3SA8B_NAJAT
ID 3SA8B_NAJAT Reviewed; 81 AA.
AC Q91124;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Cytotoxin 8;
DE AltName: Full=Cardiotoxin VIII;
DE AltName: Full=Cardiotoxin-8;
DE Short=CTX8;
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;
RA Chu R.C., Yang C.-C.;
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
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; U42586; AAB01542.1; -; mRNA.
DR AlphaFoldDB; Q91124; -.
DR SMR; Q91124; -.
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..81
FT /note="Cytotoxin 8"
FT /id="PRO_0000035386"
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; 8900 MW; 9FECB4B99C0D5A48 CRC64;
MKTLLLTLVV VTIVCLDLGY TLKCNKLIPI ASKTCPAGKN LCYKMFMVAT PKVPVKRGCI
DVCPKSSLLV KYVCCNTDRC N