ID   3SA1_DABRR              Reviewed;          20 AA.
AC   P0C5H4;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Cytotoxin drCT-1;
DE   AltName: Full=drCT-I;
DE   Flags: Fragment;
OS   Daboia russelii (Russel's viper) (Vipera russelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Daboia.
OX   NCBI_TaxID=8707;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=17055549; DOI=10.1016/j.toxicon.2006.09.009;
RA   Gomes A., Choudhury S.R., Saha A., Mishra R., Giri B., Biswas A.K.,
RA   Debnath A., Gomes A.;
RT   "A heat stable protein toxin (drCT-I) from the Indian Viper (Daboia
RT   russelli russelli) venom having antiproliferative, cytotoxic and apoptotic
RT   activities.";
RL   Toxicon 49:46-56(2007).
RN   [2]
RP   CRYSTALLIZATION, FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=16511326; DOI=10.1107/s1744309106005963;
RA   Choudhury S.R., Gomes A., Gomes A., Dattagupta J.K., Sen U.;
RT   "Purification, crystallization and preliminary X-ray structural studies of
RT   a 7.2 kDa cytotoxin isolated from the venom of Daboia russelli russelli of
RT   the Viperidae family.";
RL   Acta Crystallogr. F 62:292-294(2006).
CC   -!- FUNCTION: This three-finger cytotoxin has antiproliferative, cytotoxic
CC       and apoptotic activities. Both in vivo and in vitro experimental
CC       results suggests that this protein possess anticancer potential. Also
CC       shows neurotoxicity, cardiotoxicity and myotoxicity.
CC       {ECO:0000269|PubMed:16511326, ECO:0000269|PubMed:17055549}.
CC   -!- SUBUNIT: Monomer in solution; Homodimer and oligomer in the presence of
CC       negatively charged lipids forming a pore with a size ranging between 20
CC       and 30 Angstroms. {ECO:0000250|UniProtKB:P60301}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16511326,
CC       ECO:0000269|PubMed:17055549}. Target cell membrane
CC       {ECO:0000250|UniProtKB:P60301}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain
CC       subfamily. Type IA cytotoxin sub-subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C5H4; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Apoptosis; Cardiotoxin; Cytolysis; Direct protein sequencing; Membrane;
KW   Myotoxin; Neurotoxin; Secreted; Target cell membrane; Target membrane;
KW   Toxin.
FT   CHAIN           1..>20
FT                   /note="Cytotoxin drCT-1"
FT                   /evidence="ECO:0000269|PubMed:17055549"
FT                   /id="PRO_0000306089"
FT   NON_TER         20
SQ   SEQUENCE   20 AA;  2251 MW;  1D75033D3ED5BE85 CRC64;
     LKCNKLVPLF YKTCPAGKNL