ID   TXVE_BITAR              Reviewed;         150 AA.
AC   C0K3N1;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Snake venom vascular endothelial growth factor toxin barietin {ECO:0000303|PubMed:19208624};
DE            Short=svVEGF;
DE   AltName: Full=VEGF-F {ECO:0000250|UniProtKB:P0DL42};
DE   Flags: Precursor;
OS   Bitis arietans (African puff adder).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Bitis.
OX   NCBI_TaxID=8692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-29, SUBUNIT, INTERACTION
RP   WITH KDR AND FLT1, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and 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: Induces capillary permeability and angiogenesis through VEGF
CC       receptor (KDR/VEGFR-2) signaling. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with high affinity with
CC       VEGF receptor-2 (KDR), and with a lower affinity with VEGF receptor-1
CC       (FLT1). Does not bind VEGF receptor-3 (FLT4) and neuropilin-1 (NRP1).
CC       {ECO:0000269|PubMed:19208624}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19208624}.
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}.
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DR   EMBL; FJ554635; ACN22038.1; -; mRNA.
DR   AlphaFoldDB; C0K3N1; -.
DR   SMR; C0K3N1; -.
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; Signal; Toxin.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:19208624"
FT   CHAIN           25..121
FT                   /note="Snake venom vascular endothelial growth factor toxin
FT                   barietin"
FT                   /id="PRO_5000452060"
FT   PROPEP          122..150
FT                   /id="PRO_0000406348"
FT   REGION          119..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         25
FT                   /note="Pyrrolidone carboxylic acid (Glu)"
FT                   /evidence="ECO:0000250|UniProtKB:P0DL42"
FT   DISULFID        38..80
FT                   /evidence="ECO:0000250"
FT   DISULFID        63
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   DISULFID        69..115
FT                   /evidence="ECO:0000250"
FT   DISULFID        72
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   DISULFID        73..117
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   150 AA;  16623 MW;  82BD24404458E41B CRC64;
     MAAYLLAVAI LFCIQGWPSG TVQGEVRPFM EVYQRSVCQP RETLVSILEE YPDKISKIFR
     PSCVAVLRCG GCCSDESLTC TSVGERTVEL QVMQVTPKTL SSKIKVMKFR EHTACECRPR
     SGSRVNIGKH KRSPEEGERE PSSPLTPGSL