3SA2_NAJNI
ID 3SA2_NAJNI Reviewed; 60 AA.
AC P01463;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Cytotoxin 2;
DE AltName: Full=Toxin V(II)2;
OS Naja nivea (Cape cobra) (Coluber niveus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=8655;
RN [1]
RP PROTEIN SEQUENCE, TOXIC DOSE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=823968; DOI=10.1016/0005-2795(76)90091-x;
RA Botes D.P., Viljoen C.C.;
RT "The amino acid sequence of three non-curarimimetictoxins from Naja nivea
RT venom.";
RL Biochim. Biophys. Acta 446:1-9(1976).
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:823968}. Target cell
CC membrane {ECO:0000250|UniProtKB:P60301}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- TOXIC DOSE: LD(50) is 1.5 mg/kg by subcutaneous injection into mice.
CC {ECO:0000269|PubMed:823968}.
CC -!- MISCELLANEOUS: Shows very weak hemolytic activity.
CC {ECO:0000269|PubMed:823968}.
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; A01726; H3NJ2C.
DR AlphaFoldDB; P01463; -.
DR SMR; P01463; -.
DR PRIDE; P01463; -.
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:823968"
FT /id="PRO_0000093514"
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"
SQ SEQUENCE 60 AA; 6871 MW; 22558CC7BF8199C4 CRC64;
LKCHQLIPPF WKTCPEGKNL CYKMYMVATP MIPVKRGCID VCPKNSALVK YMCCNTDKCN
