ID   3SA0_NAJSP              Reviewed;          81 AA.
AC   Q02454;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Cytotoxin;
DE            Short=CTX;
DE   AltName: Full=Cardiotoxin;
DE   Flags: Precursor;
OS   Naja sputatrix (Malayan spitting cobra) (Naja naja sputatrix).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX   NCBI_TaxID=33626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=8446963; DOI=10.1016/0041-0101(93)90356-n;
RA   Yeo M.S., Jeyaseelan K., Chung M.C., Gopalakrishnakone P., Tan C.H.,
RA   Wong H.A.;
RT   "Molecular cloning of a cardiotoxin structural gene from Malayan spitting
RT   cobra (Naja naja sputatrix).";
RL   Toxicon 31:53-60(1993).
CC   -!- FUNCTION: Shows cytolytic activity on many different cells by forming
CC       pore in lipid membranes. In vivo, increases heart rate or kills the
CC       animal by cardiac arrest. In addition, it binds to heparin with high
CC       affinity, interacts with Kv channel-interacting protein 1 (KCNIP1) in a
CC       calcium-independent manner, and binds to integrin alpha-V/beta-3
CC       (ITGAV/ITGB3) with moderate affinity. {ECO:0000250|UniProtKB:P60301,
CC       ECO:0000250|UniProtKB:P60304}.
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:0000250}. Target cell membrane
CC       {ECO:0000250|UniProtKB:P60301}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- MISCELLANEOUS: Is classified as a P-type cytotoxin, since a proline
CC       residue stands at position 51 (Pro-31 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   EMBL; L04640; AAA49386.1; -; mRNA.
DR   PIR; A44335; A44335.
DR   AlphaFoldDB; Q02454; -.
DR   SMR; Q02454; -.
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   3: Inferred from homology;
KW   Cardiotoxin; Cytolysis; Disulfide bond; Membrane; Secreted; Signal;
KW   Target cell membrane; Target membrane; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..81
FT                   /note="Cytotoxin"
FT                   /id="PRO_0000035392"
FT   DISULFID        24..42
FT                   /evidence="ECO:0000250|UniProtKB:P60301"
FT   DISULFID        35..59
FT                   /evidence="ECO:0000250|UniProtKB:P60301"
FT   DISULFID        63..74
FT                   /evidence="ECO:0000250|UniProtKB:P60301"
FT   DISULFID        75..80
FT                   /evidence="ECO:0000250|UniProtKB:P60301"
SQ   SEQUENCE   81 AA;  9098 MW;  70E30F9AE4AFA697 CRC64;
     MKTLLLTTVV VTIVCLDLEY TLKCNKLVPL FYKTCPAGKN LCYKMFMVAT PKVPVKRGCI
     DVCPKSSLLV KYVCCNTDRC N