ID   3SA7_NAJSP              Reviewed;          62 AA.
AC   O73859;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Cytotoxin 7;
DE   AltName: Full=Cardiotoxin-7;
DE            Short=CTX-7;
DE            Short=Ctx7;
DE   Flags: Precursor; Fragment;
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 [GENOMIC DNA].
RC   TISSUE=Liver;
RX   PubMed=9738945; DOI=10.1016/s0014-5793(98)00894-1;
RA   Lachumanan R., Armugam A., Tan C.H., Jeyaseelan K.;
RT   "Structure and organization of the cardiotoxin genes in Naja naja
RT   sputatrix.";
RL   FEBS Lett. 433:119-124(1998).
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 S-type cytotoxin, since a serine
CC       residue stands at position 30 (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   EMBL; AF064101; AAC61319.1; -; Genomic_DNA.
DR   AlphaFoldDB; O73859; -.
DR   SMR; O73859; -.
DR   PRIDE; O73859; -.
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..2
FT                   /evidence="ECO:0000250"
FT   CHAIN           3..62
FT                   /note="Cytotoxin 7"
FT                   /id="PRO_0000035403"
FT   DISULFID        5..23
FT                   /evidence="ECO:0000250|UniProtKB:P60301"
FT   DISULFID        16..40
FT                   /evidence="ECO:0000250|UniProtKB:P60301"
FT   DISULFID        44..55
FT                   /evidence="ECO:0000250|UniProtKB:P60301"
FT   DISULFID        56..61
FT                   /evidence="ECO:0000250|UniProtKB:P60301"
FT   NON_TER         1
SQ   SEQUENCE   62 AA;  7062 MW;  61937BDC54AC3EDB CRC64;
     YTLKCNKLVP LFYKTCPAGK NLCYKMFMMS NKTVPVKRGC IDVCPKNSAL VKYVCCNTDR
     CN