ID   3SAA_NAJAT              Reviewed;          82 AA.
AC   Q9W6W6;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Cytotoxin 10;
DE   AltName: Full=Cardiotoxin-10;
DE            Short=CTX10;
DE            Short=Ctx-10;
DE   Flags: Precursor;
OS   Naja atra (Chinese cobra).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX   NCBI_TaxID=8656;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   PubMed=15587986; DOI=10.1023/b:bigi.0000043955.35906.c2;
RA   Chang L.-S., Lin S.-K., Chung C.;
RT   "Molecular cloning and evolution of the genes encoding the precursors of
RT   taiwan cobra cardiotoxin and cardiotoxin-like basic protein.";
RL   Biochem. Genet. 42:429-440(2004).
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 52 (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; Y18957; CAB41507.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9W6W6; -.
DR   SMR; Q9W6W6; -.
DR   PRIDE; Q9W6W6; -.
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..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..82
FT                   /note="Cytotoxin 10"
FT                   /id="PRO_0000035387"
FT   DISULFID        25..43
FT                   /evidence="ECO:0000250|UniProtKB:P60301"
FT   DISULFID        36..60
FT                   /evidence="ECO:0000250|UniProtKB:P60301"
FT   DISULFID        64..75
FT                   /evidence="ECO:0000250|UniProtKB:P60301"
FT   DISULFID        76..81
FT                   /evidence="ECO:0000250|UniProtKB:P60301"
SQ   SEQUENCE   82 AA;  9087 MW;  865C19341300F722 CRC64;
     MKTLLLTLVV VVTIVCLDLG YTLKCNQHIP PFYKTCAAGK NLCYKIFMVA APKVPVKRGC
     IDVCPKSSDL VKYVCCNTDR CN