TXVE_VIPAA
ID TXVE_VIPAA Reviewed; 145 AA.
AC P67863; C0K3N8;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 2.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Snake venom vascular endothelial growth factor toxin vammin;
DE Short=svVEGF;
DE AltName: Full=VEGF-F {ECO:0000250|UniProtKB:P0DL42};
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).
RN [2]
RP PROTEIN SEQUENCE OF 25-110, INTERACTION WITH KDR, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), DISULFIDE BONDS, SUBCELLULAR
RP LOCATION, AND PYROGLUTAMATE FORMATION AT GLN-25.
RC TISSUE=Venom;
RX PubMed=15542594; DOI=10.1074/jbc.m411395200;
RA Suto K., Yamazaki Y., Morita T., Mizuno H.;
RT "Crystal structures of novel vascular endothelial growth factors (VEGF)
RT from snake venoms: insight into selective VEGF binding to kinase insert
RT domain-containing receptor but not to fms-like tyrosine kinase-1.";
RL J. Biol. Chem. 280:2126-2131(2005).
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. May also induce capillary
CC permeability.
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:14600159, ECO:0000269|PubMed:15542594}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14600159,
CC ECO:0000269|PubMed:15542594}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:15542594}.
CC -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family. Snake venom
CC VEGF subfamily. {ECO:0000305}.
CC -!- CAUTION: 1WQ8 PDB entry indicates an origin from V.aspis aspis, whereas
CC PubMed:15542594 that mentions 1WQ8 indicates an origin from V.ammodytes
CC ammodytes. {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; FJ554642; ACN22045.1; -; mRNA.
DR PDB; 1WQ8; X-ray; 1.90 A; A=26-134.
DR PDBsum; 1WQ8; -.
DR AlphaFoldDB; P67863; -.
DR SMR; P67863; -.
DR EvolutionaryTrace; P67863; -.
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 3D-structure; Direct protein sequencing; Disulfide bond; Growth factor;
KW Pyrrolidone carboxylic acid; Secreted; Signal; Toxin.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..134
FT /note="Snake venom vascular endothelial growth factor toxin
FT vammin"
FT /id="PRO_0000162363"
FT PROPEP 135..145
FT /id="PRO_0000406345"
FT REGION 118..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:15542594"
FT DISULFID 38..80
FT /evidence="ECO:0000269|PubMed:15542594"
FT DISULFID 63
FT /note="Interchain (with C-72)"
FT /evidence="ECO:0000269|PubMed:15542594"
FT DISULFID 69..115
FT /evidence="ECO:0000269|PubMed:15542594"
FT DISULFID 72
FT /note="Interchain (with C-63)"
FT /evidence="ECO:0000269|PubMed:15542594"
FT DISULFID 73..117
FT /evidence="ECO:0000269|PubMed:15542594"
FT HELIX 29..36
FT /evidence="ECO:0007829|PDB:1WQ8"
FT STRAND 37..46
FT /evidence="ECO:0007829|PDB:1WQ8"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:1WQ8"
FT STRAND 56..70
FT /evidence="ECO:0007829|PDB:1WQ8"
FT STRAND 79..95
FT /evidence="ECO:0007829|PDB:1WQ8"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:1WQ8"
FT STRAND 102..118
FT /evidence="ECO:0007829|PDB:1WQ8"
SQ SEQUENCE 145 AA; 16307 MW; 359E5ED852FA1779 CRC64;
MAAYLLAVAI LFCIQGWPSG TVQGQVRPFL EVHERSACQA RETLVPILQE YPDEISDIFR
PSCVAVLRCS GCCTDESLKC TPVGKHTVDL QIMRVNPRTQ SSKMEVMKFT EHTACECRPR
RKQGEPDGPK EKPRRGGVRA RFPFV
