3SA2_NAJHA
ID 3SA2_NAJHA Reviewed; 60 AA.
AC P01462;
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 2;
DE AltName: Full=Toxin V(II)2/V(II)2A;
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, TOXIC DOSE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=1213684; DOI=10.1515/bchm2.1975.356.2.1893;
RA Joubert F.J.;
RT "The amino acid sequence of toxin V II 2, a cytotoxin homologue from banded
RT Egyptian cobra (Naja haje annulifera) venom.";
RL Hoppe-Seyler's Z. Physiol. Chem. 356:1893-1900(1975).
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:1213684}. Target
CC cell membrane {ECO:0000250|UniProtKB:P60301}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- TOXIC DOSE: LD(50) is 1.98 mg/kg by intravenous injection.
CC {ECO:0000269|PubMed:1213684}.
CC -!- MISCELLANEOUS: The sequence of the major component is shown, it is
CC called toxin V(II)2 and the minor component is called toxin V(II)2A.
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; A01725; H3NJ2E.
DR AlphaFoldDB; P01462; -.
DR SMR; P01462; -.
DR PRIDE; P01462; -.
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 2"
FT /evidence="ECO:0000269|PubMed:1213684"
FT /id="PRO_0000093486"
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 toxin V(II)2A)"
FT VARIANT 55
FT /note="N -> S (in toxin V(II)2A)"
SQ SEQUENCE 60 AA; 6858 MW; 8A2A96DDBAC6C7B0 CRC64;
LKCHKLVPPF WKTCPEGKNL CYKMYMVATP MLPVKRGCID VCPKDSALVK YMCCNTDKCN
