TXVE2_MACLB
ID TXVE2_MACLB Reviewed; 110 AA.
AC P82475;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 2.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Snake venom vascular endothelial growth factor toxin ICPP {ECO:0000303|PubMed:10652214};
DE Short=svVEGF;
DE AltName: Full=Increasing capillary permeability protein {ECO:0000303|PubMed:10652214};
DE AltName: Full=Increasing capillary-2 {ECO:0000303|PubMed:19695228};
DE Short=IC2 {ECO:0000303|PubMed:19695228};
DE AltName: Full=VEGF-F {ECO:0000250|UniProtKB:P0DL42};
OS Macrovipera lebetina (Levantine viper) (Vipera lebetina).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Macrovipera.
OX NCBI_TaxID=8709;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MASS
RP SPECTROMETRY, AND PYROGLUTAMATE FORMATION AT GLN-1.
RC TISSUE=Venom;
RX PubMed=12021274; DOI=10.1074/jbc.m202202200;
RA Gasmi A., Bourcier C., Aloui Z., Srairi N., Marchetti S., Gimond C.,
RA Wedge S.R., Hennequin L., Pouyssegur J.;
RT "Complete structure of an increasing capillary permeability protein (ICPP)
RT purified from Vipera lebetina venom. ICPP is angiogenic via vascular
RT endothelial growth factor receptor signalling.";
RL J. Biol. Chem. 277:29992-29998(2002).
RN [2]
RP PROTEIN SEQUENCE OF 1-28, SUBUNIT, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=10652214; DOI=10.1006/bbrc.2000.2078;
RA Gasmi A., Abidi F., Srairi N., Oijatayer A., Karoui H., Elayeb M.;
RT "Purification and characterization of a growth factor-like which increases
RT capillary permeability from Vipera lebetina venom.";
RL Biochem. Biophys. Res. Commun. 268:69-72(2000).
RN [3]
RP INTERACTION WITH KDR; NRP1 AND NRP2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=19695228; DOI=10.1016/j.bbrc.2009.08.068;
RA Aloui Z., Hoos S., Geretti E., Kharmachi H., Haumont P.Y., Mejdoub H.,
RA Klagsbrun M., England P., Gasmi A.;
RT "Novel svVEGF isoforms from Macrovipera lebetina venom interact with
RT neuropilins.";
RL Biochem. Biophys. Res. Commun. 389:10-15(2009).
CC -!- FUNCTION: Induces capillary permeability and angiogenesis through VEGF
CC receptor (KDR/VEGFR-2) signaling. Induces DNA synthesis in human
CC umbilical vein endothelial cells, and promotes mouse embryonic stem
CC cell proliferation and differentiation. {ECO:0000269|PubMed:12021274}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with high affinity with
CC KDR/VEGFR-2, and with a lower affinity with neuropilin-1 (NRP1) and
CC neuropilin-2 (NRP2). {ECO:0000269|PubMed:10652214,
CC ECO:0000269|PubMed:12021274, ECO:0000269|PubMed:19695228}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10652214,
CC ECO:0000269|PubMed:12021274}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:10652214, ECO:0000269|PubMed:12021274}.
CC -!- MASS SPECTROMETRY: Mass=25115; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12021274};
CC -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family. Snake venom
CC VEGF subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P82475; -.
DR SMR; P82475; -.
DR PRIDE; P82475; -.
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 ICPP"
FT /id="PRO_0000162365"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:12021274"
FT DISULFID 14..56
FT /evidence="ECO:0000250"
FT DISULFID 39
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 45..91
FT /evidence="ECO:0000250"
FT DISULFID 48
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 49..93
FT /evidence="ECO:0000250"
SQ SEQUENCE 110 AA; 12574 MW; B28D19F21FF75746 CRC64;
QVRPFPDVYQ RSACQARETL VSILQEYPDE ISDIFRPSCV AVLRCSGCCT DESLKCTPVG
KHTVDMQIMR VNPRTQSSKM EVMKFTEHTA CECRPRRKQG EPDGPKEKPR
