VEGFA_MOUSE
ID VEGFA_MOUSE Reviewed; 214 AA.
AC Q00731; O70123; Q66S31; Q6GT23; Q6WZL9;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 198.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS VEGF-1; VEGF-2 AND VEGF-3).
RX PubMed=1592003; DOI=10.1242/dev.114.2.521;
RA Breier G., Albrecht U., Sterrer S., Risau W.;
RT "Expression of vascular endothelial growth factor during embryonic
RT angiogenesis and endothelial cell differentiation.";
RL Development 114:521-532(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF-1).
RX PubMed=1644816; DOI=10.1016/s0021-9258(18)42003-0;
RA Claffey K.P., Wilkison W.O., Spiegelman B.M.;
RT "Vascular endothelial growth factor. Regulation by cell differentiation and
RT activated second messenger pathways.";
RL J. Biol. Chem. 267:16317-16322(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF-4).
RC STRAIN=ICR;
RX PubMed=9446618; DOI=10.1074/jbc.273.5.3033;
RA Sugihara T., Wadhwa R., Kaul S.C., Mitsui Y.;
RT "A novel alternatively spliced form of murine vascular endothelial growth
RT factor, VEGF 115.";
RL J. Biol. Chem. 273:3033-3038(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF-5).
RC STRAIN=FVB/N;
RA Jankowsky J.A., Adamski F.M., Robertson F.M.;
RT "Identification of a unique Mus musculus VEGF isoform of 102 amino acids.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM L-VEGF-1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-123 (ISOFORMS VEGF-1/VEGF-2/VEGF-3).
RC STRAIN=C57BL/6J; TISSUE=Retina;
RA Minchenko O.H., Minchenko D.O., Opentanova I.L.;
RT "Alternatively spliced forms of mouse VEGF.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-3 (ISOFORMS
RP VEGF-1/VEGF-2/VEGF-3/VEGF-4/VEGF-5).
RX PubMed=8632007; DOI=10.1074/jbc.271.7.3877;
RA Shima D.T., Kuroki M., Deutsch U., Ng Y., Adamis A.P., D'Amore P.A.;
RT "The mouse gene for vascular endothelial growth factor. Genomic structure,
RT definition of the transcriptional unit, and characterization of
RT transcriptional and post-transcriptional regulatory sequences.";
RL J. Biol. Chem. 271:3877-3883(1996).
RN [9]
RP DEVELOPMENTAL STAGE.
RX PubMed=10878616;
RX DOI=10.1002/1097-0177(200007)218:3<507::aid-dvdy1012>3.0.co;2-5;
RA Pepper M.S., Baetens D., Mandriota S.J., Di Sanza C., Oikemus S.,
RA Lane T.F., Soriano J.V., Montesano R., Iruela-Arispe M.L.;
RT "Regulation of VEGF and VEGF receptor expression in the rodent mammary
RT gland during pregnancy, lactation, and involution.";
RL Dev. Dyn. 218:507-524(2000).
RN [10]
RP FUNCTION.
RX PubMed=16293765; DOI=10.1152/physiolgenomics.00144.2005;
RA Herrera V.L., Ponce L.R., Bagamasbad P.D., VanPelt B.D., Didishvili T.,
RA Ruiz-Opazo N.;
RT "Embryonic lethality in Dear gene-deficient mice: new player in
RT angiogenesis.";
RL Physiol. Genomics 23:257-268(2005).
RN [11]
RP INDUCTION.
RX PubMed=16259067; DOI=10.3349/ymj.2005.46.5.679;
RA Shin S.-Y., Lee H.-J., Ko D.-S., Lee H.-C., Park W.I.;
RT "The regulators of VEGF expression in mouse ovaries.";
RL Yonsei Med. J. 46:679-686(2005).
RN [12]
RP FUNCTION, AND 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 [13]
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).
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. May play a role in
CC increasing vascular permeability during lactation, when increased
CC transport of molecules from the blood is required for efficient milk
CC protein synthesis (By similarity). Binding to NRP1 receptor initiates a
CC signaling pathway needed for motor neuron axon guidance and cell body
CC migration, including for the caudal migration of facial motor neurons
CC from rhombomere 4 to rhombomere 6 during embryonic development
CC (PubMed:26503042). Also binds the DEAR/FBXW7-AS1 receptor
CC (PubMed:16293765). {ECO:0000250|UniProtKB:P15692,
CC ECO:0000269|PubMed:16293765, ECO:0000269|PubMed:26503042}.
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 (By similarity).
CC {ECO:0000250|UniProtKB:P15692, ECO:0000250|UniProtKB:P16612,
CC ECO:0000269|PubMed:26503042}.
CC -!- SUBCELLULAR LOCATION: [Isoform VEGF-1]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Isoform VEGF-2]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Isoform VEGF-3]: Cell membrane; Peripheral
CC membrane protein. Note=Remains cell-surface associated unless released
CC by heparin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing, Alternative initiation; Named isoforms=6;
CC Name=VEGF-3; Synonyms=VEGF188;
CC IsoId=Q00731-1; Sequence=Displayed;
CC Name=VEGF-1; Synonyms=VEGF164;
CC IsoId=Q00731-2; Sequence=VSP_004626, VSP_004627;
CC Name=VEGF-2; Synonyms=VEGF120;
CC IsoId=Q00731-3; Sequence=VSP_004628;
CC Name=VEGF-4; Synonyms=VEGF115;
CC IsoId=Q00731-4; Sequence=VSP_016418, VSP_016421;
CC Name=VEGF-5; Synonyms=VEGF102;
CC IsoId=Q00731-5; Sequence=VSP_016419, VSP_016420;
CC Name=L-VEGF-1;
CC IsoId=Q00731-6; Sequence=VSP_038746, VSP_004626, VSP_004627;
CC -!- TISSUE SPECIFICITY: In developing embryos, expressed mainly in the
CC choroid plexus, paraventricular neuroepithelium, placenta and kidney
CC glomeruli. Also found in bronchial epithelium, adrenal gland and in
CC seminiferous tubules of testis. High expression of VEGF continues in
CC kidney glomeruli and choroid plexus in adults.
CC -!- DEVELOPMENTAL STAGE: Levels increase during pregnancy (maximum 5.5-fold
CC at 5 days) and a more marked increase occurs during lactation (maximal
CC 9.7-fold at 7 days). Levels decrease progressively during the phase of
CC involution. {ECO:0000269|PubMed:10878616}.
CC -!- INDUCTION: By IL-6 and FSH in vitro. {ECO:0000269|PubMed:16259067}.
CC -!- DOMAIN: Isoform VEGF-3 contains a basic insert which acts as a cell
CC retention signal.
CC -!- MISCELLANEOUS: [Isoform L-VEGF-1]: Produced by alternative promoter
CC usage and alternative initiation. 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=AAH61468.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; S37052; AAB22252.1; -; mRNA.
DR EMBL; S38083; AAB22253.1; -; mRNA.
DR EMBL; S38100; AAB22254.1; -; mRNA.
DR EMBL; M95200; AAA40547.1; -; mRNA.
DR EMBL; U50279; AAC05442.1; -; mRNA.
DR EMBL; AY263146; AAP86647.1; -; mRNA.
DR EMBL; AC127690; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC061468; AAH61468.1; ALT_INIT; mRNA.
DR EMBL; AY707864; AAU11325.1; -; mRNA.
DR EMBL; AY750956; AAU95484.1; -; mRNA.
DR EMBL; AY750957; AAU95485.1; -; mRNA.
DR EMBL; U41383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS28818.2; -. [Q00731-6]
DR CCDS; CCDS70817.1; -. [Q00731-3]
DR PIR; A44881; A44881.
DR PIR; B44881; B44881.
DR RefSeq; NP_001020421.2; NM_001025250.3.
DR RefSeq; NP_001020428.2; NM_001025257.3.
DR RefSeq; NP_001103736.1; NM_001110266.1.
DR RefSeq; NP_001103737.1; NM_001110267.1.
DR RefSeq; NP_001103738.1; NM_001110268.1.
DR RefSeq; NP_001273985.1; NM_001287056.1. [Q00731-1]
DR RefSeq; NP_001273986.1; NM_001287057.1. [Q00731-2]
DR RefSeq; NP_001273987.1; NM_001287058.1. [Q00731-3]
DR RefSeq; NP_001303970.1; NM_001317041.1.
DR RefSeq; NP_033531.3; NM_009505.4. [Q00731-6]
DR AlphaFoldDB; Q00731; -.
DR SMR; Q00731; -.
DR BioGRID; 204512; 6.
DR ComplexPortal; CPX-3160; Vascular endothelial growth factor A complex.
DR DIP; DIP-31909N; -.
DR IntAct; Q00731; 2.
DR STRING; 10090.ENSMUSP00000115883; -.
DR GlyGen; Q00731; 1 site.
DR iPTMnet; Q00731; -.
DR PhosphoSitePlus; Q00731; -.
DR MaxQB; Q00731; -.
DR PaxDb; Q00731; -.
DR PRIDE; Q00731; -.
DR ProteomicsDB; 297539; -. [Q00731-1]
DR ProteomicsDB; 297540; -. [Q00731-2]
DR ProteomicsDB; 297541; -. [Q00731-3]
DR ProteomicsDB; 297542; -. [Q00731-4]
DR ProteomicsDB; 297543; -. [Q00731-5]
DR ProteomicsDB; 297544; -. [Q00731-6]
DR Antibodypedia; 3956; 2485 antibodies from 55 providers.
DR DNASU; 22339; -.
DR Ensembl; ENSMUST00000024747; ENSMUSP00000024747; ENSMUSG00000023951. [Q00731-3]
DR Ensembl; ENSMUST00000071648; ENSMUSP00000071575; ENSMUSG00000023951. [Q00731-6]
DR GeneID; 22339; -.
DR KEGG; mmu:22339; -.
DR UCSC; uc008crn.4; mouse. [Q00731-1]
DR UCSC; uc008cro.4; mouse. [Q00731-2]
DR UCSC; uc008crp.4; mouse. [Q00731-3]
DR UCSC; uc008crr.3; mouse. [Q00731-5]
DR CTD; 7422; -.
DR MGI; MGI:103178; Vegfa.
DR VEuPathDB; HostDB:ENSMUSG00000023951; -.
DR eggNOG; ENOG502QVI8; Eukaryota.
DR GeneTree; ENSGT00940000157284; -.
DR HOGENOM; CLU_042996_3_0_1; -.
DR InParanoid; Q00731; -.
DR OrthoDB; 1364454at2759; -.
DR PhylomeDB; Q00731; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-194313; VEGF ligand-receptor interactions.
DR Reactome; R-MMU-195399; VEGF binds to VEGFR leading to receptor dimerization.
DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-MMU-5218921; VEGFR2 mediated cell proliferation.
DR BioGRID-ORCS; 22339; 5 hits in 80 CRISPR screens.
DR ChiTaRS; Vegfa; mouse.
DR PRO; PR:Q00731; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q00731; protein.
DR Bgee; ENSMUSG00000023951; Expressed in retinal neural layer and 292 other tissues.
DR ExpressionAtlas; Q00731; baseline and differential.
DR Genevisible; Q00731; MM.
DR GO; GO:0005912; C:adherens junction; ISO:MGI.
DR GO; GO:0005604; C:basement membrane; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030141; C:secretory granule; ISS:UniProtKB.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0042056; F:chemoattractant activity; IDA:BHF-UCL.
DR GO; GO:0005125; F:cytokine activity; ISS:UniProtKB.
DR GO; GO:0001968; F:fibronectin binding; ISS:UniProtKB.
DR GO; GO:0008083; F:growth factor activity; ISS:UniProtKB.
DR GO; GO:0019838; F:growth factor binding; ISO:MGI.
DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0038191; F:neuropilin binding; ISO:MGI.
DR GO; GO:0005161; F:platelet-derived growth factor receptor binding; ISS:UniProtKB.
DR GO; GO:0048018; F:receptor ligand activity; ISS:UniProtKB.
DR GO; GO:0043183; F:vascular endothelial growth factor receptor 1 binding; ISS:UniProtKB.
DR GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; ISS:UniProtKB.
DR GO; GO:0005172; F:vascular endothelial growth factor receptor binding; ISS:UniProtKB.
DR GO; GO:0032147; P:activation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IDA:MGI.
DR GO; GO:0060978; P:angiogenesis involved in coronary vascular morphogenesis; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0048844; P:artery morphogenesis; IMP:MGI.
DR GO; GO:0002575; P:basophil chemotaxis; ISO:MGI.
DR GO; GO:0001568; P:blood vessel development; IMP:MGI.
DR GO; GO:0048514; P:blood vessel morphogenesis; IDA:MGI.
DR GO; GO:0001974; P:blood vessel remodeling; ISO:MGI.
DR GO; GO:0060346; P:bone trabecula formation; IMP:MGI.
DR GO; GO:0061430; P:bone trabecula morphogenesis; IMP:MGI.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; ISO:MGI.
DR GO; GO:0048593; P:camera-type eye morphogenesis; IMP:MGI.
DR GO; GO:0055013; P:cardiac muscle cell development; IMP:MGI.
DR GO; GO:0060948; P:cardiac vascular smooth muscle cell development; IMP:BHF-UCL.
DR GO; GO:0060326; P:cell chemotaxis; ISO:MGI.
DR GO; GO:0016477; P:cell migration; IDA:MGI.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IGI:MGI.
DR GO; GO:0071456; P:cellular response to hypoxia; ISS:UniProtKB.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IGI:BHF-UCL.
DR GO; GO:0097533; P:cellular stress response to acid chemical; ISO:MGI.
DR GO; GO:0071679; P:commissural neuron axon guidance; IDA:BHF-UCL.
DR GO; GO:0060982; P:coronary artery morphogenesis; IMP:BHF-UCL.
DR GO; GO:0003169; P:coronary vein morphogenesis; IMP:BHF-UCL.
DR GO; GO:0071542; P:dopaminergic neuron differentiation; IGI:MGI.
DR GO; GO:0035767; P:endothelial cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0043542; P:endothelial cell migration; IMP:MGI.
DR GO; GO:0001935; P:endothelial cell proliferation; IDA:MGI.
DR GO; GO:0030855; P:epithelial cell differentiation; IMP:MGI.
DR GO; GO:0002070; P:epithelial cell maturation; IMP:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IMP:MGI.
DR GO; GO:0042462; P:eye photoreceptor cell development; IMP:MGI.
DR GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0050930; P:induction of positive chemotaxis; ISO:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0007595; P:lactation; IMP:MGI.
DR GO; GO:0048286; P:lung alveolus development; ISO:MGI.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:0060426; P:lung vasculature development; IMP:MGI.
DR GO; GO:0036303; P:lymph vessel morphogenesis; IMP:BHF-UCL.
DR GO; GO:0001946; P:lymphangiogenesis; IDA:MGI.
DR GO; GO:0030225; P:macrophage differentiation; ISS:UniProtKB.
DR GO; GO:0060749; P:mammary gland alveolus development; IMP:MGI.
DR GO; GO:0007498; P:mesoderm development; IMP:MGI.
DR GO; GO:0030224; P:monocyte differentiation; ISS:UniProtKB.
DR GO; GO:0097475; P:motor neuron migration; IMP:UniProtKB.
DR GO; GO:0048255; P:mRNA stabilization; ISO:MGI.
DR GO; GO:1903392; P:negative regulation of adherens junction organization; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:1905604; P:negative regulation of blood-brain barrier permeability; ISO:MGI.
DR GO; GO:0045779; P:negative regulation of bone resorption; ISO:MGI.
DR GO; GO:0022408; P:negative regulation of cell-cell adhesion; IGI:MGI.
DR GO; GO:2000048; P:negative regulation of cell-cell adhesion mediated by cadherin; ISO:MGI.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; IMP:BHF-UCL.
DR GO; GO:1903141; P:negative regulation of establishment of endothelial barrier; ISO:MGI.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IDA:BHF-UCL.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:BHF-UCL.
DR GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
DR GO; GO:0043069; P:negative regulation of programmed cell death; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0007399; P:nervous system development; ISO:MGI.
DR GO; GO:0007405; P:neuroblast proliferation; IGI:MGI.
DR GO; GO:0048666; P:neuron development; IMP:BHF-UCL.
DR GO; GO:0003151; P:outflow tract morphogenesis; IMP:BHF-UCL.
DR GO; GO:0001541; P:ovarian follicle development; IMP:MGI.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
DR GO; GO:0050918; P:positive chemotaxis; IDA:BHF-UCL.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA:MGI.
DR GO; GO:0048842; P:positive regulation of axon extension involved in axon guidance; IDA:BHF-UCL.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISS:UniProtKB.
DR GO; GO:1903589; P:positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; ISO:MGI.
DR GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; IDA:UniProtKB.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISS:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0038089; P:positive regulation of cell migration by vascular endothelial growth factor signaling pathway; ISO:MGI.
DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:MGI.
DR GO; GO:0038091; P:positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0032793; P:positive regulation of CREB transcription factor activity; ISS:UniProtKB.
DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; ISO:MGI.
DR GO; GO:0038033; P:positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:MGI.
DR GO; GO:1905278; P:positive regulation of epithelial tube formation; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:1901727; P:positive regulation of histone deacetylase activity; ISO:MGI.
DR GO; GO:1901492; P:positive regulation of lymphangiogenesis; IDA:MGI.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
DR GO; GO:0060754; P:positive regulation of mast cell chemotaxis; ISO:MGI.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IGI:MGI.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:MGI.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; ISO:MGI.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISS:UniProtKB.
DR GO; GO:1900086; P:positive regulation of peptidyl-tyrosine autophosphorylation; ISS:UniProtKB.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:MGI.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:MGI.
DR GO; GO:0042327; P:positive regulation of phosphorylation; ISO:MGI.
DR GO; GO:0050927; P:positive regulation of positive chemotaxis; ISS:UniProtKB.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:1903572; P:positive regulation of protein kinase D signaling; ISS:UniProtKB.
DR GO; GO:1902966; P:positive regulation of protein localization to early endosome; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:0002092; P:positive regulation of receptor internalization; ISS:UniProtKB.
DR GO; GO:1902336; P:positive regulation of retinal ganglion cell axon guidance; IMP:BHF-UCL.
DR GO; GO:0009967; P:positive regulation of signal transduction; ISO:MGI.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0061419; P:positive regulation of transcription from RNA polymerase II promoter in response to hypoxia; ISO:MGI.
DR GO; GO:1901165; P:positive regulation of trophoblast cell migration; ISO:MGI.
DR GO; GO:0043117; P:positive regulation of vascular permeability; IDA:MGI.
DR GO; GO:0031077; P:post-embryonic camera-type eye development; IMP:MGI.
DR GO; GO:0060319; P:primitive erythrocyte differentiation; IMP:MGI.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:0045601; P:regulation of endothelial cell differentiation; IDA:MGI.
DR GO; GO:0040008; P:regulation of growth; IMP:MGI.
DR GO; GO:1901532; P:regulation of hematopoietic progenitor cell differentiation; IDA:MGI.
DR GO; GO:0010749; P:regulation of nitric oxide mediated signal transduction; ISO:MGI.
DR GO; GO:0090259; P:regulation of retinal ganglion cell axon guidance; IDA:BHF-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
DR GO; GO:0002040; P:sprouting angiogenesis; IDA:BHF-UCL.
DR GO; GO:0043129; P:surfactant homeostasis; IMP:MGI.
DR GO; GO:0042088; P:T-helper 1 type immune response; ISO:MGI.
DR GO; GO:0035148; P:tube formation; ISS:UniProtKB.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0036324; P:vascular endothelial growth factor receptor-2 signaling pathway; ISO:MGI.
DR GO; GO:0038084; P:vascular endothelial growth factor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0061042; P:vascular wound healing; ISO:MGI.
DR GO; GO:0001944; P:vasculature development; IMP:MGI.
DR GO; GO:0042311; P:vasodilation; IDA:MGI.
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 Alternative initiation; Alternative promoter usage; Alternative splicing;
KW Angiogenesis; Cell membrane; Developmental protein; Differentiation;
KW Disulfide bond; Glycoprotein; Growth factor; Heparin-binding; Membrane;
KW Mitogen; Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000250"
FT CHAIN 27..214
FT /note="Vascular endothelial growth factor A"
FT /id="PRO_0000023388"
FT REGION 131..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 51..93
FT /evidence="ECO:0000250"
FT DISULFID 76
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 82..127
FT /evidence="ECO:0000250"
FT DISULFID 85
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 86..129
FT /evidence="ECO:0000250"
FT VAR_SEQ 1
FT /note="M -> MTDRQTDTAPSPSAHLLAGGLPTVDAAASREEPKPAPGGGVEGVGAR
FT GIARKLFVQLLGSSRSVVAVVCAAGDKPIGAGRSASSGLEKPGPEKRGEEEKEEERGPQ
FT WALGSQEPSSWTGEAAVCADSAPAARAPQAPARASVPEGRGARQGAQESGLPRSPSRRG
FT SASRAGPGRASETM (in isoform L-VEGF-1)"
FT /evidence="ECO:0000305"
FT /id="VSP_038746"
FT VAR_SEQ 105..141
FT /note="IMRIKPHQSQHIGEMSFLQHSRCECRPKKDRTKPEKK -> VGTCGTGDGAG
FT AGGGRRTVVQGGALEGCLGLCLGNFW (in isoform VEGF-4)"
FT /evidence="ECO:0000303|PubMed:9446618"
FT /id="VSP_016418"
FT VAR_SEQ 105..128
FT /note="IMRIKPHQSQHIGEMSFLQHSRCE -> VGTCGTGDGAGAGGAGGQWYKEGH
FT (in isoform VEGF-5)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_016419"
FT VAR_SEQ 129..214
FT /note="Missing (in isoform VEGF-5)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_016420"
FT VAR_SEQ 140
FT /note="K -> N (in isoform VEGF-1 and isoform L-VEGF-1)"
FT /evidence="ECO:0000303|PubMed:1592003,
FT ECO:0000303|PubMed:1644816"
FT /id="VSP_004626"
FT VAR_SEQ 141..208
FT /note="Missing (in isoform VEGF-2)"
FT /evidence="ECO:0000303|PubMed:1592003"
FT /id="VSP_004628"
FT VAR_SEQ 141..164
FT /note="Missing (in isoform VEGF-1 and isoform L-VEGF-1)"
FT /evidence="ECO:0000303|PubMed:1592003,
FT ECO:0000303|PubMed:1644816"
FT /id="VSP_004627"
FT VAR_SEQ 142..214
FT /note="Missing (in isoform VEGF-4)"
FT /evidence="ECO:0000303|PubMed:9446618"
FT /id="VSP_016421"
FT CONFLICT 61
FT /note="F -> I (in Ref. 3; AAC05442)"
FT /evidence="ECO:0000305"
FT CONFLICT 117..118
FT /note="GE -> ER (in Ref. 2; AAA40547)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 214 AA; 25283 MW; B5540B51E4BB6E17 CRC64;
MNFLLSWVHW TLALLLYLHH AKWSQAAPTT EGEQKSHEVI KFMDVYQRSY CRPIETLVDI
FQEYPDEIEY IFKPSCVPLM RCAGCCNDEA LECVPTSESN ITMQIMRIKP HQSQHIGEMS
FLQHSRCECR PKKDRTKPEK KSVRGKGKGQ KRKRKKSRFK SWSVHCEPCS ERRKHLFVQD
PQTCKCSCKN TDSRCKARQL ELNERTCRCD KPRR
