ID   TXVE_VIPAP              Reviewed;         110 AA.
AC   P83942;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Snake venom vascular endothelial growth factor toxin HF;
DE            Short=svVEGF;
DE   AltName: Full=Heparin-binding dimeric hypotensive factor;
DE   AltName: Full=VEGF-F {ECO:0000250|UniProtKB:P0DL42};
OS   Vipera aspis aspis (Aspic viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Vipera.
OX   NCBI_TaxID=194601;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, MASS SPECTROMETRY, PYROGLUTAMATE FORMATION AT GLN-1, AND
RP   VARIANT TRP-62.
RC   TISSUE=Venom;
RX   PubMed=10512636; DOI=10.1021/bi990562z;
RA   Komori Y., Nikai T., Taniguchi K., Masuda K., Sugihara H.;
RT   "Vascular endothelial growth factor VEGF-like heparin-binding protein from
RT   the venom of Vipera aspis aspis (Aspic viper).";
RL   Biochemistry 38:11796-11803(1999).
RN   [2]
RP   FUNCTION, AND INTERACTION WITH KDR.
RX   PubMed=14600159; DOI=10.1074/jbc.c300454200;
RA   Yamazaki Y., Takani K., Atoda H., Morita T.;
RT   "Snake venom vascular endothelial growth factors (VEGFs) exhibit potent
RT   activity through their specific recognition of KDR (VEGF receptor 2).";
RL   J. Biol. Chem. 278:51985-51988(2003).
CC   -!- FUNCTION: Induces angiogenesis, probably through VEGF receptor
CC       (KDR/VEGFR-2) signaling, as well as drastic hypotension. The
CC       hypotension is mediated by nitric oxide (NO), which is produced by
CC       VEGF-activated endothelium NO synthase. Increases capillary
CC       permeability when injected intradermally into rat.
CC       {ECO:0000269|PubMed:10512636, ECO:0000269|PubMed:14600159}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with VEGF receptor-2
CC       (KDR) with high affinity, but not with VEGF receptor-1 (Flt-1), VEGF
CC       receptor-3 (FLT4), and neuropilin-1 (NRP1).
CC       {ECO:0000269|PubMed:10512636, ECO:0000269|PubMed:14600159}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10512636}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:10512636}.
CC   -!- MASS SPECTROMETRY: Mass=25071.1; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:10512636};
CC   -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family. Snake venom
CC       VEGF subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P83942; -.
DR   SMR; P83942; -.
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Growth factor;
KW   Pyrrolidone carboxylic acid; Secreted; Toxin.
FT   CHAIN           1..110
FT                   /note="Snake venom vascular endothelial growth factor toxin
FT                   HF"
FT                   /id="PRO_0000162364"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:10512636"
FT   DISULFID        14..56
FT                   /evidence="ECO:0000250|UniProtKB:P15692"
FT   DISULFID        39
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:P15692"
FT   DISULFID        45..91
FT                   /evidence="ECO:0000250|UniProtKB:P15692"
FT   DISULFID        48
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:P15692"
FT   DISULFID        49..93
FT                   /evidence="ECO:0000250|UniProtKB:P15692"
FT   VARIANT         62
FT                   /note="H -> W"
FT                   /evidence="ECO:0000269|PubMed:10512636"
SQ   SEQUENCE   110 AA;  12561 MW;  E858EE393E5A1B48 CRC64;
     QVRPFLEVHE RSACQARETL VSILQEYPDE ISDIFRPSCV AVLRCSGCCT DESLKCTPVG
     KHTVDLQIMR VNPRTQSSKM EVMKFTEHTA CECRPRRKQG EPDGPKEKPR