ID   3SA6_NAJAT              Reviewed;          82 AA.
AC   Q98965;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Cytotoxin 6;
DE   AltName: Full=Cardiotoxin-6;
DE            Short=CTX6;
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 [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=9192088; DOI=10.1080/15216549700202461;
RA   Chang L.-S., Lin J., Wu P.-F.;
RT   "cDNA sequence analysis of cardiotoxin variants from Taiwan cobra.";
RL   Biochem. Mol. Biol. Int. 42:85-92(1997).
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   -!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain
CC       subfamily. Type IA cytotoxin sub-subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Y08727; CAA69977.1; -; mRNA.
DR   AlphaFoldDB; Q98965; -.
DR   SMR; Q98965; -.
DR   PRIDE; Q98965; -.
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   InterPro; IPR035076; Toxin/TOLIP.
DR   Pfam; PF00087; Toxin_TOLIP; 1.
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:0000250"
FT   CHAIN           22..82
FT                   /note="Cytotoxin 6"
FT                   /id="PRO_0000035381"
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   82 AA;  9201 MW;  4912FA608DABD307 CRC64;
     MKTLLLTLVV VTIVCLDLGY TLKCNQLIPP FYKTCAAGKN LCYKMFMVAA QRFPVKRGCI
     DVCPKSSLLV KYVCCNTDRC NN