for interaction with CBL, NCK1 and CRK. Is probably
CC dephosphorylated by PTPRB. {ECO:0000269|PubMed:11513746,
CC ECO:0000269|PubMed:12796773, ECO:0000269|PubMed:9299537,
CC ECO:0000269|PubMed:9600074, ECO:0000269|PubMed:9722576}.
CC -!- DISEASE: Note=Can contribute to cancer cell survival, proliferation,
CC migration, and invasion, and tumor angiogenesis and metastasis. May
CC contribute to cancer pathogenesis by promoting inflammatory responses
CC and recruitment of tumor-infiltrating macrophages.
CC -!- DISEASE: Note=Abnormally high expression of soluble isoforms (isoform
CC 2, isoform 3 or isoform 4) may be a cause of preeclampsia.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. CSF-1/PDGF receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X51602; CAA35946.1; -; mRNA.
DR EMBL; U01134; AAC50060.1; -; mRNA.
DR EMBL; AF063657; AAC16449.2; -; mRNA.
DR EMBL; EU826561; ACF47597.1; -; mRNA.
DR EMBL; EU368830; ACA62948.1; -; mRNA.
DR EMBL; DQ836394; ABI53803.1; -; mRNA.
DR EMBL; DQ836395; ABI53804.1; -; mRNA.
DR EMBL; DQ836396; ABI53805.1; -; mRNA.
DR EMBL; EF491868; ABS32268.1; -; mRNA.
DR EMBL; EF491869; ABS32269.1; -; mRNA.
DR EMBL; EF491870; ABS32270.1; -; mRNA.
DR EMBL; EU360600; ACB05747.1; -; mRNA.
DR EMBL; EU332841; ABY87530.1; -; Genomic_DNA.
DR EMBL; AK292936; BAF85625.1; -; mRNA.
DR EMBL; AK300392; BAG62125.1; -; mRNA.
DR EMBL; AL138712; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL139005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08431.1; -; Genomic_DNA.
DR EMBL; CH471075; EAX08432.1; -; Genomic_DNA.
DR EMBL; BC039007; AAH39007.1; -; mRNA.
DR EMBL; D00133; BAA00080.1; -; Genomic_DNA.
DR CCDS; CCDS53860.1; -. [P17948-3]
DR CCDS; CCDS53861.1; -. [P17948-4]
DR CCDS; CCDS73556.1; -. [P17948-2]
DR CCDS; CCDS9330.1; -. [P17948-1]
DR PIR; A49636; A49636.
DR PIR; S09982; S09982.
DR RefSeq; NP_001153392.1; NM_001159920.1. [P17948-2]
DR RefSeq; NP_001153502.1; NM_001160030.1. [P17948-3]
DR RefSeq; NP_001153503.1; NM_001160031.1. [P17948-4]
DR RefSeq; NP_002010.2; NM_002019.4. [P17948-1]
DR PDB; 1FLT; X-ray; 1.70 A; X/Y=132-226.
DR PDB; 1QSV; NMR; -; A=129-229.
DR PDB; 1QSZ; NMR; -; A=129-229.
DR PDB; 1QTY; X-ray; 2.70 A; T/U/X/Y=129-229.
DR PDB; 1RV6; X-ray; 2.45 A; X/Y=130-229.
DR PDB; 2XAC; X-ray; 2.71 A; C/X=129-226.
DR PDB; 3HNG; X-ray; 2.70 A; A=801-1158.
DR PDB; 4CKV; X-ray; 2.06 A; X=132-225.
DR PDB; 4CL7; X-ray; 2.00 A; A/B/C/D=132-225.
DR PDB; 5ABD; X-ray; 2.00 A; E/I/X=132-226.
DR PDB; 5EX3; X-ray; 2.41 A; D=827-835.
DR PDB; 5T89; X-ray; 4.00 A; X/Y=27-656.
DR PDBsum; 1FLT; -.
DR PDBsum; 1QSV; -.
DR PDBsum; 1QSZ; -.
DR PDBsum; 1QTY; -.
DR PDBsum; 1RV6; -.
DR PDBsum; 2XAC; -.
DR PDBsum; 3HNG; -.
DR PDBsum; 4CKV; -.
DR PDBsum; 4CL7; -.
DR PDBsum; 5ABD; -.
DR PDBsum; 5EX3; -.
DR PDBsum; 5T89; -.
DR AlphaFoldDB; P17948; -.
DR SMR; P17948; -.
DR BioGRID; 108609; 67.
DR DIP; DIP-643N; -.
DR IntAct; P17948; 49.
DR MINT; P17948; -.
DR STRING; 9606.ENSP00000282397; -.
DR BindingDB; P17948; -.
DR ChEMBL; CHEMBL1868; -.
DR DrugBank; DB06626; Axitinib.
DR DrugBank; DB05932; Denibulin.
DR DrugBank; DB10770; Foreskin fibroblast (neonatal).
DR DrugBank; DB12010; Fostamatinib.
DR DrugBank; DB06101; IMC-1C11.
DR DrugBank; DB09078; Lenvatinib.
DR DrugBank; DB06080; Linifanib.
DR DrugBank; DB07288; N-(4-chlorophenyl)-2-[(pyridin-4-ylmethyl)amino]benzamide.
DR DrugBank; DB09079; Nintedanib.
DR DrugBank; DB05913; OSI-930.
DR DrugBank; DB06589; Pazopanib.
DR DrugBank; DB09221; Polaprezinc.
DR DrugBank; DB08896; Regorafenib.
DR DrugBank; DB15685; Selpercatinib.
DR DrugBank; DB00398; Sorafenib.
DR DrugBank; DB01268; Sunitinib.
DR DrugBank; DB05075; TG-100801.
DR DrugBank; DB11800; Tivozanib.
DR DrugBank; DB04879; Vatalanib.
DR DrugCentral; P17948; -.
DR GuidetoPHARMACOLOGY; 1812; -.
DR GlyConnect; 771; 5 N-Linked glycans (6 sites).
DR GlyGen; P17948; 13 sites, 8 N-linked glycans (6 sites).
DR iPTMnet; P17948; -.
DR PhosphoSitePlus; P17948; -.
DR BioMuta; FLT1; -.
DR DMDM; 143811474; -.
DR EPD; P17948; -.
DR jPOST; P17948; -.
DR MassIVE; P17948; -.
DR MaxQB; P17948; -.
DR PaxDb; P17948; -.
DR PeptideAtlas; P17948; -.
DR PRIDE; P17948; -.
DR ProteomicsDB; 3403; -.
DR ProteomicsDB; 53530; -. [P17948-1]
DR ProteomicsDB; 53531; -. [P17948-2]
DR ProteomicsDB; 53532; -. [P17948-3]
DR ProteomicsDB; 53533; -. [P17948-4]
DR ProteomicsDB; 53534; -. [P17948-5]
DR ProteomicsDB; 53535; -. [P17948-6]
DR ProteomicsDB; 53536; -. [P17948-7]
DR ABCD; P17948; 59 sequenced antibodies.
DR Antibodypedia; 1563; 1608 antibodies from 50 providers.
DR DNASU; 2321; -.
DR Ensembl; ENST00000282397.9; ENSP00000282397.4; ENSG00000102755.12. [P17948-1]
DR Ensembl; ENST00000539099.1; ENSP00000442630.1; ENSG00000102755.12. [P17948-4]
DR Ensembl; ENST00000541932.5; ENSP00000437631.1; ENSG00000102755.12. [P17948-3]
DR Ensembl; ENST00000543394.2; ENSP00000437841.1; ENSG00000102755.12. [P17948-8]
DR Ensembl; ENST00000615840.4; ENSP00000484039.1; ENSG00000102755.12. [P17948-2]
DR GeneID; 2321; -.
DR KEGG; hsa:2321; -.
DR MANE-Select; ENST00000282397.9; ENSP00000282397.4; NM_002019.4; NP_002010.2.
DR UCSC; uc001usb.4; human. [P17948-1]
DR CTD; 2321; -.
DR DisGeNET; 2321; -.
DR GeneCards; FLT1; -.
DR HGNC; HGNC:3763; FLT1.
DR HPA; ENSG00000102755; Tissue enriched (placenta).
DR MalaCards; FLT1; -.
DR MIM; 165070; gene.
DR neXtProt; NX_P17948; -.
DR OpenTargets; ENSG00000102755; -.
DR Orphanet; 275555; Preeclampsia.
DR PharmGKB; PA28180; -.
DR VEuPathDB; HostDB:ENSG00000102755; -.
DR eggNOG; KOG0200; Eukaryota.
DR GeneTree; ENSGT00940000158713; -.
DR HOGENOM; CLU_000288_49_4_1; -.
DR InParanoid; P17948; -.
DR OMA; TRNSGFT; -.
DR PhylomeDB; P17948; -.
DR TreeFam; TF325768; -.
DR BRENDA; 2.7.10.1; 2681.
DR PathwayCommons; P17948; -.
DR Reactome; R-HSA-194306; Neurophilin interactions with VEGF and VEGFR.
DR Reactome; R-HSA-195399; VEGF binds to VEGFR leading to receptor dimerization.
DR SignaLink; P17948; -.
DR SIGNOR; P17948; -.
DR BioGRID-ORCS; 2321; 10 hits in 1106 CRISPR screens.
DR ChiTaRS; FLT1; human.
DR EvolutionaryTrace; P17948; -.
DR GeneWiki; FLT1; -.
DR GenomeRNAi; 2321; -.
DR Pharos; P17948; Tclin.
DR PRO; PR:P17948; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; P17948; protein.
DR Bgee; ENSG00000102755; Expressed in pericardium and 200 other tissues.
DR ExpressionAtlas; P17948; baseline and differential.
DR Genevisible; P17948; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019838; F:growth factor binding; IPI:UniProtKB.
DR GO; GO:0036332; F:placental growth factor receptor activity; IDA:UniProtKB.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0005021; F:vascular endothelial growth factor receptor activity; IDA:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0048514; P:blood vessel morphogenesis; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IDA:UniProtKB.
DR GO; GO:0048598; P:embryonic morphogenesis; ISS:UniProtKB.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IBA:GO_Central.
DR GO; GO:1990384; P:hyaloid vascular plexus regression; ISS:UniProtKB.
DR GO; GO:0002548; P:monocyte chemotaxis; IDA:UniProtKB.
DR GO; GO:1905563; P:negative regulation of vascular endothelial cell proliferation; IGI:BHF-UCL.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:UniProtKB.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IMP:UniProtKB.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IMP:UniProtKB.
DR GO; GO:0010863; P:positive regulation of phospholipase C activity; IMP:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0036323; P:vascular endothelial growth factor receptor-1 signaling pathway; IDA:UniProtKB.
DR Gene3D; 2.60.40.10; -; 7.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
DR InterPro; IPR041348; VEGFR-2_TMD.
DR InterPro; IPR009135; VEGFR1_rcpt.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF17988; VEGFR-2_TMD; 1.
DR PRINTS; PR01833; VEGFRECEPTR1.
DR SMART; SM00409; IG; 7.
DR SMART; SM00408; IGc2; 5.
DR SMART; SM00406; IGv; 2.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 7.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50835; IG_LIKE; 6.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Angiogenesis; ATP-binding;
KW Cell membrane; Chemotaxis; Cytoplasm; Developmental protein;
KW Differentiation; Direct protein sequencing; Disulfide bond; Endosome;
KW Glycoprotein; Immunoglobulin domain; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Secreted; Signal;
KW Transferase; Transmembrane; Transmembrane helix; Tyrosine-protein kinase;
KW Ubl conjugation.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:8248162"
FT CHAIN 27..1338
FT /note="Vascular endothelial growth factor receptor 1"
FT /id="PRO_0000016768"
FT TOPO_DOM 27..758
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 759..780
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 781..1338
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..123
FT /note="Ig-like C2-type 1"
FT DOMAIN 151..214
FT /note="Ig-like C2-type 2"
FT DOMAIN 230..327
FT /note="Ig-like C2-type 3"
FT DOMAIN 335..421
FT /note="Ig-like C2-type 4"
FT DOMAIN 428..553
FT /note="Ig-like C2-type 5"
FT DOMAIN 556..654
FT /note="Ig-like C2-type 6"
FT DOMAIN 661..747
FT /note="Ig-like C2-type 7"
FT DOMAIN 827..1158
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 940..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1022
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 833..841
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 861
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 767..768
FT /note="Cleavage; by PSEN1"
FT /evidence="ECO:0000305"
FT MOD_RES 914
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000305|PubMed:9722576"
FT MOD_RES 1053
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 1169
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:9299537"
FT MOD_RES 1213
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:11513746,
FT ECO:0000269|PubMed:12796773, ECO:0000269|PubMed:9299537,
FT ECO:0000269|PubMed:9600074, ECO:0000269|PubMed:9722576"
FT MOD_RES 1242
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:9722576"
FT MOD_RES 1309
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:12796773"
FT MOD_RES 1327
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:12796773,
FT ECO:0000269|PubMed:9722576"
FT MOD_RES 1333
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:9722576"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 597
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 625
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 666
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 158..207
FT DISULFID 252..311
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 454..535
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 577..636
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 682..731
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..995
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:20512933"
FT /id="VSP_041983"
FT VAR_SEQ 1..875
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:20512933"
FT /id="VSP_041984"
FT VAR_SEQ 1..782
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:20512933"
FT /id="VSP_041985"
FT VAR_SEQ 1..7
FT /note="MVSYWDT -> MNSDLLV (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:20512933"
FT /id="VSP_047759"
FT VAR_SEQ 8..984
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:20512933"
FT /id="VSP_047760"
FT VAR_SEQ 518..541
FT /note="MASTLVVADSRISGIYICIASNKV -> LPPANSSFMLPPTSFSSNYFHFLP
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:18593464"
FT /id="VSP_041929"
FT VAR_SEQ 542..1338
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:18593464"
FT /id="VSP_041930"
FT VAR_SEQ 657..687
FT /note="DQEAPYLLRNLSDHTVAISSSTTLDCHANGV -> GEHCNKKAVFSRISKFK
FT STRNDCTTQSNVKH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8248162"
FT /id="VSP_002955"
FT VAR_SEQ 688..1338
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8248162"
FT /id="VSP_002956"
FT VAR_SEQ 706..733
FT /note="GIILGPGSSTLFIERVTEEDEGVYHCKA -> ELYTSTSPSSSSSSPLSSSS
FT SSSSSSSS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:18515749, ECO:0000303|Ref.7"
FT /id="VSP_041927"
FT VAR_SEQ 734..1338
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:18515749, ECO:0000303|Ref.7"
FT /id="VSP_041928"
FT VARIANT 60
FT /note="K -> T (in dbSNP:rs56409818)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042045"
FT VARIANT 128
FT /note="I -> L (in dbSNP:rs35073261)"
FT /id="VAR_049719"
FT VARIANT 144
FT /note="E -> K (in dbSNP:rs55974987)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042046"
FT VARIANT 281
FT /note="R -> Q (in dbSNP:rs55687105)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042047"
FT VARIANT 422
FT /note="L -> I (in a lung adenocarcinoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042048"
FT VARIANT 781
FT /note="R -> Q (in a glioma low grade oligodendroglioma
FT sample; somatic mutation; dbSNP:rs553261958)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042049"
FT VARIANT 938
FT /note="M -> V (in dbSNP:rs35549791)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042050"
FT VARIANT 982
FT /note="E -> A (in dbSNP:rs35832528)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042051"
FT VARIANT 1061
FT /note="L -> V (in a bladder transitional cell carcinoma
FT sample; somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042052"
FT MUTAGEN 767
FT /note="V->A: Abolishes proteolytic cleavage by PSEN1."
FT /evidence="ECO:0000269|PubMed:22016384"
FT MUTAGEN 861
FT /note="K->M: Abolishes enzyme activity. Abolishes
FT interaction with PLCG."
FT /evidence="ECO:0000269|PubMed:9299537"
FT MUTAGEN 914
FT /note="Y->F: Reduces phosphorylation at other tyrosine
FT residues."
FT /evidence="ECO:0000269|PubMed:9722576"
FT MUTAGEN 1050
FT /note="N->D: Strongly increases kinase activity. Increases
FT activity in promoting proliferation of endothelial cells."
FT /evidence="ECO:0000269|PubMed:16286478"
FT MUTAGEN 1169
FT /note="Y->F: Loss of phosphorylation site. Abolishes
FT interaction with PLCG."
FT /evidence="ECO:0000269|PubMed:9299537"
FT MUTAGEN 1213
FT /note="Y->F: Loss of phosphorylation site. Abolishes
FT interaction with PIK3R1."
FT /evidence="ECO:0000269|PubMed:9722576"
FT MUTAGEN 1242
FT /note="Y->F: Loss of phosphorylation site."
FT /evidence="ECO:0000269|PubMed:9722576"
FT MUTAGEN 1327
FT /note="Y->F: Loss of phosphorylation site."
FT /evidence="ECO:0000269|PubMed:9722576"
FT MUTAGEN 1333
FT /note="Y->F: Loss of phosphorylation site. Abolishes
FT interaction with CBL."
FT /evidence="ECO:0000269|PubMed:15001553,
FT ECO:0000269|PubMed:9722576"
FT CONFLICT 490
FT /note="F -> S (in Ref. 3; AAC16449)"
FT /evidence="ECO:0000305"
FT CONFLICT 779
FT /note="F -> L (in Ref. 1; CAA35946)"
FT /evidence="ECO:0000305"
FT CONFLICT 1029
FT /note="L -> F (in Ref. 6; ABI53803/ABI53804)"
FT /evidence="ECO:0000305"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:1QSV"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:1FLT"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:4CL7"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:1FLT"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:1QSZ"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:1FLT"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:5ABD"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:1QSV"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:1FLT"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:1FLT"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:1FLT"
FT STRAND 181..187
FT /evidence="ECO:0007829|PDB:1FLT"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:1FLT"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:1FLT"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:1FLT"
FT STRAND 203..211
FT /evidence="ECO:0007829|PDB:1FLT"
FT STRAND 214..224
FT /evidence="ECO:0007829|PDB:1FLT"
FT HELIX 806..809
FT /evidence="ECO:0007829|PDB:3HNG"
FT HELIX 817..820
FT /evidence="ECO:0007829|PDB:3HNG"
FT HELIX 824..826
FT /evidence="ECO:0007829|PDB:3HNG"
FT STRAND 827..835
FT /evidence="ECO:0007829|PDB:3HNG"
FT STRAND 837..848
FT /evidence="ECO:0007829|PDB:3HNG"
FT HELIX 849..851
FT /evidence="ECO:0007829|PDB:3HNG"
FT STRAND 854..863
FT /evidence="ECO:0007829|PDB:3HNG"
FT HELIX 869..883
FT /evidence="ECO:0007829|PDB:3HNG"
FT STRAND 894..898
FT /evidence="ECO:0007829|PDB:3HNG"
FT STRAND 906..910
FT /evidence="ECO:0007829|PDB:3HNG"
FT HELIX 917..922
FT /evidence="ECO:0007829|PDB:3HNG"
FT HELIX 996..1014
FT /evidence="ECO:0007829|PDB:3HNG"
FT TURN 1015..1017
FT /evidence="ECO:0007829|PDB:3HNG"
FT HELIX 1025..1027
FT /evidence="ECO:0007829|PDB:3HNG"
FT STRAND 1028..1030
FT /evidence="ECO:0007829|PDB:3HNG"
FT HELIX 1032..1034
FT /evidence="ECO:0007829|PDB:3HNG"
FT STRAND 1036..1038
FT /evidence="ECO:0007829|PDB:3HNG"
FT HELIX 1042..1044
FT /evidence="ECO:0007829|PDB:3HNG"
FT TURN 1047..1049
FT /evidence="ECO:0007829|PDB:3HNG"
FT STRAND 1053..1055
FT /evidence="ECO:0007829|PDB:3HNG"
FT HELIX 1063..1065
FT /evidence="ECO:0007829|PDB:3HNG"
FT HELIX 1068..1073
FT /evidence="ECO:0007829|PDB:3HNG"
FT HELIX 1078..1093
FT /evidence="ECO:0007829|PDB:3HNG"
FT HELIX 1107..1113
FT /evidence="ECO:0007829|PDB:3HNG"
FT TURN 1114..1116
FT /evidence="ECO:0007829|PDB:3HNG"
FT HELIX 1127..1136
FT /evidence="ECO:0007829|PDB:3HNG"
FT HELIX 1141..1143
FT /evidence="ECO:0007829|PDB:3HNG"
FT HELIX 1147..1157
FT /evidence="ECO:0007829|PDB:3HNG"
SQ 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
