VEGFA_SHEEP
ID VEGFA_SHEEP Reviewed; 146 AA.
AC P50412;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 99.
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 Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=8958842; DOI=10.1530/jrf.0.1080157;
RA Redmer D.A., Dai Y., Li J., Charnock-Jones D.S., Smith S.K., Reynolds L.P.,
RA Moor R.M.;
RT "Characterization and expression of vascular endothelial growth factor
RT (VEGF) in the ovine corpus luteum.";
RL J. Reprod. Fertil. 108:157-165(1996).
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 -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
CC {ECO:0000305}.
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DR EMBL; X89506; CAA61677.1; -; mRNA.
DR PIR; S57956; S57956.
DR RefSeq; NP_001020281.1; NM_001025110.1.
DR AlphaFoldDB; P50412; -.
DR SMR; P50412; -.
DR STRING; 9940.ENSOARP00000008938; -.
DR GeneID; 443103; -.
DR KEGG; oas:443103; -.
DR CTD; 7422; -.
DR eggNOG; ENOG502QVI8; Eukaryota.
DR OrthoDB; 1364454at2759; -.
DR Proteomes; UP000002356; Unplaced.
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; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR023581; PD_growth_factor_CS.
DR InterPro; IPR000072; PDGF/VEGF_dom.
DR Pfam; PF00341; PDGF; 1.
DR SMART; SM00141; PDGF; 1.
DR SUPFAM; SSF57501; SSF57501; 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 Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000250"
FT CHAIN 27..146
FT /note="Vascular endothelial growth factor A"
FT /id="PRO_0000023391"
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 146 AA; 17247 MW; 4E792CB557F91760 CRC64;
MNFLLSWVHW SLALLLYLHH AKWSQAAPMA EGGQKPHEVM KFMDVYQRSF CRPIETLVDI
FQEYPDEIEF IFKPSCVPLM RCGGCCNDES LECVPTEEFN ITMQIMRIKP HQSQHIGEMS
FLQHNKCECR PKKDKARQEK CDKPRR