ID   VEGFA_VIPAA             Reviewed;         192 AA.
AC   C0K3N5;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=Vascular endothelial growth factor A;
DE   Flags: Precursor;
OS   Vipera ammodytes ammodytes (Western sand viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Vipera.
OX   NCBI_TaxID=8705;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=19208624; DOI=10.1074/jbc.m809071200;
RA   Yamazaki Y., Matsunaga Y., Tokunaga Y., Obayashi S., Saito M., Morita T.;
RT   "Snake venom vascular endothelial growth factors (VEGF-Fs) exclusively vary
RT   their structures and functions among species.";
RL   J. Biol. Chem. 284:9885-9891(2009).
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. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. Also found as heterodimer with
CC       PGF Interacts with FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan
CC       sulfate and heparin. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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; FJ554639; ACN22042.1; -; mRNA.
DR   AlphaFoldDB; C0K3N5; -.
DR   SMR; C0K3N5; -.
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   2: Evidence at transcript level;
KW   Angiogenesis; Developmental protein; Differentiation; Disulfide bond;
KW   Glycoprotein; Growth factor; Heparin-binding; Mitogen; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..192
FT                   /note="Vascular endothelial growth factor A"
FT                   /id="PRO_5000452064"
FT   CARBOHYD        101
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        52..94
FT                   /evidence="ECO:0000250"
FT   DISULFID        77
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   DISULFID        83..128
FT                   /evidence="ECO:0000250"
FT   DISULFID        86
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   DISULFID        87..130
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   192 AA;  22460 MW;  67724F020E0432E2 CRC64;
     MNFLLSWIHW GLAALLYFHN AKVLQAAPAQ GDGDRQQGEV ISFLTVYERS ACRPVETMVD
     IFQEYPDEVE YIFKPSCVAL MRCGGCCNDE ALECVPTEVY NVTMEIMKLK PFQSQHIHPM
     SFQQHSKCEC RPKKEVRIRQ ENHCEPCSER RKHLYKQDPL TCKCSCKFTD SRCKSKQLEL
     NERTCRCEKP RR