ID   TXVE2_PROMU             Reviewed;         143 AA.
AC   Q330K6;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Snake venom vascular endothelial growth factor toxin;
DE            Short=svVEGF;
DE   AltName: Full=PM-VEGF;
DE   AltName: Full=TM-VEGF;
DE   AltName: Full=VEGF-F {ECO:0000250|UniProtKB:P67862};
DE   Flags: Precursor;
OS   Protobothrops mucrosquamatus (Taiwan habu) (Trimeresurus mucrosquamatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX   NCBI_TaxID=103944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP   INTERACTION WITH FLT1 AND KDR.
RC   TISSUE=Venom gland;
RX   PubMed=15711751; DOI=10.1160/th04-09-0568;
RA   Chen Y.-L., Tsai I.-H., Hong T.-M., Tsai S.-H.;
RT   "Crotalid venom vascular endothelial growth factors has preferential
RT   affinity for VEGFR-1. Characterization of Protobothrops mucrosquamatus
RT   venom VEGF.";
RL   Thromb. Haemost. 93:331-338(2005).
CC   -!- FUNCTION: Activates the vascular endothelial growth factor receptor-1
CC       (VEGFR-1/FLT1), and consequently promotes the proliferation and tissue
CC       factor production of endothelial cells, the neovascularization in the
CC       chicken chorioallantoic membrane, and increases vascular permeability.
CC       Also stimulates tissue-factor production and human monocyte chemotaxis.
CC       {ECO:0000269|PubMed:15711751}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts with
CC       high affinity with VEGFR-1/FLT1, and with lower affinity with VEGFR-
CC       2/KDR. Does not bind to VEGFR-3/FLT4 and neuropilin-1 (NRP1).
CC       {ECO:0000250, ECO:0000269|PubMed:15711751}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15711751}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family. Snake venom
CC       VEGF subfamily. {ECO:0000305}.
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DR   EMBL; AY442328; AAS07632.1; -; mRNA.
DR   RefSeq; XP_015676137.1; XM_015820651.1.
DR   AlphaFoldDB; Q330K6; -.
DR   SMR; Q330K6; -.
DR   GeneID; 107291631; -.
DR   KEGG; pmur:107291631; -.
DR   OrthoDB; 1364454at2759; -.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
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"
FT   CHAIN           25..143
FT                   /note="Snake venom vascular endothelial growth factor
FT                   toxin"
FT                   /id="PRO_5000092370"
FT   REGION          117..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..136
FT                   /note="Basic and acidic residues"
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   143 AA;  15925 MW;  9A49F9F41A9AFACF CRC64;
     MAVYLLAVAI LFCIQGWPSG TVQGEVMPFM EVYDRSACQT REMLVPILKE YPNEVSHLFK
     PSCVPVLRCG GCCSDESLTC TATGKRSVGR EVMRVDPHKG TSKIEVMQFK EHTACECRPR
     SPGDVNDGRN PKEGEPRARF PFV