VEGFA_RAT
ID VEGFA_RAT Reviewed; 214 AA.
AC P16612; Q541S6; Q91ZE1; Q9JKX7; Q9QXG6; Q9QXG7;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 182.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF-A164), AND PROTEIN SEQUENCE OF
RP 27-190.
RX PubMed=2320579; DOI=10.1073/pnas.87.7.2628;
RA Conn G., Bayne M.L., Soderman D.D., Kwok P.W., Sullivan K.A., Palisi T.M.,
RA Hope D.A., Thomas K.A.;
RT "Amino acid and cDNA sequences of a vascular endothelial cell mitogen that
RT is homologous to platelet-derived growth factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:2628-2633(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS VEGF-A188; VEGF-A164; VEGF-A144 AND
RP VEGF-A120).
RX PubMed=11163598; DOI=10.1016/s0003-9969(00)00081-9;
RA Ishii H., Oota I., Takuma T., Inomata K.;
RT "Developmental expression of vascular endothelial growth factor in the
RT masseter muscle of rats.";
RL Arch. Oral Biol. 46:77-82(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS VEGF-A164 AND VEGF-A188).
RC STRAIN=Sprague-Dawley;
RA Marion S., Lee T.-C.;
RT "Cloning of multiple VEGF splice variants from hypoxic neonatal rat
RT cardiomyocytes.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 27-40, AND SUBUNIT.
RC TISSUE=Glial tumor;
RX PubMed=7706320; DOI=10.1074/jbc.270.13.7717;
RA DiSalvo J., Bayne M.L., Conn G., Kwok P.W., Trivedi P.G., Soderman D.D.,
RA Palisi T.M., Sullivan K.A., Thomas K.A.;
RT "Purification and characterization of a naturally occurring vascular
RT endothelial growth factor.placenta growth factor heterodimer.";
RL J. Biol. Chem. 270:7717-7723(1995).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND 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).
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. Binding to NRP1 receptor 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 (By similarity).
CC {ECO:0000250|UniProtKB:P15692, ECO:0000250|UniProtKB:Q00731,
CC ECO:0000269|PubMed:10878616}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:7706320). Also found as
CC heterodimer with PGF (PubMed:7706320). Interacts with NRP1 (By
CC similarity). Interacts with isoform 2 of BSG (By similarity).
CC {ECO:0000250|UniProtKB:P15692, ECO:0000269|PubMed:7706320}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=VEGF-A120 is acidic
CC and freely secreted. VEGF-A164 is more basic, has heparin-binding
CC properties and, although a significant proportion remains cell-
CC associated, most is freely secreted. VEGF-A188 is very basic, it is
CC cell-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 (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=VEGF-A188;
CC IsoId=P16612-1; Sequence=Displayed;
CC Name=VEGF-A164;
CC IsoId=P16612-2; Sequence=VSP_004629, VSP_004630;
CC Name=VEGF-A144;
CC IsoId=P16612-3; Sequence=VSP_004632;
CC Name=VEGF-A120;
CC IsoId=P16612-4; Sequence=VSP_004631;
CC -!- TISSUE SPECIFICITY: Expressed in the pituitary, in brain, in
CC particularly in supraoptic and paraventricular nuclei and the choroid
CC plexus. Also found abundantly in the corpus luteum of the ovary and in
CC kidney glomeruli. Expressed in the ductal epithelial cells of post-
CC pubertal mammary glands. Expressed in the ductal and alveolar
CC epithelial cells throughout the whole period of gestational evolution,
CC lactation and involution. {ECO:0000269|PubMed:10878616}.
CC -!- DEVELOPMENTAL STAGE: Increases during pregnancy (5.0-fold increase on
CC day 12 with a subsequent decrease on day 18) and during lactation
CC (18.5-fold increase on day 7). Levels appear to be minimally altered
CC during involution. {ECO:0000269|PubMed:10878616}.
CC -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M32167; AAA41211.1; -; mRNA.
DR EMBL; AF215725; AAF19211.1; -; mRNA.
DR EMBL; AF215726; AAF19212.1; -; mRNA.
DR EMBL; AF222779; AAF25958.1; -; mRNA.
DR EMBL; AY033506; AAL07526.1; -; mRNA.
DR EMBL; AY033508; AAL07528.1; -; mRNA.
DR PIR; A35987; A35987.
DR RefSeq; NP_001103804.1; NM_001110334.2.
DR RefSeq; NP_001274036.1; NM_001287107.1. [P16612-1]
DR RefSeq; NP_001274037.1; NM_001287108.1. [P16612-2]
DR RefSeq; NP_001274039.1; NM_001287110.1. [P16612-4]
DR RefSeq; NP_001274040.1; NM_001287111.1.
DR RefSeq; NP_001274041.1; NM_001287112.1. [P16612-3]
DR RefSeq; NP_001274043.1; NM_001287114.1.
DR RefSeq; NP_114024.2; NM_031836.3.
DR AlphaFoldDB; P16612; -.
DR SMR; P16612; -.
DR BioGRID; 249830; 2.
DR STRING; 10116.ENSRNOP00000026637; -.
DR GlyGen; P16612; 1 site.
DR PhosphoSitePlus; P16612; -.
DR PaxDb; P16612; -.
DR ABCD; P16612; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000044163; ENSRNOP00000050127; ENSRNOG00000019598. [P16612-4]
DR GeneID; 83785; -.
DR KEGG; rno:83785; -.
DR UCSC; RGD:619991; rat. [P16612-1]
DR CTD; 7422; -.
DR RGD; 619991; Vegfa.
DR eggNOG; ENOG502QVI8; Eukaryota.
DR GeneTree; ENSGT00940000157284; -.
DR InParanoid; P16612; -.
DR OrthoDB; 1364454at2759; -.
DR PhylomeDB; P16612; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-194313; VEGF ligand-receptor interactions.
DR Reactome; R-RNO-195399; VEGF binds to VEGFR leading to receptor dimerization.
DR Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-RNO-5218921; VEGFR2 mediated cell proliferation.
DR PRO; PR:P16612; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Genevisible; P16612; RN.
DR GO; GO:0005912; C:adherens junction; ISO:RGD.
DR GO; GO:0005604; C:basement membrane; IDA:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0030141; C:secretory granule; ISO:RGD.
DR GO; GO:0031982; C:vesicle; IDA:RGD.
DR GO; GO:0042056; F:chemoattractant activity; IMP:RGD.
DR GO; GO:0005125; F:cytokine activity; ISO:RGD.
DR GO; GO:0001968; F:fibronectin binding; ISO:RGD.
DR GO; GO:0008083; F:growth factor activity; IDA:RGD.
DR GO; GO:0019838; F:growth factor binding; IPI:RGD.
DR GO; GO:0008201; F:heparin binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0005161; F:platelet-derived growth factor receptor binding; ISO:RGD.
DR GO; GO:0048018; F:receptor ligand activity; ISO:RGD.
DR GO; GO:0043183; F:vascular endothelial growth factor receptor 1 binding; ISO:RGD.
DR GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; IMP:RGD.
DR GO; GO:0005172; F:vascular endothelial growth factor receptor binding; ISO:RGD.
DR GO; GO:0032147; P:activation of protein kinase activity; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0001525; P:angiogenesis; IMP:RGD.
DR GO; GO:0060978; P:angiogenesis involved in coronary vascular morphogenesis; IMP:RGD.
DR GO; GO:0048844; P:artery morphogenesis; ISO:RGD.
DR GO; GO:0001568; P:blood vessel development; ISO:RGD.
DR GO; GO:0048514; P:blood vessel morphogenesis; ISO:RGD.
DR GO; GO:0001974; P:blood vessel remodeling; IMP:RGD.
DR GO; GO:0060346; P:bone trabecula formation; ISO:RGD.
DR GO; GO:0061430; P:bone trabecula morphogenesis; ISO:RGD.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; ISO:RGD.
DR GO; GO:0048593; P:camera-type eye morphogenesis; ISO:RGD.
DR GO; GO:0055013; P:cardiac muscle cell development; ISO:RGD.
DR GO; GO:0060948; P:cardiac vascular smooth muscle cell development; ISO:RGD.
DR GO; GO:0060326; P:cell chemotaxis; IMP:RGD.
DR GO; GO:0048469; P:cell maturation; ISO:RGD.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; ISO:RGD.
DR GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEP:RGD.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEP:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; ISO:RGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; ISO:RGD.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0097533; P:cellular stress response to acid chemical; ISO:RGD.
DR GO; GO:0071679; P:commissural neuron axon guidance; ISO:RGD.
DR GO; GO:0060982; P:coronary artery morphogenesis; ISO:RGD.
DR GO; GO:0003169; P:coronary vein morphogenesis; ISO:RGD.
DR GO; GO:0071542; P:dopaminergic neuron differentiation; ISO:RGD.
DR GO; GO:0035767; P:endothelial cell chemotaxis; ISO:RGD.
DR GO; GO:0043542; P:endothelial cell migration; ISO:RGD.
DR GO; GO:0001935; P:endothelial cell proliferation; ISO:RGD.
DR GO; GO:0030855; P:epithelial cell differentiation; ISO:RGD.
DR GO; GO:0042462; P:eye photoreceptor cell development; ISO:RGD.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0003007; P:heart morphogenesis; ISO:RGD.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0050930; P:induction of positive chemotaxis; IBA:GO_Central.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
DR GO; GO:0007595; P:lactation; ISO:RGD.
DR GO; GO:0048286; P:lung alveolus development; IMP:RGD.
DR GO; GO:0030324; P:lung development; ISO:RGD.
DR GO; GO:0060426; P:lung vasculature development; ISO:RGD.
DR GO; GO:0036303; P:lymph vessel morphogenesis; ISO:RGD.
DR GO; GO:0001946; P:lymphangiogenesis; ISO:RGD.
DR GO; GO:0030225; P:macrophage differentiation; ISO:RGD.
DR GO; GO:0060749; P:mammary gland alveolus development; ISO:RGD.
DR GO; GO:0007498; P:mesoderm development; ISO:RGD.
DR GO; GO:0030224; P:monocyte differentiation; ISO:RGD.
DR GO; GO:0097475; P:motor neuron migration; ISS:UniProtKB.
DR GO; GO:0048255; P:mRNA stabilization; IDA:RGD.
DR GO; GO:1903392; P:negative regulation of adherens junction organization; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:1905604; P:negative regulation of blood-brain barrier permeability; ISO:RGD.
DR GO; GO:0045779; P:negative regulation of bone resorption; IMP:RGD.
DR GO; GO:0022408; P:negative regulation of cell-cell adhesion; ISO:RGD.
DR GO; GO:2000048; P:negative regulation of cell-cell adhesion mediated by cadherin; ISO:RGD.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; ISO:RGD.
DR GO; GO:1903141; P:negative regulation of establishment of endothelial barrier; ISO:RGD.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:1901215; P:negative regulation of neuron death; IMP:RGD.
DR GO; GO:0043069; P:negative regulation of programmed cell death; IMP:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0007399; P:nervous system development; IDA:RGD.
DR GO; GO:0003151; P:outflow tract morphogenesis; ISO:RGD.
DR GO; GO:0001541; P:ovarian follicle development; ISO:RGD.
DR GO; GO:0050918; P:positive chemotaxis; ISO:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA:RGD.
DR GO; GO:0048842; P:positive regulation of axon extension involved in axon guidance; ISO:RGD.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:RGD.
DR GO; GO:1903589; P:positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; ISO:RGD.
DR GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; ISO:RGD.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISO:RGD.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0038091; P:positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0038033; P:positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISO:RGD.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:1901727; P:positive regulation of histone deacetylase activity; ISO:RGD.
DR GO; GO:1901492; P:positive regulation of lymphangiogenesis; ISO:RGD.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:RGD.
DR GO; GO:0060754; P:positive regulation of mast cell chemotaxis; IBA:GO_Central.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; ISO:RGD.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:RGD.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; ISO:RGD.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:1900086; P:positive regulation of peptidyl-tyrosine autophosphorylation; ISO:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:RGD.
DR GO; GO:0042327; P:positive regulation of phosphorylation; ISO:RGD.
DR GO; GO:0050927; P:positive regulation of positive chemotaxis; ISO:RGD.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; ISO:RGD.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:RGD.
DR GO; GO:0090037; P:positive regulation of protein kinase C signaling; ISO:RGD.
DR GO; GO:1903572; P:positive regulation of protein kinase D signaling; ISO:RGD.
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; ISO:RGD.
DR GO; GO:1902336; P:positive regulation of retinal ganglion cell axon guidance; ISO:RGD.
DR GO; GO:0009967; P:positive regulation of signal transduction; IDA:RGD.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:RGD.
DR GO; GO:0061419; P:positive regulation of transcription from RNA polymerase II promoter in response to hypoxia; ISO:RGD.
DR GO; GO:1901165; P:positive regulation of trophoblast cell migration; ISO:RGD.
DR GO; GO:0043117; P:positive regulation of vascular permeability; IMP:RGD.
DR GO; GO:0031077; P:post-embryonic camera-type eye development; ISO:RGD.
DR GO; GO:0060319; P:primitive erythrocyte differentiation; ISO:RGD.
DR GO; GO:0008360; P:regulation of cell shape; ISO:RGD.
DR GO; GO:0045601; P:regulation of endothelial cell differentiation; ISO:RGD.
DR GO; GO:0040008; P:regulation of growth; ISO:RGD.
DR GO; GO:1901532; P:regulation of hematopoietic progenitor cell differentiation; ISO:RGD.
DR GO; GO:0010749; P:regulation of nitric oxide mediated signal transduction; ISO:RGD.
DR GO; GO:0090259; P:regulation of retinal ganglion cell axon guidance; ISO:RGD.
DR GO; GO:0009409; P:response to cold; IEP:RGD.
DR GO; GO:0071548; P:response to dexamethasone; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0051593; P:response to folic acid; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IDA:RGD.
DR GO; GO:0070482; P:response to oxygen levels; IEP:RGD.
DR GO; GO:0032570; P:response to progesterone; IEP:RGD.
DR GO; GO:0033189; P:response to vitamin A; IEP:RGD.
DR GO; GO:0002040; P:sprouting angiogenesis; ISO:RGD.
DR GO; GO:0043129; P:surfactant homeostasis; ISO:RGD.
DR GO; GO:0042088; P:T-helper 1 type immune response; IDA:RGD.
DR GO; GO:0035148; P:tube formation; ISS:UniProtKB.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IMP:RGD.
DR GO; GO:0036324; P:vascular endothelial growth factor receptor-2 signaling pathway; ISO:RGD.
DR GO; GO:0038084; P:vascular endothelial growth factor signaling pathway; ISO:RGD.
DR GO; GO:0061042; P:vascular wound healing; ISO:RGD.
DR GO; GO:0001944; P:vasculature development; ISO:RGD.
DR GO; GO:0042311; P:vasodilation; ISO:RGD.
DR GO; GO:0038190; P:VEGF-activated neuropilin signaling pathway; ISO:RGD.
DR GO; GO:0042060; P:wound healing; IEP:RGD.
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 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:2320579,
FT ECO:0000269|PubMed:7706320"
FT CHAIN 27..214
FT /note="Vascular endothelial growth factor A"
FT /id="PRO_0000023390"
FT REGION 131..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..159
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
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 140
FT /note="K -> N (in isoform VEGF-A164)"
FT /evidence="ECO:0000303|PubMed:11163598,
FT ECO:0000303|PubMed:2320579, ECO:0000303|Ref.3"
FT /id="VSP_004629"
FT VAR_SEQ 141..208
FT /note="Missing (in isoform VEGF-A120)"
FT /evidence="ECO:0000303|PubMed:11163598"
FT /id="VSP_004631"
FT VAR_SEQ 141..164
FT /note="Missing (in isoform VEGF-A164)"
FT /evidence="ECO:0000303|PubMed:11163598,
FT ECO:0000303|PubMed:2320579, ECO:0000303|Ref.3"
FT /id="VSP_004630"
FT VAR_SEQ 165..208
FT /note="Missing (in isoform VEGF-A144)"
FT /evidence="ECO:0000303|PubMed:11163598"
FT /id="VSP_004632"
FT CONFLICT 101
FT /note="V -> A (in Ref. 2; AAF19212)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 214 AA; 25239 MW; 60FBB876F5304946 CRC64;
MNFLLSWVHW TLALLLYLHH AKWSQAAPTT EGEQKAHEVV KFMDVYQRSY CRPIETLVDI
FQEYPDEIEY IFKPSCVPLM RCAGCCNDEA LECVPTSESN VTMQIMRIKP HQSQHIGEMS
FLQHSRCECR PKKDRTKPEK KSVRGKGKGQ KRKRKKSRFK SWSVHCEPCS ERRKHLFVQD
PQTCKCSCKN TDSRCKARQL ELNERTCRCD KPRR
