BENG_DECBE
ID BENG_DECBE Reviewed; 20 AA.
AC P0CC11;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 25-MAY-2022, entry version 20.
DE RecName: Full=Bengalin;
DE Flags: Fragment;
OS Deccanometrus bengalensis (Indian black scorpion) (Heterometrus
OS bengalensis).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Iurida; Scorpionoidea; Scorpionidae; Heterometrinae;
OC Deccanometrus.
OX NCBI_TaxID=696368;
RN [1]
RP PROTEIN SEQUENCE, AND FUNCTION.
RC TISSUE=Venom;
RX PubMed=19913524; DOI=10.1016/j.cbi.2009.11.006;
RA Gupta S.D., Gomes A., Debnath A., Saha A., Gomes A.;
RT "Apoptosis induction in human leukemic cells by a novel protein Bengalin,
RT isolated from Indian black scorpion venom: through mitochondrial pathway
RT and inhibition of heat shock proteins.";
RL Chem. Biol. Interact. 183:293-303(2010).
RN [2]
RP PROTEIN SEQUENCE, AND FUNCTION.
RC TISSUE=Venom;
RX PubMed=19800909; DOI=10.1016/j.toxicon.2009.09.013;
RA Haldar S., Das Gupta S., Gomes A., Giri B., Dasgupta S.C., Biswas A.,
RA Mishra R., Gomes A.;
RT "A high molecular weight protein Bengalin from the Indian black scorpion
RT (Heterometrus bengalensis C.L. Koch) venom having antiosteoporosis activity
RT in female albino rats.";
RL Toxicon 55:455-461(2010).
CC -!- FUNCTION: Toxin that shows cardiotoxicity on isolated guinea pig heart
CC and auricle and neurotoxicity on isolated rat phrenic nerve diaphragm.
CC Shows antiosteoporosis activity in experimental rats. Also induces
CC apoptosis against human leukemic cells (U937 and K562). Has no effect
CC on normal human lymphocytes. Apoptosis has been evidenced from damaged
CC nuclei, cell cycle arrest at sub G1 phase, increase of early apoptotic
CC cells, augmentation of DNA fragmentation and also a reduction of
CC telomerase activity. Also elicits loss of mitochondrial membrane
CC potential (MMP) which induces cytochrome c release in cytosol,
CC decreases heat shock protein (HSP) 70 and 90 expression, activates
CC caspase-9, caspase-3, induces poly (ADP-ribose) polymerase (PARP)
CC cleavage, and up-regulates caspase-3. {ECO:0000269|PubMed:19800909,
CC ECO:0000269|PubMed:19913524}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
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DR AlphaFoldDB; P0CC11; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR InterPro; IPR006146; 5'-Nucleotdase_CS.
PE 1: Evidence at protein level;
KW Apoptosis; Cardiotoxin; Cell cycle; Direct protein sequencing; Neurotoxin;
KW Secreted; Toxin.
FT CHAIN 1..>20
FT /note="Bengalin"
FT /id="PRO_0000390673"
FT UNSURE 14
FT /note="A or R"
FT UNSURE 17
FT /note="Q or G"
FT UNSURE 18
FT /note="F or G"
FT NON_TER 20
SQ SEQUENCE 20 AA; 2237 MW; 8F075286AB3FFBFB CRC64;
GPLTILHIND VHAAFEQFNT