3SA6_NAJHA
ID 3SA6_NAJHA Reviewed; 60 AA.
AC P01465;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Cytotoxin 6;
DE AltName: Full=Toxin CM-2H;
OS Naja annulifera (Banded Egyptian cobra) (Naja haje annulifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=96794;
RN [1]
RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND TOXIC DOSE.
RC TISSUE=Venom;
RX PubMed=838473; DOI=10.1515/bchm2.1977.358.1.79;
RA Joubert F.J.;
RT "Snake venom toxin. The amino acid sequence of three toxins (CM-2h, CM-4b
RT and CM-6) from Naja haje annulifera (Egyptian cobra) venom.";
RL Hoppe-Seyler's Z. Physiol. Chem. 358:79-96(1977).
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:0000269|PubMed:838473}. Target cell
CC membrane {ECO:0000250|UniProtKB:P60301}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- TOXIC DOSE: LD(50) is 5.09 mg/kg by subcutaneous injection.
CC {ECO:0000269|PubMed:838473}.
CC -!- MISCELLANEOUS: Is classified as a P-type cytotoxin, since a proline
CC residue stands at position 30 (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 PIR; B01727; H3NJ6E.
DR PIR; C01727; H3NJ6M.
DR AlphaFoldDB; P01465; -.
DR SMR; P01465; -.
DR PRIDE; P01465; -.
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 1: Evidence at protein level;
KW Cardiotoxin; Cytolysis; Direct protein sequencing; Disulfide bond;
KW Membrane; Secreted; Target cell membrane; Target membrane; Toxin.
FT CHAIN 1..60
FT /note="Cytotoxin 6"
FT /evidence="ECO:0000269|PubMed:838473"
FT /id="PRO_0000093490"
FT DISULFID 3..21
FT /evidence="ECO:0000250|UniProtKB:P60301"
FT DISULFID 14..38
FT /evidence="ECO:0000250|UniProtKB:P60301"
FT DISULFID 42..53
FT /evidence="ECO:0000250|UniProtKB:P60301"
FT DISULFID 54..59
FT /evidence="ECO:0000250|UniProtKB:P60301"
FT VARIANT 52
FT /note="M -> V (in minor component)"
FT VARIANT 55
FT /note="N -> S (in minor component)"
SQ SEQUENCE 60 AA; 6857 MW; 8A2A96D35AC6C7B0 CRC64;
LKCHKLVPPF WKTCPEGKNL CYKMYMVATP MLPVKRGCID VCPKDSALVK YMCCNTNKCN
