VEGFA_CANLF
ID VEGFA_CANLF Reviewed; 214 AA.
AC Q9MYV3; Q9XSF3; Q9XSF4; Q9XSF5;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF-188).
RX PubMed=10661874; DOI=10.1515/bc.1999.187;
RA Scheidegger P., Weiglhofer W., Suarez S., Kaser-Hotz B., Steiner R.,
RA Ballmer-Hofer K., Jaussi R.;
RT "Vascular endothelial growth factor (VEGF) and its receptors in tumor-
RT bearing dogs.";
RL Biol. Chem. 380:1449-1454(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS VEGF-188; VEGF-182 AND VEGF-164).
RC TISSUE=Heart;
RA Jingjing L., Roque R.S.;
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC Binding to NRP1 receptor initiates a signaling pathway needed for motor
CC neuron axon guidance and cell body migration, including for the caudal
CC migration of facial motor neurons from rhombomere 4 to rhombomere 6
CC during embryonic development (By similarity). Also binds the
CC DEAR/FBXW7-AS1 receptor (By similarity). {ECO:0000250|UniProtKB:P15692,
CC ECO:0000250|UniProtKB:Q00731}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Also found as
CC heterodimer with PGF (By similarity). Interacts with NRP1 (By
CC similarity). Interacts with BSG (By similarity).
CC {ECO:0000250|UniProtKB:P15692, ECO:0000250|UniProtKB:P16612}.
CC -!- INTERACTION:
CC Q9MYV3-3; P35968: KDR; Xeno; NbExp=2; IntAct=EBI-15622828, EBI-1005487;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Secreted but remains
CC associated to cells or to the extracellular matrix unless released by
CC heparin. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=VEGF-188;
CC IsoId=Q9MYV3-1; Sequence=Displayed;
CC Name=VEGF-182;
CC IsoId=Q9MYV3-2; Sequence=VSP_004617;
CC Name=VEGF-164;
CC IsoId=Q9MYV3-3; Sequence=VSP_004615, VSP_004616;
CC -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
CC {ECO:0000305}.
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DR EMBL; AJ133758; CAB82426.1; -; mRNA.
DR EMBL; AF133250; AAD29684.1; -; mRNA.
DR EMBL; AF133249; AAD29683.1; -; mRNA.
DR EMBL; AF133248; AAD29682.1; -; mRNA.
DR RefSeq; NP_001003175.2; NM_001003175.2. [Q9MYV3-1]
DR RefSeq; NP_001103971.1; NM_001110501.1. [Q9MYV3-2]
DR RefSeq; NP_001103972.1; NM_001110502.1. [Q9MYV3-3]
DR AlphaFoldDB; Q9MYV3; -.
DR BMRB; Q9MYV3; -.
DR SMR; Q9MYV3; -.
DR DIP; DIP-29294N; -.
DR IntAct; Q9MYV3; 1.
DR STRING; 9612.ENSCAFP00000041911; -.
DR PaxDb; Q9MYV3; -.
DR GeneID; 403802; -.
DR KEGG; cfa:403802; -.
DR CTD; 7422; -.
DR eggNOG; ENOG502QVI8; Eukaryota.
DR HOGENOM; CLU_042996_2_0_1; -.
DR InParanoid; Q9MYV3; -.
DR OrthoDB; 1364454at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0030141; C:secretory granule; ISS:UniProtKB.
DR GO; GO:0042056; F:chemoattractant activity; ISS:UniProtKB.
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:0008201; F:heparin binding; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; ISS:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; ISS:UniProtKB.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0035767; P:endothelial cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0050930; P:induction of positive chemotaxis; IBA:GO_Central.
DR GO; GO:0030225; P:macrophage differentiation; ISS:UniProtKB.
DR GO; GO:0030224; P:monocyte differentiation; ISS:UniProtKB.
DR GO; GO:0097475; P:motor neuron migration; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISS: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:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
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:0032793; P:positive regulation of CREB transcription factor activity; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:UniProtKB.
DR GO; GO:0060754; P:positive regulation of mast cell chemotaxis; IBA:GO_Central.
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; ISS:UniProtKB.
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: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: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:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
DR GO; GO:0002040; P:sprouting angiogenesis; IBA:GO_Central.
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:0038084; P:vascular endothelial growth factor signaling pathway; IBA:GO_Central.
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 Disulfide bond; Glycoprotein; Growth factor; Heparin-binding; Mitogen;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..214
FT /note="Vascular endothelial growth factor A"
FT /id="PRO_0000023384"
FT REGION 131..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..160
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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-164)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_004615"
FT VAR_SEQ 141..164
FT /note="Missing (in isoform VEGF-164)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_004616"
FT VAR_SEQ 159..164
FT /note="Missing (in isoform VEGF-182)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_004617"
FT CONFLICT 143
FT /note="I -> V (in Ref. 2; AAD29683/AAD29684)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="P -> S (in Ref. 2; AAD29683/AAD29684)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 214 AA; 25175 MW; 0AC980A158C44B27 CRC64;
MNFLLSWVHW SLALLLYLHH AKWSQAAPMA GGEHKPHEVV KFMDVYQRSY CRPIETLVDI
FQEYPDEIEY IFKPSCVPLM RCGGCCNDEG LECVPTEEFN ITMQIMRIKP HQGQHIGEMS
FLQHSKCECR PKKDRARQEK KSIRGKGKGQ KRKRKKSRYK PWSVPCGPCS ERRKHLFVQD
PQTCKCSCKN TDSRCKARQL ELNERTCRCD KPRR
