ID   3SA1_NAJKA              Reviewed;          60 AA.
AC   P0CH80;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Cytotoxin 1;
DE            Short=NK-CT1 {ECO:0000303|PubMed:20595038};
OS   Naja kaouthia (Monocled cobra) (Naja siamensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX   NCBI_TaxID=8649;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, TOXIC DOSE, IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=20595038; DOI=10.1016/j.toxicon.2010.05.016;
RA   Debnath A., Saha A., Gomes A., Biswas S., Chakrabarti P., Giri B.,
RA   Biswas A.K., Gupta S.D., Gomes A.;
RT   "A lethal cardiotoxic-cytotoxic protein from the Indian monocellate cobra
RT   (Naja kaouthia) venom.";
RL   Toxicon 56:569-579(2010).
CC   -!- FUNCTION: Produces complete blockade of auricular contraction, which is
CC       irreversible at high concentrations. Induces apoptosis in leukemic
CC       cells. Possesses anti-arthritic and anti-inflammatory potential.
CC       {ECO:0000269|PubMed:20595038}.
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:20595038}. Target
CC       cell membrane {ECO:0000250|UniProtKB:P60301}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- TOXIC DOSE: LD(50) is 2.5 mg/kg by intraperitoneal injection into mice.
CC       {ECO:0000269|PubMed:20595038}.
CC   -!- MISCELLANEOUS: Is classified as a S-type cytotoxin, since a serine
CC       residue stands at position 28 (Ser-29 in standard classification).
CC       {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; P0CH80; -.
DR   SMR; P0CH80; -.
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:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   CDD; cd00206; snake_toxin; 1.
DR   Gene3D; 2.10.60.10; -; 1.
DR   InterPro; IPR003572; Cytotoxin_Cobra.
DR   InterPro; IPR003571; Snake_3FTx.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   InterPro; IPR018354; Snake_toxin_con_site.
DR   PRINTS; PR00282; CYTOTOXIN.
DR   SUPFAM; SSF57302; SSF57302; 1.
DR   PROSITE; PS00272; SNAKE_TOXIN; 1.
PE   1: Evidence at protein level;
KW   Cardiotoxin; Cytolysis; Direct protein sequencing; Disulfide bond;
KW   Membrane; Secreted; Target cell membrane; Target membrane; Toxin.
FT   CHAIN           1..60
FT                   /note="Cytotoxin 1"
FT                   /evidence="ECO:0000269|PubMed:20595038"
FT                   /id="PRO_0000399989"
FT   DISULFID        3..21
FT                   /evidence="ECO:0000250|UniProtKB:P60301"
FT   DISULFID        14..38
FT                   /evidence="ECO:0000250|UniProtKB:P60301"
FT   DISULFID        42..53
FT                   /evidence="ECO:0000250|UniProtKB:P60301"
FT   DISULFID        54..59
FT                   /evidence="ECO:0000250|UniProtKB:P60301"
SQ   SEQUENCE   60 AA;  6807 MW;  6B0D5F91BE5D1E8F CRC64;
     LKCNKLVPLF YKTCPAGKNL CYKMFMVSNK TVPVKRGCID VCPKNSLVLK YVCCNTDRCN