ID VEGFA_HUMAN Reviewed; 395 AA.
AC P15692; B5BU86; H0Y2S8; H0Y407; H0Y414; H0Y462; H0Y8N2; H3BLW7; O60720;
AC O75875; Q074Z4; Q16889; Q5UB46; Q6P0P5; Q96KJ0; Q96L82; Q96NW5; Q9H1W8;
AC Q9H1W9; Q9UH58; Q9UL23;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2023, sequence version 3.
DT 27-MAR-2024, entry version 268.
DE RecName: Full=Vascular endothelial growth factor A, long form;
DE Short=L-VEGF {ECO:0000303|PubMed:11731620, ECO:0000303|PubMed:35455969};
DE AltName: Full=Vascular permeability factor;
DE Short=VPF;
DE Contains:
DE RecName: Full=N-VEGF {ECO:0000303|PubMed:35455969};
DE Contains:
DE RecName: Full=VEGFA {ECO:0000303|PubMed:35455969};
DE Flags: Precursor;
GN Name=VEGFA; Synonyms=VEGF;
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] (ISOFORMS VEGF189 AND VEGF165).
RX PubMed=2479986; DOI=10.1126/science.2479986;
RA Leung D.W., Cachianes G., Kuang W.-J., Goeddel D.V., Ferrara N.;
RT "Vascular endothelial growth factor is a secreted angiogenic mitogen.";
RL Science 246:1306-1309(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF189), AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2479987; DOI=10.1126/science.2479987;
RA Keck P.J., Hauser S.D., Krivi G., Sanzo K., Warren T., Feder J.,
RA Connolly D.T.;
RT "Vascular permeability factor, an endothelial cell mitogen related to
RT PDGF.";
RL Science 246:1309-1312(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM VEGF189).
RX PubMed=1711045; DOI=10.1016/s0021-9258(18)99049-6;
RA Tischer E., Mitchell R., Hartman T., Silva M., Gospodarowicz D.,
RA Fiddes J.C., Abraham J.A.;
RT "The human gene for vascular endothelial growth factor. Multiple protein
RT forms are encoded through alternative exon splicing.";
RL J. Biol. Chem. 266:11947-11954(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM VEGF206).
RX PubMed=1791831; DOI=10.1210/mend-5-12-1806;
RA Houck K.A., Ferrara N., Winer J., Cachianes G., Li B., Leung D.W.;
RT "The vascular endothelial growth factor family: identification of a fourth
RT molecular species and characterization of alternative splicing of RNA.";
RL Mol. Endocrinol. 5:1806-1814(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165).
RX PubMed=1567395; DOI=10.1016/s0006-291x(05)80313-4;
RA Weindel K., Marme D., Weich H.A.;
RT "AIDS-associated Kaposi's sarcoma cells in culture express vascular
RT endothelial growth factor.";
RL Biochem. Biophys. Res. Commun. 183:1167-1174(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF145).
RX PubMed=9054410; DOI=10.1074/jbc.272.11.7151;
RA Poltorak Z., Cohen T., Sivan R., Kandelis Y., Spira G., Vlodavsky I.,
RA Keshet E., Neufeld G.;
RT "VEGF145, a secreted vascular endothelial growth factor isoform that binds
RT to extracellular matrix.";
RL J. Biol. Chem. 272:7151-7158(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF183).
RC TISSUE=Kidney;
RX PubMed=9878851; DOI=10.1016/s0167-4781(98)00240-1;
RA Lei J., Jiang A., Pei D.;
RT "Identification and characterization of a new splicing variant of vascular
RT endothelial growth factor: VEGF183.";
RL Biochim. Biophys. Acta 1443:400-406(1998).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM L-VEGF165).
RC TISSUE=Mammary gland;
RX PubMed=9450968; DOI=10.1091/mbc.9.2.469;
RA Claffey K.P., Shih S.-C., Mullen A., Dziennis S., Cusick J.L., Abrams K.R.,
RA Lee S.W., Detmar M.;
RT "Identification of a human VPF/VEGF 3' untranslated region mediating
RT hypoxia-induced mRNA stability.";
RL Mol. Biol. Cell 9:469-481(1998).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF148).
RC TISSUE=Renal glomerulus;
RX PubMed=10464055; DOI=10.1042/cs0970303;
RA Whittle C.J., Gillespie K.M., Harrison R., Mathieson P.W., Harper S.J.;
RT "Heterogeneous vascular endothelial growth factor (VEGF) isoform mRNA and
RT receptor mRNA expression in human glomeruli, and the identification of
RT VEGF148 mRNA, a novel truncated splice variant.";
RL Clin. Sci. 97:303-312(1999).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165B).
RC TISSUE=Kidney;
RX PubMed=12124351;
RA Bates D.O., Cui T.-G., Doughty J.M., Winkler M., Sugiono M., Shields J.D.,
RA Peat D., Gillatt D., Harper S.J.;
RT "VEGF165b, an inhibitory splice variant of vascular endothelial growth
RT factor, is down-regulated in renal cell carcinoma.";
RL Cancer Res. 62:4123-4131(2002).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165).
RC TISSUE=Hemangioendothelioma;
RA Murata H., Fukushima J., Hattori S., Okuda K., Yanagi H.;
RT "Human cDNA for the vascular endothelial growth factor isoform VEGF165.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF121).
RA Sato J.D., Whitney R.G.;
RT "Human cDNA for vascular endothelial growth factor isoform VEGF121.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165).
RA Liu J., Peng X., Yuan J., Qiang B.;
RT "Cloning of vascular endothelial growth factor (VEGF) cDNA.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165).
RC TISSUE=Heart;
RA Shan Z.X., Yu X.Y., Lin Q.X., Fu Y.H., Zheng M., Tan H.H., Lin S.G.;
RT "Cloning and identification of vascular endothelial growth factor isoform
RT VEGF165.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [15]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165).
RA Koul S., Johnson T., Meacham R.B., Koul H.K.;
RT "Cloning and characterization of VEGF from LNCaP cells, a line of prostate
RT cancer cells.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [16]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF111).
RA Mineur P.J., Colige A.C., Lambert C.A.;
RT "VEGF111, a new VEGF-A variant lacking exons 5, 6 and 7.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [17]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM VEGF165).
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [18]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [19]
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 [20]
RP PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM L-VEGF121).
RC TISSUE=Lung;
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 [21]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 203-395.
RG SeattleSNPs variation discovery resource;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [22]
RP PROTEIN SEQUENCE OF 207-221.
RX PubMed=7678805; DOI=10.1111/j.1432-1033.1993.tb19865.x;
RA Fiebich B.L., Jaeger B., Schoellmann C., Weindel K., Wilting J., Kochs G.,
RA Marme D., Hug H., Weich H.A.;
RT "Synthesis and assembly of functionally active human vascular endothelial
RT growth factor homodimers in insect cells.";
RL Eur. J. Biochem. 211:19-26(1993).
RN [23]
RP PROTEIN SEQUENCE OF 207-221.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [24]
RP PRELIMINARY PROTEIN SEQUENCE OF 207-216; 223-230 AND 239-261.
RX PubMed=2584205; DOI=10.1016/s0021-9258(19)47212-8;
RA Connolly D.T., Olander J.V., Heuvelman D., Nelson R., Monsell R.,
RA Siegel N., Haymore B.L., Leimgruber R., Feder J.;
RT "Human vascular permeability factor. Isolation from U937 cells.";
RL J. Biol. Chem. 264:20017-20024(1989).
RN [25]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 294-372 (ISOFORM VEGF183).
RC TISSUE=Retina;
RX PubMed=10067980;
RA Jingjing L., Xue Y., Agarwal N., Roque R.S.;
RT "Human Muller cells express VEGF183, a novel spliced variant of vascular
RT endothelial growth factor.";
RL Invest. Ophthalmol. Vis. Sci. 40:752-759(1999).
RN [26]
RP ALTERNATIVE SPLICING (ISOFORMS L-VEGF121 AND L-VEGF165), PROCESSING, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11563986; DOI=10.1042/0264-6021:3590219;
RA Tee M.K., Jaffe R.B.;
RT "A precursor form of vascular endothelial growth factor arises by
RT initiation from an upstream in-frame CUG codon.";
RL Biochem. J. 359:219-226(2001).
RN [27]
RP FUNCTION.
RX PubMed=11427521; DOI=10.1096/fj.00-0757fje;
RA Murphy J.F., Fitzgerald D.J.;
RT "Vascular endothelial growth factor induces cyclooxygenase-dependent
RT proliferation of endothelial cells via the VEGF-2 receptor.";
RL FASEB J. 15:1667-1669(2001).
RN [28]
RP ALTERNATIVE SPLICING (ISOFORM L-VEGF189), PROCESSING, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11731620; DOI=10.1210/mend.15.12.0738;
RA Huez I., Bornes S., Bresson D., Creancier L., Prats H.;
RT "New vascular endothelial growth factor isoform generated by internal
RT ribosome entry site-driven CUG translation initiation.";
RL Mol. Endocrinol. 15:2197-2210(2001).
RN [29]
RP INVOLVEMENT IN MVCD1.
RX PubMed=11978667; DOI=10.2337/diabetes.51.5.1635;
RA Awata T., Inoue K., Kurihara S., Ohkubo T., Watanabe M., Inukai K.,
RA Inoue I., Katayama S.;
RT "A common polymorphism in the 5'-untranslated region of the VEGF gene is
RT associated with diabetic retinopathy in type 2 diabetes.";
RL Diabetes 51:1635-1639(2002).
RN [30]
RP FUNCTION (ISOFORM VEGF165B).
RX PubMed=15520188; DOI=10.1158/0008-5472.can-04-0934;
RA Woolard J., Wang W.-Y., Bevan H.S., Qiu Y., Morbidelli L.,
RA Pritchard-Jones R.O., Cui T.-G., Sugiono M., Waine E., Perrin R.,
RA Foster R., Digby-Bell J., Shields J.D., Whittles C.E., Mushens R.E.,
RA Gillatt D.A., Ziche M., Harper S.J., Bates D.O.;
RT "VEGF165b, an inhibitory vascular endothelial growth factor splice variant:
RT mechanism of action, in vivo effect on angiogenesis and endogenous protein
RT expression.";
RL Cancer Res. 64:7822-7835(2004).
RN [31]
RP ALTERNATIVE SPLICING (ISOFORMS L-VEGF121; L-VEGF165 AND L-VEGF189).
RX PubMed=14764596; DOI=10.1074/jbc.m308410200;
RA Bornes S., Boulard M., Hieblot C., Zanibellato C., Iacovoni J.S., Prats H.,
RA Touriol C.;
RT "Control of the vascular endothelial growth factor internal ribosome entry
RT site (IRES) activity and translation initiation by alternatively spliced
RT coding sequences.";
RL J. Biol. Chem. 279:18717-18726(2004).
RN [32]
RP ALTERNATIVE SPLICING (ISOFORMS L-VEGF121 AND L-VEGF165), PROCESSING, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15896327; DOI=10.1016/j.bbrc.2005.04.123;
RA Rosenbaum-Dekel Y., Fuchs A., Yakirevich E., Azriel A., Mazareb S.,
RA Resnick M.B., Levi B.Z.;
RT "Nuclear localization of long-VEGF is associated with hypoxia and tumor
RT angiogenesis.";
RL Biochem. Biophys. Res. Commun. 332:271-278(2005).
RN [33]
RP FUNCTION IN CELL MIGRATION.
RX PubMed=16489009; DOI=10.1158/0008-5472.can-05-2217;
RA Dixelius J., Olsson A.K., Thulin A., Lee C., Johansson I.,
RA Claesson-Welsh L.;
RT "Minimal active domain and mechanism of action of the angiogenesis
RT inhibitor histidine-rich glycoprotein.";
RL Cancer Res. 66:2089-2097(2006).
RN [34]
RP FUNCTION.
RX PubMed=17446437; DOI=10.1161/01.res.0000267716.96196.60;
RA Glorioso N., Herrera V.L., Bagamasbad P., Filigheddu F., Troffa C.,
RA Argiolas G., Bulla E., Decano J.L., Ruiz-Opazo N.;
RT "Association of ATP1A1 and dear single-nucleotide polymorphism haplotypes
RT with essential hypertension: sex-specific and haplotype-specific effects.";
RL Circ. Res. 100:1522-1529(2007).
RN [35]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=22009797; DOI=10.1530/erc-11-0211;
RA Shan B., Gerez J., Haedo M., Fuertes M., Theodoropoulou M., Buchfelder M.,
RA Losa M., Stalla G.K., Arzt E., Renner U.;
RT "RSUME is implicated in HIF-1-induced VEGF-A production in pituitary tumour
RT cells.";
RL Endocr. Relat. Cancer 19:13-27(2012).
RN [36]
RP INTERACTION WITH NRP1.
RX PubMed=26503042; DOI=10.1038/nature15510;
RA He W., Bai G., Zhou H., Wei N., White N.M., Lauer J., Liu H., Shi Y.,
RA Dumitru C.D., Lettieri K., Shubayev V., Jordanova A., Guergueltcheva V.,
RA Griffin P.R., Burgess R.W., Pfaff S.L., Yang X.L.;
RT "CMT2D neuropathy is linked to the neomorphic binding activity of glycyl-
RT tRNA synthetase.";
RL Nature 526:710-714(2015).
RN [37]
RP ERRATUM OF PUBMED:26503042.
RX PubMed=26789244; DOI=10.1038/nature16499;
RA He W., Bai G., Zhou H., Wei N., White N.M., Lauer J., Liu H., Shi Y.,
RA Dan Dumitru C., Lettieri K., Shubayev V., Jordanova A., Guergueltcheva V.,
RA Griffin P.R., Burgess R.W., Pfaff S.L., Yang X.L.;
RT "Corrigendum: CMT2D neuropathy is linked to the neomorphic binding activity
RT of glycyl-tRNA synthetase.";
RL Nature 532:402-402(2016).
RN [38]
RP FUNCTION, AND INTERACTION WITH BSG.
RX PubMed=25825981; DOI=10.18632/oncotarget.2870;
RA Khayati F., Perez-Cano L., Maouche K., Sadoux A., Boutalbi Z.,
RA Podgorniak M.P., Maskos U., Setterblad N., Janin A., Calvo F., Lebbe C.,
RA Menashi S., Fernandez-Recio J., Mourah S.;
RT "EMMPRIN/CD147 is a novel coreceptor of VEGFR-2 mediating its activation by
RT VEGF.";
RL Oncotarget 6:9766-9780(2015).
RN [39]
RP FUNCTION (N-VEGF), AND SUBCELLULAR LOCATION (N-VEGF).
RX PubMed=35455969; DOI=10.3390/cells11081289;
RA Katsman M., Azriel A., Horev G., Reizel Y., Levi B.Z.;
RT "N-VEGF, the Autoregulatory Arm of VEGF-A.";
RL Cells 11:0-0(2022).
RN [40]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 214-315.
RX PubMed=9207067; DOI=10.1073/pnas.94.14.7192;
RA Muller Y.A., Li B., Christinger H.W., Wells J.A., Cunningham B.C.,
RA de Vos A.M.;
RT "Vascular endothelial growth factor: crystal structure and functional
RT mapping of the kinase domain receptor binding site.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:7192-7197(1997).
RN [41]
RP STRUCTURE BY NMR OF 214-315.
RX PubMed=9336848; DOI=10.1002/pro.5560061020;
RA Fairbrother W.J., Champe M.A., Christinger H.W., Keyt B.A.,
RA Starovasnik M.A.;
RT "1H, 13C, and 15N backbone assignment and secondary structure of the
RT receptor-binding domain of vascular endothelial growth factor.";
RL Protein Sci. 6:2250-2260(1997).
RN [42]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 214-315.
RX PubMed=9351807; DOI=10.1016/s0969-2126(97)00284-0;
RA Muller Y.A., Christinger H.W., Keyt B.A., de Vos A.M.;
RT "The crystal structure of vascular endothelial growth factor (VEGF) refined
RT to 1.93-A resolution: multiple copy flexibility and receptor binding.";
RL Structure 5:1325-1338(1997).
RN [43]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 219-314.
RX PubMed=9922142; DOI=10.1021/bi9819327;
RA Wiesmann C., Christinger H.W., Cochran A.G., Cunningham B.C.,
RA Fairbrother W.J., Keenan C.J., Meng G., de Vos A.M.;
RT "Crystal structure of the complex between VEGF and a receptor-blocking
RT peptide.";
RL Biochemistry 37:17765-17772(1998).
RN [44]
RP STRUCTURE BY NMR OF 317-378.
RX PubMed=9634701; DOI=10.1016/s0969-2126(98)00065-3;
RA Fairbrother W.J., Champe M.A., Christinger H.W., Keyt B.A.,
RA Starovasnik M.A.;
RT "Solution structure of the heparin-binding domain of vascular endothelial
RT growth factor.";
RL Structure 6:637-648(1998).
CC -!- FUNCTION: [N-VEGF]: Participates in the induction of key genes involved
CC in the response to hypoxia and in the induction of angiogenesis such as
CC HIF1A (PubMed:35455969). Involved in protecting cells from hypoxia-
CC mediated cell death (By similarity). {ECO:0000250|UniProtKB:Q00731,
CC ECO:0000269|PubMed:35455969}.
CC -!- FUNCTION: [VEGFA]: Growth factor active in angiogenesis, vasculogenesis
CC and endothelial cell growth. Induces endothelial cell proliferation,
CC promotes cell migration, inhibits apoptosis and induces
CC permeabilization of blood vessels. Binds to the FLT1/VEGFR1 and
CC KDR/VEGFR2 receptors, heparan sulfate and heparin. Binds to the
CC NRP1/neuropilin-1 receptor. Binding to NRP1 initiates a signaling
CC pathway needed for motor neuron axon guidance and cell body migration,
CC including for the caudal migration of facial motor neurons from
CC rhombomere 4 to rhombomere 6 during embryonic development (By
CC similarity). Also binds the DEAR/FBXW7-AS1 receptor (PubMed:17446437).
CC {ECO:0000250|UniProtKB:Q00731, ECO:0000269|PubMed:11427521,
CC ECO:0000269|PubMed:16489009, ECO:0000269|PubMed:17446437,
CC ECO:0000269|PubMed:25825981}.
CC -!- FUNCTION: [Isoform VEGF165B]: Binds to the KDR receptor but does not
CC activate downstream signaling pathways, does not activate angiogenesis
CC and inhibits tumor growth. {ECO:0000269|PubMed:15520188}.
CC -!- SUBUNIT: [VEGFA]: Homodimer; disulfide-linked (By similarity). Also
CC found as heterodimer with PGF (By similarity). Interacts with NRP1
CC (PubMed:26503042). Interacts with isoform 2 of BSG (PubMed:25825981).
CC {ECO:0000250|UniProtKB:P16612, ECO:0000269|PubMed:25825981,
CC ECO:0000269|PubMed:26503042}.
CC -!- INTERACTION:
CC P15692; P17948: FLT1; NbExp=4; IntAct=EBI-1026643, EBI-1026718;
CC P15692; P35968: KDR; NbExp=5; IntAct=EBI-1026643, EBI-1005487;
CC P15692; O14786: NRP1; NbExp=4; IntAct=EBI-1026643, EBI-1187100;
CC P15692; P15692: VEGFA; NbExp=10; IntAct=EBI-1026643, EBI-1026643;
CC P15692-4; P17948: FLT1; NbExp=3; IntAct=EBI-1026691, EBI-1026718;
CC P15692-4; P35968: KDR; NbExp=8; IntAct=EBI-1026691, EBI-1005487;
CC P15692-4; O14786-2: NRP1; NbExp=4; IntAct=EBI-1026691, EBI-6285281;
CC P15692-4; P15692-4: VEGFA; NbExp=5; IntAct=EBI-1026691, EBI-1026691;
CC P15692-12; P08034: GJB1; NbExp=3; IntAct=EBI-6622053, EBI-17565645;
CC P15692-12; P80188: LCN2; NbExp=3; IntAct=EBI-6622053, EBI-11911016;
CC P15692-12; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-6622053, EBI-17295964;
CC P15692-12; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-6622053, EBI-10982110;
CC -!- SUBCELLULAR LOCATION: [N-VEGF]: Cytoplasm
CC {ECO:0000269|PubMed:15896327}. Nucleus {ECO:0000269|PubMed:15896327,
CC ECO:0000269|PubMed:35455969}. Note=Cytoplasmic in normoxic conditions
CC and localizes to the nucleus under hypoxic conditions.
CC {ECO:0000269|PubMed:15896327, ECO:0000269|PubMed:35455969}.
CC -!- SUBCELLULAR LOCATION: [VEGFA]: Secreted {ECO:0000269|PubMed:11563986,
CC ECO:0000269|PubMed:11731620, ECO:0000269|PubMed:15896327}.
CC -!- SUBCELLULAR LOCATION: [Isoform L-VEGF189]: Endoplasmic reticulum
CC {ECO:0000269|PubMed:11731620}. Golgi apparatus
CC {ECO:0000269|PubMed:11731620}. Secreted, extracellular space,
CC extracellular matrix {ECO:0000269|PubMed:11563986}.
CC -!- SUBCELLULAR LOCATION: [Isoform VEGF121]: Secreted
CC {ECO:0000269|PubMed:15896327}.
CC -!- SUBCELLULAR LOCATION: [Isoform VEGF165]: Secreted
CC {ECO:0000269|PubMed:15896327}.
CC -!- SUBCELLULAR LOCATION: [Isoform VEGF189]: Secreted. Note=Cell-associated
CC after secretion and is bound avidly by heparin and the extracellular
CC matrix, although it may be released as a soluble form by heparin,
CC heparinase or plasmin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing, Alternative initiation; Named isoforms=17;
CC Comment=A subset of isoforms are produced by use of an alternative
CC upstream CUG codon, giving rise to long isoforms which have an
CC N-terminal extension compared to the classical shorter AUG-initiated
CC forms. These longer forms are post-translationally processed to
CC produce an N-terminal N-VEGF chain and a C-terminal VEGFA chain.;
CC Name=L-VEGF189;
CC IsoId=P15692-13; Sequence=Displayed;
CC Name=VEGF206;
CC IsoId=P15692-1; Sequence=VSP_061891, VSP_061898;
CC Name=VEGF189;
CC IsoId=P15692-2; Sequence=VSP_061891;
CC Name=VEGF183;
CC IsoId=P15692-3; Sequence=VSP_061891, VSP_061897;
CC Name=VEGF165; Synonyms=VEGF;
CC IsoId=P15692-4; Sequence=VSP_061891, VSP_061894;
CC Name=VEGF148;
CC IsoId=P15692-5; Sequence=VSP_061891, VSP_061894, VSP_061901,
CC VSP_061902;
CC Name=VEGF145;
CC IsoId=P15692-6; Sequence=VSP_061891, VSP_061899, VSP_061900;
CC Name=VEGF165B;
CC IsoId=P15692-8; Sequence=VSP_061891, VSP_061894, VSP_061903;
CC Name=VEGF121;
CC IsoId=P15692-9; Sequence=VSP_061891, VSP_061895, VSP_061896;
CC Name=VEGF111;
CC IsoId=P15692-10; Sequence=VSP_061891, VSP_061892, VSP_061893;
CC Name=L-VEGF165;
CC IsoId=P15692-11; Sequence=VSP_061894;
CC Name=L-VEGF121;
CC IsoId=P15692-12; Sequence=VSP_061895, VSP_061896;
CC Name=L-VEGF206;
CC IsoId=P15692-14; Sequence=VSP_061898;
CC Name=15;
CC IsoId=P15692-15; Sequence=VSP_061894, VSP_061903;
CC Name=16;
CC IsoId=P15692-16; Sequence=VSP_061897;
CC Name=17;
CC IsoId=P15692-17; Sequence=VSP_061894, VSP_061901, VSP_061902;
CC Name=18;
CC IsoId=P15692-18; Sequence=VSP_061892, VSP_061893;
CC -!- TISSUE SPECIFICITY: Higher expression in pituitary tumors than the
CC pituitary gland. {ECO:0000269|PubMed:22009797}.
CC -!- TISSUE SPECIFICITY: [Isoform VEGF189]: Widely expressed.
CC -!- TISSUE SPECIFICITY: [Isoform VEGF165]: Widely expressed.
CC -!- TISSUE SPECIFICITY: [Isoform VEGF121]: Widely expressed.
CC -!- TISSUE SPECIFICITY: [Isoform VEGF206]: Not widely expressed.
CC -!- TISSUE SPECIFICITY: [Isoform VEGF145]: Not widely expressed.
CC -!- INDUCTION: By hypoxia. Regulated by growth factors, cytokines,
CC gonadotropins, nitric oxide, hypoglycemia and oncogenic mutations.
CC {ECO:0000269|PubMed:22009797}.
CC -!- PTM: [Vascular endothelial growth factor A, long form]: Produced by use
CC of an alternative upstream CUG codon and post-translationally processed
CC into the N-terminal N-VEGF form and the C-terminal secreted VEGFA form.
CC {ECO:0000269|PubMed:11731620}.
CC -!- DISEASE: Microvascular complications of diabetes 1 (MVCD1)
CC [MIM:603933]: Pathological conditions that develop in numerous tissues
CC and organs as a consequence of diabetes mellitus. They include diabetic
CC retinopathy, diabetic nephropathy leading to end-stage renal disease,
CC and diabetic neuropathy. Diabetic retinopathy remains the major cause
CC of new-onset blindness among diabetic adults. It is characterized by
CC vascular permeability and increased tissue ischemia and angiogenesis.
CC {ECO:0000269|PubMed:11978667}. Note=Disease susceptibility is
CC associated with variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform L-VEGF189]: Produced by alternative promoter
CC usage and alternative initiation. Starts at an alternative upstream CUG
CC codon.
CC -!- MISCELLANEOUS: [Isoform L-VEGF165]: Produced by alternative promoter
CC usage and alternative initiation. Starts at an alternative upstream CUG
CC codon.
CC -!- MISCELLANEOUS: [Isoform L-VEGF121]: Produced by alternative promoter
CC usage and alternative initiation. Starts at an alternative upstream CUG
CC codon.
CC -!- MISCELLANEOUS: [Isoform L-VEGF206]: Produced by alternative promoter
CC usage and alternative initiation. Starts at an alternative upstream CUG
CC codon. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 15]: Starts at an alternative upstream CUG
CC codon. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 16]: Starts at an alternative upstream CUG
CC codon. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 17]: Starts at an alternative upstream CUG
CC codon. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 18]: Starts at an alternative upstream CUG
CC codon. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC63102.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAC63143.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=VEGF entry;
CC URL="https://en.wikipedia.org/wiki/Vascular_endothelial_growth_factor";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/vegf/";
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DR EMBL; M32977; AAA35789.1; -; mRNA.
DR EMBL; M27281; AAA36807.1; -; mRNA.
DR EMBL; M63978; AAA36804.1; -; Genomic_DNA.
DR EMBL; M63971; AAA36804.1; JOINED; Genomic_DNA.
DR EMBL; M63972; AAA36804.1; JOINED; Genomic_DNA.
DR EMBL; M63973; AAA36804.1; JOINED; Genomic_DNA.
DR EMBL; M63974; AAA36804.1; JOINED; Genomic_DNA.
DR EMBL; M63975; AAA36804.1; JOINED; Genomic_DNA.
DR EMBL; M63976; AAA36804.1; JOINED; Genomic_DNA.
DR EMBL; M63977; AAA36804.1; JOINED; Genomic_DNA.
DR EMBL; S85192; AAC63102.1; ALT_INIT; mRNA.
DR EMBL; AH006909; AAC63101.1; -; Genomic_DNA.
DR EMBL; X62568; CAA44447.1; -; mRNA.
DR EMBL; AJ010438; CAA09179.1; -; mRNA.
DR EMBL; AF022375; AAC63143.1; ALT_SEQ; mRNA.
DR EMBL; AF091352; AAD55345.1; -; mRNA.
DR EMBL; AF430806; AAL27435.1; -; mRNA.
DR EMBL; AB021221; BAA78418.1; -; mRNA.
DR EMBL; AF214570; AAF19659.1; -; mRNA.
DR EMBL; AY047581; AAK95847.1; -; mRNA.
DR EMBL; AF486837; AAM03108.1; -; mRNA.
DR EMBL; AY766116; AAV34601.1; -; mRNA.
DR EMBL; DQ229900; ABB58912.1; -; mRNA.
DR EMBL; AB451322; BAG70136.1; -; mRNA.
DR EMBL; AB451451; BAG70265.1; -; mRNA.
DR EMBL; AL136131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX04229.1; -; Genomic_DNA.
DR EMBL; BC065522; AAH65522.2; -; mRNA.
DR EMBL; AF437895; AAL27630.1; -; Genomic_DNA.
DR EMBL; AF062645; AAC16730.1; -; mRNA.
DR CCDS; CCDS34457.1; -. [P15692-14]
DR CCDS; CCDS34458.1; -. [P15692-11]
DR CCDS; CCDS47432.1; -. [P15692-15]
DR CCDS; CCDS47433.1; -. [P15692-16]
DR CCDS; CCDS47434.1; -. [P15692-12]
DR CCDS; CCDS47435.1; -. [P15692-17]
DR CCDS; CCDS4907.2; -. [P15692-13]
DR CCDS; CCDS55007.1; -. [P15692-18]
DR CCDS; CCDS55008.1; -. [P15692-3]
DR CCDS; CCDS55009.1; -. [P15692-2]
DR CCDS; CCDS55010.1; -. [P15692-1]
DR CCDS; CCDS55011.1; -. [P15692-5]
DR CCDS; CCDS55012.1; -. [P15692-4]
DR CCDS; CCDS55013.1; -. [P15692-8]
DR CCDS; CCDS55014.1; -. [P15692-9]
DR CCDS; CCDS55015.1; -. [P15692-10]
DR PIR; A41551; A41551.
DR RefSeq; NP_001020537.2; NM_001025366.2. [P15692-14]
DR RefSeq; NP_001020538.2; NM_001025367.2. [P15692-16]
DR RefSeq; NP_001020539.2; NM_001025368.2. [P15692-11]
DR RefSeq; NP_001020540.2; NM_001025369.2. [P15692-17]
DR RefSeq; NP_001020541.2; NM_001025370.2. [P15692-12]
DR RefSeq; NP_001028928.1; NM_001033756.2. [P15692-15]
DR RefSeq; NP_001165093.1; NM_001171622.1. [P15692-18]
DR RefSeq; NP_001165094.1; NM_001171623.1. [P15692-1]
DR RefSeq; NP_001165095.1; NM_001171624.1. [P15692-2]
DR RefSeq; NP_001165096.1; NM_001171625.1. [P15692-3]
DR RefSeq; NP_001165097.1; NM_001171626.1. [P15692-4]
DR RefSeq; NP_001165098.1; NM_001171627.1. [P15692-5]
DR RefSeq; NP_001165099.1; NM_001171628.1. [P15692-9]
DR RefSeq; NP_001165100.1; NM_001171629.1. [P15692-8]
DR RefSeq; NP_001165101.1; NM_001171630.1. [P15692-10]
DR RefSeq; NP_001191313.1; NM_001204384.1. [P15692-6]
DR RefSeq; NP_001191314.1; NM_001204385.1.
DR RefSeq; NP_001273973.1; NM_001287044.1.
DR RefSeq; NP_001303939.1; NM_001317010.1.
DR RefSeq; NP_003367.4; NM_003376.5. [P15692-13]
DR PDB; 1BJ1; X-ray; 2.40 A; V/W=214-315.
DR PDB; 1CZ8; X-ray; 2.40 A; V/W=220-313.
DR PDB; 1FLT; X-ray; 1.70 A; V/W=218-315.
DR PDB; 1KAT; NMR; -; V/W=217-315.
DR PDB; 1KMX; NMR; -; A=346-395.
DR PDB; 1MJV; X-ray; 2.10 A; A/B=220-314.
DR PDB; 1MKG; X-ray; 2.50 A; A/B/C/D=220-314.
DR PDB; 1MKK; X-ray; 1.32 A; A/B=220-314.
DR PDB; 1QTY; X-ray; 2.70 A; R/S/V/W=214-315.
DR PDB; 1TZH; X-ray; 2.60 A; V/W=214-315.
DR PDB; 1TZI; X-ray; 2.80 A; V=214-315.
DR PDB; 1VGH; NMR; -; A=183-395.
DR PDB; 1VPF; X-ray; 2.50 A; A/B/C/D=214-315.
DR PDB; 1VPP; X-ray; 1.90 A; V/W=214-315.
DR PDB; 2FJG; X-ray; 2.80 A; V/W=214-315.
DR PDB; 2FJH; X-ray; 3.10 A; V/W=214-315.
DR PDB; 2QR0; X-ray; 3.50 A; C/D/I/J/O/P/U/V=219-315.
DR PDB; 2VGH; NMR; -; A=183-395.
DR PDB; 2VPF; X-ray; 1.93 A; A/B/C/D/E/F/G/H=214-315.
DR PDB; 3BDY; X-ray; 2.60 A; V=214-315.
DR PDB; 3P9W; X-ray; 2.41 A; A/C/E/G=215-318.
DR PDB; 3QTK; X-ray; 1.85 A; A/B/C/D/E/F=214-315.
DR PDB; 3S1B; X-ray; 2.90 A; V=218-313.
DR PDB; 3S1K; X-ray; 2.55 A; V/W=214-315.
DR PDB; 3V2A; X-ray; 3.20 A; A=207-320.
DR PDB; 4DEQ; X-ray; 2.65 A; A/B=346-395.
DR PDB; 4GLN; X-ray; 1.60 A; E/F=214-315.
DR PDB; 4GLS; X-ray; 1.60 A; E/F=214-315.
DR PDB; 4KZN; X-ray; 1.71 A; A=219-315.
DR PDB; 4QAF; X-ray; 1.80 A; C/D=214-315.
DR PDB; 4WPB; X-ray; 3.11 A; A/B=214-315.
DR PDB; 4ZFF; X-ray; 2.75 A; C/D=217-315.
DR PDB; 5DN2; X-ray; 1.95 A; E/F/G=368-395.
DR PDB; 5FV1; X-ray; 2.70 A; V/W=207-316.
DR PDB; 5FV2; X-ray; 3.45 A; V/W/X=207-316.
DR PDB; 5HHC; X-ray; 2.10 A; A/B=214-315.
DR PDB; 5HHD; X-ray; 2.10 A; A/B=214-315.
DR PDB; 5O4E; X-ray; 2.15 A; E/F=219-314.
DR PDB; 5T89; X-ray; 4.00 A; V/W=207-335.
DR PDB; 6BFT; X-ray; 2.55 A; C/G=216-315.
DR PDB; 6D3O; X-ray; 3.10 A; A/B=214-315.
DR PDB; 6T9D; X-ray; 2.90 A; CCC/DDD=207-321.
DR PDB; 6V7K; X-ray; 2.50 A; A/B=214-315.
DR PDB; 6Z13; X-ray; 1.80 A; V/W=219-313.
DR PDB; 6Z3F; X-ray; 2.10 A; V/W=219-313.
DR PDB; 6ZBR; X-ray; 1.60 A; V/W=219-313.
DR PDB; 6ZCD; X-ray; 1.80 A; V/W=219-313.
DR PDB; 6ZFL; X-ray; 1.60 A; V/W=219-313.
DR PDB; 7KEZ; X-ray; 2.31 A; V=207-316.
DR PDB; 7KF0; X-ray; 2.32 A; C/V=207-316.
DR PDB; 7KF1; X-ray; 2.45 A; C/F/J/V=207-316.
DR PDB; 7LL8; X-ray; 2.31 A; A/B=214-315.
DR PDB; 7LL9; X-ray; 2.90 A; A/B/E/F=214-315.
DR PDBsum; 1BJ1; -.
DR PDBsum; 1CZ8; -.
DR PDBsum; 1FLT; -.
DR PDBsum; 1KAT; -.
DR PDBsum; 1KMX; -.
DR PDBsum; 1MJV; -.
DR PDBsum; 1MKG; -.
DR PDBsum; 1MKK; -.
DR PDBsum; 1QTY; -.
DR PDBsum; 1TZH; -.
DR PDBsum; 1TZI; -.
DR PDBsum; 1VGH; -.
DR PDBsum; 1VPF; -.
DR PDBsum; 1VPP; -.
DR PDBsum; 2FJG; -.
DR PDBsum; 2FJH; -.
DR PDBsum; 2QR0; -.
DR PDBsum; 2VGH; -.
DR PDBsum; 2VPF; -.
DR PDBsum; 3BDY; -.
DR PDBsum; 3P9W; -.
DR PDBsum; 3QTK; -.
DR PDBsum; 3S1B; -.
DR PDBsum; 3S1K; -.
DR PDBsum; 3V2A; -.
DR PDBsum; 4DEQ; -.
DR PDBsum; 4GLN; -.
DR PDBsum; 4GLS; -.
DR PDBsum; 4KZN; -.
DR PDBsum; 4QAF; -.
DR PDBsum; 4WPB; -.
DR PDBsum; 4ZFF; -.
DR PDBsum; 5DN2; -.
DR PDBsum; 5FV1; -.
DR PDBsum; 5FV2; -.
DR PDBsum; 5HHC; -.
DR PDBsum; 5HHD; -.
DR PDBsum; 5O4E; -.
DR PDBsum; 5T89; -.
DR PDBsum; 6BFT; -.
DR PDBsum; 6D3O; -.
DR PDBsum; 6T9D; -.
DR PDBsum; 6V7K; -.
DR PDBsum; 6Z13; -.
DR PDBsum; 6Z3F; -.
DR PDBsum; 6ZBR; -.
DR PDBsum; 6ZCD; -.
DR PDBsum; 6ZFL; -.
DR PDBsum; 7KEZ; -.
DR PDBsum; 7KF0; -.
DR PDBsum; 7KF1; -.
DR PDBsum; 7LL8; -.
DR PDBsum; 7LL9; -.
DR AlphaFoldDB; P15692; -.
DR BMRB; P15692; -.
DR SMR; P15692; -.
DR BioGRID; 113265; 64.
DR ComplexPortal; CPX-1977; Vascular endothelial growth factor A complex.
DR CORUM; P15692; -.
DR DIP; DIP-5740N; -.
DR IntAct; P15692; 25.
DR MINT; P15692; -.
DR BindingDB; P15692; -.
DR ChEMBL; CHEMBL1783; -.
DR DrugBank; DB05434; ABT-510.
DR DrugBank; DB08885; Aflibercept.
DR DrugBank; DB00112; Bevacizumab.
DR DrugBank; DB06642; Bevasiranib.
DR DrugBank; DB14864; Brolucizumab.
DR DrugBank; DB01136; Carvedilol.
DR DrugBank; DB09301; Chondroitin sulfate.
DR DrugBank; DB06779; Dalteparin.
DR DrugBank; DB05932; Denibulin.
DR DrugBank; DB15303; Faricimab.
DR DrugBank; DB10772; Foreskin keratinocyte (neonatal).
DR DrugBank; DB01120; Gliclazide.
DR DrugBank; DB01017; Minocycline.
DR DrugBank; DB04895; Pegaptanib.
DR DrugBank; DB03088; Pidolic acid.
DR DrugBank; DB01270; Ranibizumab.
DR DrugBank; DB05969; SNS-032.
DR DrugBank; DB05294; Vandetanib.
DR DrugBank; DB12317; Vanucizumab.
DR DrugBank; DB05890; Veglin.
DR DrugCentral; P15692; -.
DR MoonDB; P15692; Predicted.
DR GlyCosmos; P15692; 1 site, No reported glycans.
DR GlyGen; P15692; 1 site.
DR iPTMnet; P15692; -.
DR PhosphoSitePlus; P15692; -.
DR BioMuta; VEGFA; -.
DR DMDM; 17380528; -.
DR jPOST; P15692; -.
DR MassIVE; P15692; -.
DR PaxDb; 9606-ENSP00000478570; -.
DR PeptideAtlas; P15692; -.
DR ProteomicsDB; 34350; -.
DR ProteomicsDB; 34645; -.
DR ProteomicsDB; 34652; -.
DR ProteomicsDB; 34682; -.
DR ProteomicsDB; 35749; -.
DR ProteomicsDB; 40743; -.
DR ProteomicsDB; 53195; -. [P15692-1]
DR ProteomicsDB; 53196; -. [P15692-10]
DR ProteomicsDB; 53197; -. [P15692-11]
DR ProteomicsDB; 53198; -. [P15692-12]
DR ProteomicsDB; 53199; -. [P15692-13]
DR ProteomicsDB; 53200; -. [P15692-14]
DR ProteomicsDB; 53201; -. [P15692-2]
DR ProteomicsDB; 53202; -. [P15692-3]
DR ProteomicsDB; 53203; -. [P15692-4]
DR ProteomicsDB; 53204; -. [P15692-5]
DR ProteomicsDB; 53205; -. [P15692-6]
DR ProteomicsDB; 53206; -. [P15692-8]
DR ProteomicsDB; 53207; -. [P15692-9]
DR ABCD; P15692; 25 sequenced antibodies.
DR Antibodypedia; 3956; 3195 antibodies from 56 providers.
DR CPTC; P15692; 1 antibody.
DR DNASU; 7422; -.
DR Ensembl; ENST00000324450.11; ENSP00000317598.7; ENSG00000112715.26. [P15692-18]
DR Ensembl; ENST00000372055.9; ENSP00000361125.5; ENSG00000112715.26. [P15692-14]
DR Ensembl; ENST00000372064.9; ENSP00000361134.5; ENSG00000112715.26. [P15692-12]
DR Ensembl; ENST00000372067.8; ENSP00000361137.4; ENSG00000112715.26. [P15692-11]
DR Ensembl; ENST00000372077.8; ENSP00000361148.4; ENSG00000112715.26. [P15692-9]
DR Ensembl; ENST00000413642.8; ENSP00000389864.4; ENSG00000112715.26. [P15692-16]
DR Ensembl; ENST00000417285.7; ENSP00000388663.3; ENSG00000112715.26. [P15692-17]
DR Ensembl; ENST00000457104.6; ENSP00000409911.2; ENSG00000112715.26. [P15692-10]
DR Ensembl; ENST00000482630.7; ENSP00000421561.2; ENSG00000112715.26. [P15692-15]
DR Ensembl; ENST00000518689.5; ENSP00000430829.1; ENSG00000112715.26. [P15692-3]
DR Ensembl; ENST00000518824.5; ENSP00000430002.1; ENSG00000112715.26. [P15692-8]
DR Ensembl; ENST00000520948.5; ENSP00000428321.1; ENSG00000112715.26. [P15692-2]
DR Ensembl; ENST00000523125.5; ENSP00000429008.1; ENSG00000112715.26. [P15692-5]
DR Ensembl; ENST00000523873.5; ENSP00000430479.1; ENSG00000112715.26. [P15692-1]
DR Ensembl; ENST00000523950.5; ENSP00000429643.1; ENSG00000112715.26. [P15692-4]
DR Ensembl; ENST00000672860.3; ENSP00000500082.3; ENSG00000112715.26. [P15692-13]
DR GeneID; 7422; -.
DR KEGG; hsa:7422; -.
DR MANE-Select; ENST00000672860.3; ENSP00000500082.3; NM_003376.6; NP_003367.4.
DR UCSC; uc003owd.5; human. [P15692-13]
DR AGR; HGNC:12680; -.
DR CTD; 7422; -.
DR DisGeNET; 7422; -.
DR GeneCards; VEGFA; -.
DR HGNC; HGNC:12680; VEGFA.
DR HPA; ENSG00000112715; Low tissue specificity.
DR MalaCards; VEGFA; -.
DR MIM; 192240; gene.
DR MIM; 603933; phenotype.
DR neXtProt; NX_P15692; -.
DR OpenTargets; ENSG00000112715; -.
DR PharmGKB; PA37302; -.
DR VEuPathDB; HostDB:ENSG00000112715; -.
DR eggNOG; ENOG502QVI8; Eukaryota.
DR GeneTree; ENSGT00940000157284; -.
DR HOGENOM; CLU_042996_3_0_1; -.
DR InParanoid; P15692; -.
DR OMA; NFHCEPC; -.
DR OrthoDB; 4231319at2759; -.
DR PhylomeDB; P15692; -.
DR PathwayCommons; P15692; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-1234158; Regulation of gene expression by Hypoxia-inducible Factor.
DR Reactome; R-HSA-194138; Signaling by VEGF.
DR Reactome; R-HSA-194313; VEGF ligand-receptor interactions.
DR Reactome; R-HSA-195399; VEGF binds to VEGFR leading to receptor dimerization.
DR Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway. [P15692-4]
DR Reactome; R-HSA-5218921; VEGFR2 mediated cell proliferation. [P15692-4]
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-HSA-8866910; TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS. [P15692-4]
DR SignaLink; P15692; -.
DR SIGNOR; P15692; -.
DR BioGRID-ORCS; 7422; 14 hits in 1166 CRISPR screens.
DR ChiTaRS; VEGFA; human.
DR EvolutionaryTrace; P15692; -.
DR GeneWiki; Vascular_endothelial_growth_factor_A; -.
DR GenomeRNAi; 7422; -.
DR Pharos; P15692; Tclin.
DR PRO; PR:P15692; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P15692; Protein.
DR Bgee; ENSG00000112715; Expressed in right lobe of thyroid gland and 203 other cell types or tissues.
DR ExpressionAtlas; P15692; baseline and differential.
DR Genevisible; P15692; HS.
DR GO; GO:0005912; C:adherens junction; IDA:ARUK-UCL.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0031012; C:extracellular matrix; NAS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR GO; GO:0030141; C:secretory granule; IDA:UniProtKB.
DR GO; GO:1990150; C:VEGF-A complex; IPI:ComplexPortal.
DR GO; GO:0042056; F:chemoattractant activity; IDA:UniProtKB.
DR GO; GO:0005125; F:cytokine activity; IDA:BHF-UCL.
DR GO; GO:0050840; F:extracellular matrix binding; IC:BHF-UCL.
DR GO; GO:0001968; F:fibronectin binding; IDA:BHF-UCL.
DR GO; GO:0008083; F:growth factor activity; IDA:BHF-UCL.
DR GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0038191; F:neuropilin binding; IPI:BHF-UCL.
DR GO; GO:0005161; F:platelet-derived growth factor receptor binding; IPI:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:BHF-UCL.
DR GO; GO:0048018; F:receptor ligand activity; IMP:BHF-UCL.
DR GO; GO:0030297; F:transmembrane receptor protein tyrosine kinase activator activity; IDA:BHF-UCL.
DR GO; GO:0043183; F:vascular endothelial growth factor receptor 1 binding; IPI:BHF-UCL.
DR GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; IPI:UniProtKB.
DR GO; GO:0005172; F:vascular endothelial growth factor receptor binding; IPI:UniProtKB.
DR GO; GO:0032147; P:activation of protein kinase activity; IDA:BHF-UCL.
DR GO; GO:0001525; P:angiogenesis; IDA:UniProtKB.
DR GO; GO:0048844; P:artery morphogenesis; ISS:BHF-UCL.
DR GO; GO:0002575; P:basophil chemotaxis; IDA:UniProtKB.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IMP:BHF-UCL.
DR GO; GO:0048593; P:camera-type eye morphogenesis; ISS:BHF-UCL.
DR GO; GO:0055013; P:cardiac muscle cell development; ISS:BHF-UCL.
DR GO; GO:0060948; P:cardiac vascular smooth muscle cell development; ISS:BHF-UCL.
DR GO; GO:0048469; P:cell maturation; ISS:BHF-UCL.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IDA:BHF-UCL.
DR GO; GO:0071456; P:cellular response to hypoxia; IDA:MGI.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IDA:BHF-UCL.
DR GO; GO:0097533; P:cellular stress response to acid chemical; IDA:BHF-UCL.
DR GO; GO:0071679; P:commissural neuron axon guidance; ISS:BHF-UCL.
DR GO; GO:0060982; P:coronary artery morphogenesis; ISS:BHF-UCL.
DR GO; GO:0003169; P:coronary vein morphogenesis; ISS:BHF-UCL.
DR GO; GO:0071542; P:dopaminergic neuron differentiation; ISS:BHF-UCL.
DR GO; GO:0035767; P:endothelial cell chemotaxis; IDA:BHF-UCL.
DR GO; GO:0030855; P:epithelial cell differentiation; ISS:BHF-UCL.
DR GO; GO:0042462; P:eye photoreceptor cell development; ISS:BHF-UCL.
DR GO; GO:0003007; P:heart morphogenesis; ISS:BHF-UCL.
DR GO; GO:0001701; P:in utero embryonic development; ISS:BHF-UCL.
DR GO; GO:0050930; P:induction of positive chemotaxis; IDA:UniProtKB.
DR GO; GO:0001822; P:kidney development; ISS:BHF-UCL.
DR GO; GO:0007595; P:lactation; ISS:BHF-UCL.
DR GO; GO:0030324; P:lung development; ISS:BHF-UCL.
DR GO; GO:0036303; P:lymph vessel morphogenesis; ISS:BHF-UCL.
DR GO; GO:0030225; P:macrophage differentiation; IDA:DFLAT.
DR GO; GO:0060749; P:mammary gland alveolus development; ISS:BHF-UCL.
DR GO; GO:0007498; P:mesoderm development; ISS:BHF-UCL.
DR GO; GO:0030224; P:monocyte differentiation; IDA:DFLAT.
DR GO; GO:0097475; P:motor neuron migration; ISS:UniProtKB.
DR GO; GO:1903392; P:negative regulation of adherens junction organization; IDA:ARUK-UCL.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:1905604; P:negative regulation of blood-brain barrier permeability; IMP:ARUK-UCL.
DR GO; GO:2000048; P:negative regulation of cell-cell adhesion mediated by cadherin; IDA:ARUK-UCL.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:1903141; P:negative regulation of establishment of endothelial barrier; IDA:ARUK-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:BHF-UCL.
DR GO; GO:1902894; P:negative regulation of miRNA transcription; NAS:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0007399; P:nervous system development; TAS:UniProtKB.
DR GO; GO:0003151; P:outflow tract morphogenesis; ISS:BHF-UCL.
DR GO; GO:0001541; P:ovarian follicle development; ISS:BHF-UCL.
DR GO; GO:0050918; P:positive chemotaxis; IDA:BHF-UCL.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA:BHF-UCL.
DR GO; GO:0048842; P:positive regulation of axon extension involved in axon guidance; ISS:BHF-UCL.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IDA:BHF-UCL.
DR GO; GO:1903589; P:positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; IMP:ARUK-UCL.
DR GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; ISS:BHF-UCL.
DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; NAS:BHF-UCL.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IDA:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:BHF-UCL.
DR GO; GO:0038089; P:positive regulation of cell migration by vascular endothelial growth factor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IDA:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:BHF-UCL.
DR GO; GO:0038091; P:positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IDA:UniProtKB.
DR GO; GO:2001028; P:positive regulation of endothelial cell chemotaxis; IDA:BHF-UCL.
DR GO; GO:0038033; P:positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:BHF-UCL.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IDA:BHF-UCL.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:BHF-UCL.
DR GO; GO:1905278; P:positive regulation of epithelial tube formation; IDA:BHF-UCL.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL.
DR GO; GO:0002687; P:positive regulation of leukocyte migration; TAS:BHF-UCL.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:BHF-UCL.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:BHF-UCL.
DR GO; GO:0060754; P:positive regulation of mast cell chemotaxis; IDA:UniProtKB.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; ISS:BHF-UCL.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; IDA:UniProtKB.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:BHF-UCL.
DR GO; GO:1900086; P:positive regulation of peptidyl-tyrosine autophosphorylation; IDA:BHF-UCL.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL.
DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IDA:BHF-UCL.
DR GO; GO:0050927; P:positive regulation of positive chemotaxis; IDA:BHF-UCL.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0090037; P:positive regulation of protein kinase C signaling; IDA:BHF-UCL.
DR GO; GO:1902966; P:positive regulation of protein localization to early endosome; IDA:BHF-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IDA:UniProtKB.
DR GO; GO:0002092; P:positive regulation of receptor internalization; IDA:BHF-UCL.
DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:1901165; P:positive regulation of trophoblast cell migration; IMP:BHF-UCL.
DR GO; GO:1900748; P:positive regulation of vascular endothelial growth factor signaling pathway; IDA:ComplexPortal.
DR GO; GO:0043117; P:positive regulation of vascular permeability; IDA:ARUK-UCL.
DR GO; GO:0031077; P:post-embryonic camera-type eye development; ISS:BHF-UCL.
DR GO; GO:0060319; P:primitive erythrocyte differentiation; ISS:BHF-UCL.
DR GO; GO:0008360; P:regulation of cell shape; IDA:BHF-UCL.
DR GO; GO:0010749; P:regulation of nitric oxide mediated signal transduction; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; ISS:BHF-UCL.
DR GO; GO:0002040; P:sprouting angiogenesis; IBA:GO_Central.
DR GO; GO:0043129; P:surfactant homeostasis; ISS:BHF-UCL.
DR GO; GO:0035148; P:tube formation; IDA:UniProtKB.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0036324; P:vascular endothelial growth factor receptor-2 signaling pathway; IMP:BHF-UCL.
DR GO; GO:0038084; P:vascular endothelial growth factor signaling pathway; IDA:UniProtKB.
DR GO; GO:0061042; P:vascular wound healing; IMP:BHF-UCL.
DR GO; GO:0001570; P:vasculogenesis; TAS:UniProtKB.
DR GO; GO:0038190; P:VEGF-activated neuropilin signaling pathway; IMP:BHF-UCL.
DR CDD; cd00135; PDGF; 1.
DR Gene3D; 2.10.90.10; Cystine-knot cytokines; 1.
DR Gene3D; 2.10.160.10; Vascular endothelial growth factor, heparin-binding domain; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR023581; PD_growth_factor_CS.
DR InterPro; IPR000072; PDGF/VEGF_dom.
DR InterPro; IPR027928; VEGF_C.
DR InterPro; IPR036841; VEGF_C_sf.
DR PANTHER; PTHR12025; VASCULAR ENDOTHELIAL GROWTH FACTOR; 1.
DR PANTHER; PTHR12025:SF5; VASCULAR ENDOTHELIAL GROWTH FACTOR A; 1.
DR Pfam; PF00341; PDGF; 1.
DR Pfam; PF14554; VEGF_C; 1.
DR SMART; SM00141; PDGF; 1.
DR SUPFAM; SSF57501; Cystine-knot cytokines; 1.
DR SUPFAM; SSF57593; Heparin-binding domain from vascular endothelial growth factor; 1.
DR PROSITE; PS00249; PDGF_1; 1.
DR PROSITE; PS50278; PDGF_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Alternative promoter usage;
KW Alternative splicing; Angiogenesis; Cytoplasm; Developmental protein;
KW Differentiation; Direct protein sequencing; Disulfide bond;
KW Endoplasmic reticulum; Extracellular matrix; Glycoprotein; Golgi apparatus;
KW Growth factor; Heparin-binding; Mitogen; Nucleus; Reference proteome;
KW Secreted.
FT CHAIN 1..395
FT /note="Vascular endothelial growth factor A, long form"
FT /id="PRO_0000458064"
FT CHAIN 1..?
FT /note="N-VEGF"
FT /evidence="ECO:0000269|PubMed:11731620"
FT /id="PRO_0000458065"
FT CHAIN ?..395
FT /note="VEGFA"
FT /evidence="ECO:0000269|PubMed:11731620"
FT /id="PRO_0000458066"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..341
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 232..274
FT DISULFID 257
FT /note="Interchain"
FT DISULFID 263..308
FT DISULFID 266
FT /note="Interchain"
FT DISULFID 267..310
FT VAR_SEQ 1..180
FT /note="Missing (in isoform VEGF206, isoform VEGF189,
FT isoform VEGF183, isoform VEGF165, isoform VEGF148, isoform
FT VEGF145, isoform VEGF165B, isoform VEGF121 and isoform
FT VEGF111)"
FT /evidence="ECO:0000269|PubMed:10464055,
FT ECO:0000269|PubMed:12124351, ECO:0000269|PubMed:1791831,
FT ECO:0000269|PubMed:2479986, ECO:0000269|PubMed:9054410,
FT ECO:0000269|PubMed:9878851, ECO:0000269|Ref.12,
FT ECO:0000269|Ref.16"
FT /id="VSP_061891"
FT VAR_SEQ 312..317
FT /note="PKKDRA -> CDKPRR (in isoform VEGF111 and isoform
FT 18)"
FT /evidence="ECO:0000269|Ref.16"
FT /id="VSP_061892"
FT VAR_SEQ 318..395
FT /note="Missing (in isoform VEGF111 and isoform 18)"
FT /evidence="ECO:0000269|Ref.16"
FT /id="VSP_061893"
FT VAR_SEQ 321..345
FT /note="KKSVRGKGKGQKRKRKKSRYKSWSV -> N (in isoform VEGF165,
FT isoform VEGF148, isoform VEGF165B, isoform L-VEGF165,
FT isoform 15 and isoform 17)"
FT /evidence="ECO:0000269|PubMed:10464055,
FT ECO:0000269|PubMed:12124351, ECO:0000269|PubMed:2479986,
FT ECO:0000269|PubMed:9450968"
FT /id="VSP_061894"
FT VAR_SEQ 322..327
FT /note="KSVRGK -> CDKPRR (in isoform VEGF121 and isoform L-
FT VEGF121)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.12"
FT /id="VSP_061895"
FT VAR_SEQ 328..395
FT /note="Missing (in isoform VEGF121 and isoform L-VEGF121)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.12"
FT /id="VSP_061896"
FT VAR_SEQ 339..345
FT /note="RYKSWSV -> R (in isoform VEGF183 and isoform 16)"
FT /evidence="ECO:0000269|PubMed:9878851"
FT /id="VSP_061897"
FT VAR_SEQ 345
FT /note="V -> VYVGARCCLMPWSLPGPH (in isoform VEGF206 and
FT isoform L-VEGF206)"
FT /evidence="ECO:0000269|PubMed:1791831"
FT /id="VSP_061898"
FT VAR_SEQ 346..351
FT /note="PCGPCS -> CDKPRR (in isoform VEGF145)"
FT /evidence="ECO:0000269|PubMed:9054410"
FT /id="VSP_061899"
FT VAR_SEQ 352..395
FT /note="Missing (in isoform VEGF145)"
FT /evidence="ECO:0000269|PubMed:9054410"
FT /id="VSP_061900"
FT VAR_SEQ 378
FT /note="A -> M (in isoform VEGF148 and isoform 17)"
FT /evidence="ECO:0000269|PubMed:10464055"
FT /id="VSP_061901"
FT VAR_SEQ 379..395
FT /note="Missing (in isoform VEGF148 and isoform 17)"
FT /evidence="ECO:0000269|PubMed:10464055"
FT /id="VSP_061902"
FT VAR_SEQ 390..395
FT /note="CDKPRR -> SLTRKD (in isoform VEGF165B and isoform
FT 15)"
FT /evidence="ECO:0000269|PubMed:12124351"
FT /id="VSP_061903"
FT CONFLICT 267
FT /note="C -> S (in Ref. 8; AAC63143)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="D -> H (in Ref. 8; AAC63143)"
FT /evidence="ECO:0000305"
FT HELIX 43..50
FT /evidence="ECO:0007829|PDB:1MKK"
FT STRAND 51..60
FT /evidence="ECO:0007829|PDB:1MKK"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:1MKK"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:1MKK"
FT STRAND 71..84
FT /evidence="ECO:0007829|PDB:1MKK"
FT STRAND 93..109
FT /evidence="ECO:0007829|PDB:1MKK"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:4GLN"
FT STRAND 116..131
FT /evidence="ECO:0007829|PDB:1MKK"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:4DEQ"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:4DEQ"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:4DEQ"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:4DEQ"
FT HELIX 210..214
FT /evidence="ECO:0007829|PDB:4DEQ"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:4DEQ"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:1KMX"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:4DEQ"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:1KMX"
SQ SEQUENCE 395 AA; 43597 MW; 8ADF6524B1835A2D CRC64;
MTDRQTDTAP SPSYHLLPGR RRTVDAAASR GQGPEPAPGG GVEGVGARGV ALKLFVQLLG
CSRFGGAVVR AGEAEPSGAA RSASSGREEP QPEEGEEEEE KEEERGPQWR LGARKPGSWT
GEAAVCADSA PAARAPQALA RASGRGGRVA RRGAEESGPP HSPSRRGSAS RAGPGRASET
MNFLLSWVHW SLALLLYLHH AKWSQAAPMA EGGGQNHHEV VKFMDVYQRS YCHPIETLVD
IFQEYPDEIE YIFKPSCVPL MRCGGCCNDE GLECVPTEES NITMQIMRIK PHQGQHIGEM
SFLQHNKCEC RPKKDRARQE KKSVRGKGKG QKRKRKKSRY KSWSVPCGPC SERRKHLFVQ
DPQTCKCSCK NTDSRCKARQ LELNERTCRC DKPRR
//
