ID   TXVE_BOTJA              Reviewed;         146 AA.
AC   Q90X23;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Snake venom vascular endothelial growth factor toxin;
DE            Short=svVEGF;
DE   AltName: Full=VEGF-F {ECO:0000250|UniProtKB:P0DL42};
DE   Flags: Precursor;
OS   Bothrops jararaca (Jararaca) (Bothrops jajaraca).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=8724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom gland;
RX   PubMed=11517227; DOI=10.1074/jbc.m106531200;
RA   Junqueira de Azevedo I.L.M., Farsky S.H.P., Oliveira M.L.S., Ho P.L.;
RT   "Molecular cloning and expression of a functional snake venom vascular
RT   endothelium growth factor (VEGF) from the Bothrops insularis pit viper. A
RT   new member of the VEGF family of proteins.";
RL   J. Biol. Chem. 276:39836-39842(2001).
CC   -!- FUNCTION: Induces capillary permeability and angiogenesis through VEGF
CC       receptor (KDR/VEGFR-2) signaling. {ECO:0000250|UniProtKB:Q90X24}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:11517227}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11517227}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family. Snake venom
CC       VEGF subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY033152; AAK52103.1; -; mRNA.
DR   AlphaFoldDB; Q90X23; -.
DR   SMR; Q90X23; -.
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   Disulfide bond; Growth factor; Pyrrolidone carboxylic acid; Secreted;
KW   Signal; Toxin.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255, ECO:0000312|EMBL:AAK52103.1"
FT   CHAIN           25..146
FT                   /note="Snake venom vascular endothelial growth factor
FT                   toxin"
FT                   /id="PRO_0000023425"
FT   REGION          118..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         25
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:P83942"
FT   DISULFID        38..80
FT                   /evidence="ECO:0000250|UniProtKB:P15692"
FT   DISULFID        63
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:P15692"
FT   DISULFID        69..115
FT                   /evidence="ECO:0000250|UniProtKB:P15692"
FT   DISULFID        72
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:P15692"
FT   DISULFID        73..117
FT                   /evidence="ECO:0000250|UniProtKB:P15692"
SQ   SEQUENCE   146 AA;  16377 MW;  451EEF514EA9408E CRC64;
     MAVYLLAVAI LFCIQGWPLG TVQGQVMPFM EVYRHSVCQP RETLVSILEE YPGEISHIFR
     PSCVTALRCG GCCTDESLEC TATGKRSVGR EIMRLSPHKG TSEKEVMQFT EHTDCECRPR
     SASGVNSRKH KRNPEEGEPR AKFPFV