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 27-MAR-2024, entry version 252. 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 (By similarity). May play an essential role CC as a negative regulator of embryonic angiogenesis by inhibiting CC excessive proliferation of endothelial cells. Can promote endothelial CC cell proliferation, survival and angiogenesis in adulthood. Its CC function in promoting cell proliferation seems to be cell-type CC specific. Promotes PGF-mediated proliferation of endothelial cells, CC proliferation of some types of cancer cells, but does not promote CC proliferation of normal fibroblasts (in vitro). Has very high affinity CC for VEGFA and relatively low protein kinase activity; may function as a CC negative regulator of VEGFA signaling by limiting the amount of free CC VEGFA and preventing its binding to KDR. Modulates KDR signaling by CC forming heterodimers with KDR. Ligand binding leads to the activation CC of several signaling cascades. Activation of PLCG leads to the CC production of the cellular signaling molecules diacylglycerol and CC inositol 1,4,5-trisphosphate and the activation of protein kinase C. CC Mediates phosphorylation of PIK3R1, the regulatory subunit of CC phosphatidylinositol 3-kinase, leading to activation of CC phosphatidylinositol kinase and the downstream signaling pathway. CC Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase CC 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:0000250|UniProtKB:P35969, CC ECO:0000269|PubMed:11141500, ECO:0000269|PubMed:11312102, CC ECO:0000269|PubMed:11811792, ECO:0000269|PubMed:12796773, CC ECO:0000269|PubMed:14633857, ECO:0000269|PubMed:15735759, CC ECO:0000269|PubMed:16685275, ECO:0000269|PubMed:18079407, CC ECO:0000269|PubMed:18515749, ECO:0000269|PubMed:18583712, CC ECO:0000269|PubMed:18593464, ECO:0000269|PubMed:20512933, CC ECO:0000269|PubMed:20551949, ECO:0000269|PubMed:21752276, CC ECO:0000269|PubMed:7824266, ECO:0000269|PubMed:8248162, CC ECO:0000269|PubMed:8605350, ECO:0000269|PubMed:9299537, CC 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; 193. DR DIP; DIP-643N; -. DR IntAct; P17948; 177. 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 GlyCosmos; P17948; 13 sites, 8 glycans. DR GlyGen; P17948; 14 sites, 8 N-linked glycans (6 sites), 1 O-linked glycan (1 site). DR iPTMnet; P17948; -. DR PhosphoSitePlus; P17948; -. DR BioMuta; FLT1; -. DR DMDM; 143811474; -. DR CPTAC; CPTAC-2819; -. DR CPTAC; CPTAC-3174; -. DR EPD; P17948; -. DR jPOST; P17948; -. DR MassIVE; P17948; -. DR MaxQB; P17948; -. DR PaxDb; 9606-ENSP00000282397; -. DR PeptideAtlas; 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; 1787 antibodies from 50 providers. DR DNASU; 2321; -. DR Ensembl; ENST00000282397.9; ENSP00000282397.4; ENSG00000102755.13. [P17948-1] DR Ensembl; ENST00000539099.2; ENSP00000442630.1; ENSG00000102755.13. [P17948-4] DR Ensembl; ENST00000541932.5; ENSP00000437631.1; ENSG00000102755.13. [P17948-3] DR Ensembl; ENST00000615840.5; ENSP00000484039.1; ENSG00000102755.13. [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 AGR; HGNC:3763; -. 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; CNENFPV; -. DR OrthoDB; 1614410at2759; -. 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 1192 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 202 other cell types or tissues. DR ExpressionAtlas; P17948; baseline and differential. 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: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; TAS:ProtInc. 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:0030154; P:cell differentiation; IEA:UniProtKB-KW. 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: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: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:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; 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 CDD; cd00096; Ig; 2. DR CDD; cd05862; IgI_VEGFR; 1. DR CDD; cd07702; IgI_VEGFR-1; 1. DR CDD; cd14207; PTKc_VEGFR1; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 7. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. 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 PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1. DR PANTHER; PTHR24416:SF390; VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 1; 1. DR Pfam; PF07679; I-set; 2. DR Pfam; PF00047; ig; 1. DR Pfam; PF13927; Ig_3; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR Pfam; PF21339; VEGFR-1-like_Ig-like; 1. DR Pfam; PF17988; VEGFR-2_TMD; 1. DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 1. DR PRINTS; PR01832; VEGFRECEPTOR. 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; Immunoglobulin; 7. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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. DR Genevisible; P17948; HS. 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 //