VEGFA_HUMAN
ID VEGFA_HUMAN Reviewed; 232 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 16-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 259.
DE RecName: Full=Vascular endothelial growth factor A;
DE Short=VEGF-A;
DE AltName: Full=Vascular permeability factor;
DE Short=VPF;
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 23-232.
RG SeattleSNPs variation discovery resource;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [22]
RP PROTEIN SEQUENCE OF 27-41.
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 27-41.
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 27-36; 43-50 AND 59-81.
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 114-209 (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 X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 34-135.
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 [40]
RP STRUCTURE BY NMR OF 34-135.
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 [41]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 34-135.
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 [42]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 39-134.
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 [43]
RP STRUCTURE BY NMR OF 137-215.
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: Growth factor active in angiogenesis, vasculogenesis and
CC 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. NRP1/Neuropilin-1
CC binds isoforms VEGF-165 and VEGF-145. Isoform VEGF165B binds to KDR but
CC does not activate downstream signaling pathways, does not activate
CC angiogenesis and inhibits tumor growth. Binding to NRP1 receptor
CC initiates a signaling pathway needed for motor neuron axon guidance and
CC cell body migration, including for the caudal migration of facial motor
CC neurons from rhombomere 4 to rhombomere 6 during embryonic development
CC (By similarity). Also binds the DEAR/FBXW7-AS1 receptor
CC (PubMed:17446437). {ECO:0000250|UniProtKB:Q00731,
CC ECO:0000269|PubMed:11427521, ECO:0000269|PubMed:16489009,
CC ECO:0000269|PubMed:17446437, ECO:0000269|PubMed:25825981}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Also found as
CC 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=6; 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: Secreted {ECO:0000269|PubMed:11563986,
CC ECO:0000269|PubMed:11731620, ECO:0000269|PubMed:15896327}. Note=VEGF121
CC is acidic and freely secreted. VEGF165 is more basic, has heparin-
CC binding properties and, although a significant proportion remains cell-
CC associated, most is freely secreted. VEGF189 is very basic, it is cell-
CC associated after secretion and is bound avidly by heparin and the
CC extracellular matrix, although it may be released as a soluble form by
CC heparin, heparinase or plasmin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing, Alternative initiation; Named isoforms=17;
CC Comment=Additional isoforms seem to exist.;
CC Name=VEGF206;
CC IsoId=P15692-1; Sequence=Displayed;
CC Name=VEGF189;
CC IsoId=P15692-2; Sequence=VSP_004622;
CC Name=VEGF183;
CC IsoId=P15692-3; Sequence=VSP_004621;
CC Name=VEGF165; Synonyms=VEGF;
CC IsoId=P15692-4; Sequence=VSP_004618, VSP_004619;
CC Name=VEGF148;
CC IsoId=P15692-5; Sequence=VSP_004618, VSP_004619, VSP_004624,
CC VSP_004625;
CC Name=VEGF145;
CC IsoId=P15692-6; Sequence=VSP_004623;
CC Name=VEGF165B;
CC IsoId=P15692-8; Sequence=VSP_004618, VSP_004619, VSP_014783;
CC Name=VEGF121;
CC IsoId=P15692-9; Sequence=VSP_004620;
CC Name=VEGF111;
CC IsoId=P15692-10; Sequence=VSP_026781;
CC Name=L-VEGF165;
CC IsoId=P15692-11; Sequence=VSP_038745, VSP_004618, VSP_004619;
CC Name=L-VEGF121;
CC IsoId=P15692-12; Sequence=VSP_038745, VSP_004620;
CC Name=L-VEGF189;
CC IsoId=P15692-13; Sequence=VSP_038745, VSP_004622;
CC Name=L-VEGF206;
CC IsoId=P15692-14; Sequence=VSP_038745;
CC Name=15;
CC IsoId=P15692-15; Sequence=VSP_038745, VSP_054111, VSP_014783;
CC Name=16;
CC IsoId=P15692-16; Sequence=VSP_038745, VSP_004621;
CC Name=17;
CC IsoId=P15692-17; Sequence=VSP_038745, VSP_054111, VSP_004624,
CC VSP_004625;
CC Name=18;
CC IsoId=P15692-18; Sequence=VSP_038745, VSP_026781;
CC -!- TISSUE SPECIFICITY: Isoform VEGF189, isoform VEGF165 and isoform
CC VEGF121 are widely expressed. Isoform VEGF206 and isoform VEGF145 are
CC not widely expressed. A higher level expression seen in pituitary
CC tumors as compared to the pituitary gland.
CC {ECO:0000269|PubMed:22009797}.
CC -!- INDUCTION: By hypoxia. Regulated by growth factors, cytokines,
CC gonadotropins, nitric oxide, hypoglycemia and oncogenic mutations.
CC {ECO:0000269|PubMed:22009797}.
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-VEGF165]: Produced by alternative promoter
CC usage and alternative initiation. Starts at an alternative upstream CUG
CC codon. Post-translationally processed to produce the secreted VEGF
CC peptide and a N-terminal peptide N-VEGF. The unprocessed protein and
CC the N-VEGF peptide may localize to the nucleus (PubMed:15896327), the
CC endoplasmic reticulum and the Golgi (PubMed:11731620) or the
CC extracellular matrix (PubMed:11563986). {ECO:0000305|PubMed:11563986,
CC ECO:0000305|PubMed:11731620, ECO:0000305|PubMed:15896327}.
CC -!- MISCELLANEOUS: [Isoform L-VEGF121]: Produced by alternative promoter
CC usage and alternative initiation. Starts at an alternative upstream CUG
CC codon. Post-translationally processed to produce the secreted VEGF
CC peptide and a N-terminal peptide N-VEGF. The unprocessed protein and
CC the N-VEGF peptide may localize to the nucleus (PubMed:15896327), the
CC endoplasmic reticulum and the Golgi (PubMed:11731620) or the
CC extracellular matrix (PubMed:11563986). {ECO:0000305|PubMed:11563986,
CC ECO:0000305|PubMed:11731620, ECO:0000305|PubMed:15896327}.
CC -!- MISCELLANEOUS: [Isoform L-VEGF189]: Produced by alternative promoter
CC usage and alternative initiation. Starts at an alternative upstream CUG
CC codon. Post-translationally processed to produce the secreted VEGF
CC peptide and a N-terminal peptide N-VEGF. The unprocessed protein and
CC the N-VEGF peptide may localize to the nucleus (PubMed:15896327), the
CC endoplasmic reticulum and the Golgi (PubMed:11731620) or the
CC extracellular matrix (PubMed:11563986). {ECO:0000305|PubMed:11563986,
CC ECO:0000305|PubMed:11731620, ECO:0000305|PubMed:15896327}.
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/";
CC ---------------------------------------------------------------------------
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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=34-135.
DR PDB; 1CZ8; X-ray; 2.40 A; V/W=40-133.
DR PDB; 1FLT; X-ray; 1.70 A; V/W=38-135.
DR PDB; 1KAT; NMR; -; V/W=37-135.
DR PDB; 1KMX; NMR; -; A=183-232.
DR PDB; 1MJV; X-ray; 2.10 A; A/B=40-134.
DR PDB; 1MKG; X-ray; 2.50 A; A/B/C/D=40-134.
DR PDB; 1MKK; X-ray; 1.32 A; A/B=40-134.
DR PDB; 1QTY; X-ray; 2.70 A; R/S/V/W=34-135.
DR PDB; 1TZH; X-ray; 2.60 A; V/W=34-135.
DR PDB; 1TZI; X-ray; 2.80 A; V=34-135.
DR PDB; 1VGH; NMR; -; A=180-232.
DR PDB; 1VPF; X-ray; 2.50 A; A/B/C/D=34-135.
DR PDB; 1VPP; X-ray; 1.90 A; V/W=34-135.
DR PDB; 2FJG; X-ray; 2.80 A; V/W=34-135.
DR PDB; 2FJH; X-ray; 3.10 A; V/W=34-135.
DR PDB; 2QR0; X-ray; 3.50 A; C/D/I/J/O/P/U/V=39-135.
DR PDB; 2VGH; NMR; -; A=182-232.
DR PDB; 2VPF; X-ray; 1.93 A; A/B/C/D/E/F/G/H=34-135.
DR PDB; 3BDY; X-ray; 2.60 A; V=34-135.
DR PDB; 3P9W; X-ray; 2.41 A; A/C/E/G=35-138.
DR PDB; 3QTK; X-ray; 1.85 A; A/B/C/D/E/F=34-135.
DR PDB; 3S1B; X-ray; 2.90 A; V=38-133.
DR PDB; 3S1K; X-ray; 2.55 A; V/W=34-135.
DR PDB; 3V2A; X-ray; 3.20 A; A=27-140.
DR PDB; 4DEQ; X-ray; 2.65 A; A/B=183-232.
DR PDB; 4GLN; X-ray; 1.60 A; E/F=34-135.
DR PDB; 4GLS; X-ray; 1.60 A; E/F=34-135.
DR PDB; 4KZN; X-ray; 1.71 A; A=39-135.
DR PDB; 4QAF; X-ray; 1.80 A; C/D=34-135.
DR PDB; 4WPB; X-ray; 3.11 A; A/B=34-135.
DR PDB; 4ZFF; X-ray; 2.75 A; C/D=37-135.
DR PDB; 5DN2; X-ray; 1.95 A; E/F/G=205-232.
DR PDB; 5FV1; X-ray; 2.70 A; V/W=27-136.
DR PDB; 5FV2; X-ray; 3.45 A; V/W/X=27-136.
DR PDB; 5HHC; X-ray; 2.10 A; A/B=34-135.
DR PDB; 5HHD; X-ray; 2.10 A; A/B=34-135.
DR PDB; 5O4E; X-ray; 2.15 A; E/F=39-134.
DR PDB; 5T89; X-ray; 4.00 A; V/W=27-155.
DR PDB; 6BFT; X-ray; 2.55 A; C/G=36-135.
DR PDB; 6D3O; X-ray; 3.10 A; A/B=34-135.
DR PDB; 6T9D; X-ray; 2.90 A; CCC/DDD=27-141.
DR PDB; 6V7K; X-ray; 2.50 A; A/B=34-135.
DR PDB; 6Z13; X-ray; 1.80 A; V/W=39-133.
DR PDB; 6Z3F; X-ray; 2.10 A; V/W=39-133.
DR PDB; 6ZBR; X-ray; 1.60 A; V/W=39-133.
DR PDB; 6ZCD; X-ray; 1.80 A; V/W=39-133.
DR PDB; 6ZFL; X-ray; 1.60 A; V/W=39-133.
DR PDB; 7KEZ; X-ray; 2.31 A; V=27-136.
DR PDB; 7KF0; X-ray; 2.32 A; C/V=27-136.
DR PDB; 7KF1; X-ray; 2.45 A; C/F/J/V=27-136.
DR PDB; 7LL8; X-ray; 2.31 A; A/B=34-135.
DR PDB; 7LL9; X-ray; 2.90 A; A/B/E/F=34-135.
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; 62.
DR ComplexPortal; CPX-1977; Vascular endothelial growth factor A complex.
DR CORUM; P15692; -.
DR DIP; DIP-5740N; -.
DR IntAct; P15692; 24.
DR MINT; P15692; -.
DR STRING; 9606.ENSP00000478570; -.
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; DB05890; Veglin.
DR DrugCentral; P15692; -.
DR MoonDB; P15692; Predicted.
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; P15692; -.
DR PeptideAtlas; P15692; -.
DR PRIDE; 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; 2485 antibodies from 55 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. [P15692-13]
DR UCSC; uc003owd.5; human. [P15692-1]
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; NCAERRK; -.
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; 13 hits in 1082 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 201 other 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: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:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR GO; GO:0030141; C:secretory granule; IDA:UniProtKB.
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: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: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: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:0032793; P:positive regulation of CREB transcription factor activity; IDA:BHF-UCL.
DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IDA:UniProtKB.
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:1901727; P:positive regulation of histone deacetylase activity; 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:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IGI:BHF-UCL.
DR GO; GO:0042327; P:positive regulation of phosphorylation; IMP: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:BHF-UCL.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:BHF-UCL.
DR GO; GO:0090037; P:positive regulation of protein kinase C signaling; IDA:BHF-UCL.
DR GO; GO:1903572; P:positive regulation of protein kinase D 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:1902336; P:positive regulation of retinal ganglion cell axon guidance; ISS: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:0061419; P:positive regulation of transcription from RNA polymerase II promoter in response to hypoxia; IMP:BHF-UCL.
DR GO; GO:1901165; P:positive regulation of trophoblast cell migration; IMP:BHF-UCL.
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:0090259; P:regulation of retinal ganglion cell axon guidance; ISS:BHF-UCL.
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: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; 2.10.160.10; -; 1.
DR Gene3D; 2.10.90.10; -; 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 Pfam; PF00341; PDGF; 1.
DR Pfam; PF14554; VEGF_C; 1.
DR SMART; SM00141; PDGF; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR SUPFAM; SSF57593; SSF57593; 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; Developmental protein; Differentiation;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Growth factor;
KW Heparin-binding; Mitogen; Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:15340161,
FT ECO:0000269|PubMed:7678805"
FT CHAIN 27..232
FT /note="Vascular endothelial growth factor A"
FT /id="PRO_0000023386"
FT REGION 132..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..161
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 52..94
FT DISULFID 77
FT /note="Interchain"
FT DISULFID 83..128
FT DISULFID 86
FT /note="Interchain"
FT DISULFID 87..130
FT VAR_SEQ 1
FT /note="M -> MTDRQTDTAPSPSYHLLPGRRRTVDAAASRGQGPEPAPGGGVEGVGA
FT RGVALKLFVQLLGCSRFGGAVVRAGEAEPSGAARSASSGREEPQPEEGEEEEEKEEERG
FT PQWRLGARKPGSWTGEAAVCADSAPAARAPQALARASGRGGRVARRGAEESGPPHSPSR
FT RGSASRAGPGRASETM (in isoform L-VEGF165, isoform L-VEGF121,
FT isoform L-VEGF189, isoform L-VEGF206, isoform 15, isoform
FT 16, isoform 17 and isoform 18)"
FT /evidence="ECO:0000303|PubMed:9450968"
FT /id="VSP_038745"
FT VAR_SEQ 132..226
FT /note="Missing (in isoform VEGF111 and isoform 18)"
FT /evidence="ECO:0000303|Ref.16"
FT /id="VSP_026781"
FT VAR_SEQ 141..182
FT /note="KKSVRGKGKGQKRKRKKSRYKSWSVYVGARCCLMPWSLPGPH -> N (in
FT isoform 15 and isoform 17)"
FT /evidence="ECO:0000305"
FT /id="VSP_054111"
FT VAR_SEQ 141
FT /note="K -> N (in isoform VEGF148, isoform VEGF165, isoform
FT VEGF165B and isoform L-VEGF165)"
FT /evidence="ECO:0000303|PubMed:10464055,
FT ECO:0000303|PubMed:12124351, ECO:0000303|PubMed:1567395,
FT ECO:0000303|PubMed:19054851, ECO:0000303|PubMed:2479986,
FT ECO:0000303|PubMed:9450968, ECO:0000303|Ref.11,
FT ECO:0000303|Ref.13, ECO:0000303|Ref.14, ECO:0000303|Ref.15"
FT /id="VSP_004618"
FT VAR_SEQ 142..226
FT /note="Missing (in isoform VEGF121 and isoform L-VEGF121)"
FT /evidence="ECO:0000303|Ref.12"
FT /id="VSP_004620"
FT VAR_SEQ 142..182
FT /note="Missing (in isoform VEGF148, isoform VEGF165,
FT isoform VEGF165B and isoform L-VEGF165)"
FT /evidence="ECO:0000303|PubMed:10464055,
FT ECO:0000303|PubMed:12124351, ECO:0000303|PubMed:1567395,
FT ECO:0000303|PubMed:19054851, ECO:0000303|PubMed:2479986,
FT ECO:0000303|PubMed:9450968, ECO:0000303|Ref.11,
FT ECO:0000303|Ref.13, ECO:0000303|Ref.14, ECO:0000303|Ref.15"
FT /id="VSP_004619"
FT VAR_SEQ 160..182
FT /note="Missing (in isoform VEGF183 and isoform 16)"
FT /evidence="ECO:0000303|PubMed:10067980,
FT ECO:0000303|PubMed:9878851"
FT /id="VSP_004621"
FT VAR_SEQ 166..226
FT /note="Missing (in isoform VEGF145)"
FT /evidence="ECO:0000303|PubMed:9054410"
FT /id="VSP_004623"
FT VAR_SEQ 166..182
FT /note="Missing (in isoform VEGF189 and isoform L-VEGF189)"
FT /evidence="ECO:0000303|PubMed:2479986,
FT ECO:0000303|PubMed:2479987"
FT /id="VSP_004622"
FT VAR_SEQ 215
FT /note="A -> M (in isoform VEGF148 and isoform 17)"
FT /evidence="ECO:0000303|PubMed:10464055"
FT /id="VSP_004624"
FT VAR_SEQ 216..232
FT /note="Missing (in isoform VEGF148 and isoform 17)"
FT /evidence="ECO:0000303|PubMed:10464055"
FT /id="VSP_004625"
FT VAR_SEQ 227..232
FT /note="CDKPRR -> SLTRKD (in isoform VEGF165B and isoform
FT 15)"
FT /evidence="ECO:0000303|PubMed:12124351"
FT /id="VSP_014783"
FT CONFLICT 87
FT /note="C -> S (in Ref. 8; AAC63143)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
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 232 AA; 27042 MW; FB49F364446F4D01 CRC64;
MNFLLSWVHW SLALLLYLHH AKWSQAAPMA EGGGQNHHEV VKFMDVYQRS YCHPIETLVD
IFQEYPDEIE YIFKPSCVPL MRCGGCCNDE GLECVPTEES NITMQIMRIK PHQGQHIGEM
SFLQHNKCEC RPKKDRARQE KKSVRGKGKG QKRKRKKSRY KSWSVYVGAR CCLMPWSLPG
PHPCGPCSER RKHLFVQDPQ TCKCSCKNTD SRCKARQLEL NERTCRCDKP RR
