ID   VEGFA_BITGA             Reviewed;         191 AA.
AC   P83906;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Vascular endothelial growth factor A;
DE            Short=VEGF-A;
DE   AltName: Full=Vascular permeability factor;
DE            Short=VPF;
DE   Flags: Precursor;
OS   Bitis gabonica (Gaboon adder) (Gaboon viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Bitis.
OX   NCBI_TaxID=8694;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=15276202; DOI=10.1016/j.gene.2004.03.024;
RA   Francischetti I.M.B., My-Pham V., Harrison J., Garfield M.K.,
RA   Ribeiro J.M.C.;
RT   "Bitis gabonica (Gaboon viper) snake venom gland: toward a catalog for the
RT   full-length transcripts (cDNA) and proteins.";
RL   Gene 337:55-69(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 36-45; 109-127 AND 138-149, SUBCELLULAR LOCATION, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=17203976; DOI=10.1021/pr060494k;
RA   Calvete J.J., Marcinkiewicz C., Sanz L.;
RT   "Snake venomics of Bitis gabonica gabonica. Protein family composition,
RT   subunit organization of venom toxins, and characterization of dimeric
RT   disintegrins bitisgabonin-1 and bitisgabonin-2.";
RL   J. Proteome Res. 6:326-336(2007).
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 heparan sulfate and
CC       heparin. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. Also found as heterodimer with
CC       PGF. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17203976}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
CC       {ECO:0000305}.
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DR   EMBL; AY429481; AAR06855.1; -; mRNA.
DR   AlphaFoldDB; P83906; -.
DR   SMR; P83906; -.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
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:0031334; P:positive regulation of protein-containing complex assembly; 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   1: Evidence at protein level;
KW   Angiogenesis; Developmental protein; Differentiation;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Growth factor;
KW   Heparin-binding; Mitogen; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..191
FT                   /note="Vascular endothelial growth factor A"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000023395"
FT   CARBOHYD        101
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   DISULFID        52..94
FT                   /evidence="ECO:0000250|UniProtKB:P15692"
FT   DISULFID        77
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:P15692"
FT   DISULFID        83..128
FT                   /evidence="ECO:0000250|UniProtKB:P15692"
FT   DISULFID        86
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:P15692"
FT   DISULFID        87..130
FT                   /evidence="ECO:0000250|UniProtKB:P15692"
SQ   SEQUENCE   191 AA;  22358 MW;  259A0F0257924763 CRC64;
     MNFLLTWIHW GLAALLYFHN AKVLQAAPAQ GDGERQQGEV IPFLKVYERS ICRPVETMVD
     IFQEYPDEVE YIFKPSCVAL MRCGGCCNDE ALECVPTEMY NVTMEVMKLK PFQSQHIHPV
     SFQQHSKCEC RPKKDIRNKD NHCEPCSERR KHLYKQDPLT CKCSCKAPDL RCKSKQLELN
     ERTCRCERPR R