3SA6_NAJSP
ID 3SA6_NAJSP Reviewed; 62 AA.
AC O73858;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Cytotoxin 6;
DE AltName: Full=Cardiotoxin-6;
DE Short=CTX-6;
DE Short=Ctx6;
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; AF064100; AAC61318.1; -; Genomic_DNA.
DR AlphaFoldDB; O73858; -.
DR SMR; O73858; -.
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 6"
FT /id="PRO_0000035402"
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; 7029 MW; 61866F8D04AC3EDB CRC64;
YTLKCNKLVP LFYKTCPAGK NLCYKMFMVS NKTVPVKRGC IDVCPKNSAL VKYVCCNTDR
CN