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TXVE_PROFL
ID   TXVE_PROFL              Reviewed;         146 AA.
AC   P67862; C0K3N6; Q68BI5; T2HPC7;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Snake venom vascular endothelial growth factor toxin;
DE            Short=svVEGF;
DE   AltName: Full=VEGF-F {ECO:0000303|PubMed:19208624};
DE   Flags: Precursor;
OS   Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX   NCBI_TaxID=88087;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, INTERACTION WITH FLT1 AND
RP   KDR, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom gland;
RX   PubMed=15328352; DOI=10.1074/jbc.m403687200;
RA   Takahashi H., Hattori S., Iwamatsu A., Takizawa H., Shibuya M.;
RT   "A novel snake venom vascular endothelial growth factor (VEGF)
RT   predominantly induces vascular permeability through preferential signaling
RT   via VEGF receptor-1.";
RL   J. Biol. Chem. 279:46304-46314(2004).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=24224955; DOI=10.1186/1471-2164-14-790;
RA   Aird S.D., Watanabe Y., Villar-Briones A., Roy M.C., Terada K.,
RA   Mikheyev A.S.;
RT   "Quantitative high-throughput profiling of snake venom gland transcriptomes
RT   and proteomes (Ovophis okinavensis and Protobothrops flavoviridis).";
RL   BMC Genomics 14:790-790(2013).
CC   -!- FUNCTION: Strongly increases vascular permeability, and weakly
CC       stimulates angiogenesis. Interacts with human VEGF receptor-1 (FLT1)
CC       with a high affinity, whereas it binds to human VEGF receptor-2 (KDR)
CC       with a low affinity. Stimulates autophosphorylation of VEGF receptor-1
CC       (VEGFR-1/FLT1), and VEGF receptor-2 (VEGFR-2/KDR).
CC       {ECO:0000269|PubMed:15328352}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with human VEGF
CC       receptor-1 (FLT1) with a high affinity, whereas it binds to human VEGF
CC       receptor-2 (KDR) with a low affinity. Does not bind VEGF receptor-3
CC       (FLT4). {ECO:0000269|PubMed:15328352}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15328352}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- MISCELLANEOUS: IC(50) to VEGF receptor-1 is 30 ng/ml and IC(50) to VEGF
CC       receptor-2 is 254 ng/ml.
CC   -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family. Snake venom
CC       VEGF subfamily. {ECO:0000305}.
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DR   EMBL; AB154417; BAD38844.1; -; mRNA.
DR   EMBL; FJ554640; ACN22043.1; -; Genomic_DNA.
DR   EMBL; AB848141; BAN82012.1; -; mRNA.
DR   EMBL; AB985235; BAP39960.1; -; mRNA.
DR   AlphaFoldDB; P67862; -.
DR   SMR; P67862; -.
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"
FT   CHAIN           25..146
FT                   /note="Snake venom vascular endothelial growth factor
FT                   toxin"
FT                   /id="PRO_0000023426"
FT   REGION          118..146
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:0000250|UniProtKB:P83942"
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   146 AA;  16152 MW;  8CB18BBD80973228 CRC64;
     MAAYLLAVAI LFCIQGWPSG TVQGQVMPFM EVYSRSACQT RETLVPILKE YPDEVSHLFK
     PSCVPVLRCG GCCSDESLTC TATGKHSVGR EIMRVDPHKG TSKMEVMQFK EHTACECRPR
     SPGDVNNGKD KRNPEEGGPR ARFPFV
 
 
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