VEGFA_MESAU
ID VEGFA_MESAU Reviewed; 190 AA.
AC Q99PS1;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 91.
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 Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Decidua, and Embryo;
RX PubMed=10382276; DOI=10.1007/s004410051294;
RA Yi X.J., Jiang H.Y., Lee K.K., Tang P.L., Chow P.H.;
RT "Expression of vascular endothelial growth factor (VEGF) and its receptors
RT during embryonic implantation in the golden hamster (Mesocricetus
RT auratus).";
RL Cell Tissue Res. 296:339-349(1999).
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 -!- 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 -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
CC {ECO:0000305}.
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DR EMBL; AF063013; AAK00049.1; -; mRNA.
DR RefSeq; NP_001268772.1; NM_001281843.1.
DR AlphaFoldDB; Q99PS1; -.
DR SMR; Q99PS1; -.
DR STRING; 10036.XP_005072384.1; -.
DR GeneID; 101839822; -.
DR CTD; 7422; -.
DR eggNOG; ENOG502QVI8; Eukaryota.
DR OrthoDB; 1364454at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0097475; P:motor neuron migration; ISS:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
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:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; 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:0035148; P:tube formation; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Angiogenesis; Developmental protein; Differentiation; Disulfide bond;
KW Glycoprotein; Growth factor; Heparin-binding; Mitogen; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000250"
FT CHAIN 27..190
FT /note="Vascular endothelial growth factor A"
FT /id="PRO_0000023387"
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"
SQ SEQUENCE 190 AA; 22277 MW; F00C5A8EA79A465F CRC64;
MNFLLSWVHW TLALLLYLHH AKWSQAAPTT EGEQKAHGVV EFMDVYRRSY CHPIETLVDI
FQEYPDEIEY IFKPSCVPLM RCGGCCSDEA LECVPTSESN ITMQIMRVKP HQSQHIGEMS
FLQHSRCECR PKKVRTKPEN HCEPCSERRK HLFVQDPQTC KCSCKNTDSR CKARQLELNE
RTCRCDKPRR
